WO2025068117A1

WO2025068117A1 - Using protein deamidase in processes for obtaining a seed-based dairy alternative beverage with improved stability

Info

Publication number: WO2025068117A1
Application number: PCT/EP2024/076665
Authority: WO
Inventors: Hanne Vang Hendriksen; Zhen Long
Original assignee: Novozymes A/S
Priority date: 2023-09-26
Filing date: 2024-09-23
Publication date: 2025-04-03

Abstract

The present invention relates to the use of a protein deamidase for obtaining a seed-based dairy alternative beverage with improved stability.

Description

PROCESSES FOR OBTAINING A SEED-BASED DAIRY ALTERNATIVE BEVERAGE WITH IMPROVED STABILITY REFERENCE TO SEQUENCE LISTING This application contains a Sequence Listing in computer readable form. The computer readable form is incorporated herein by reference. FIELD OF THE INVENTION The present invention relates to novel processes comprising the use of a protein deamidase for obtaining a seed-based dairy alternative beverage with improved stability. BACKGROUND OF THE INVENTION The number of people pursuing a vegan, vegetarian, or non-dairy diet for health reasons has increased in recent years. Further, food products made from animals’ milk, such as cows’ milk, are increasingly recognized for their high environmental costs. These factors are leading to a greater demand for dairy alternative food products for foods traditionally derived from milk, including milk, cheese, and yogurt. One type of dairy alternative food products which has received great attention in recent years is the seed-based food products, such as, e.g., almond-based, pea- or soy-based beverages. Almond, pea and soy are nutritious and low in calories and some of the health benefits which have been associated with intake of these include weight loss, lower blood cholesterol levels, and reduced risk of heart disease. In addition, the seed-based beverages benefit from a pleasant flavor and a high fat and protein content relative to its carbohydrate content and, thus, these beverages do not cause a spike in blood sugar levels, making them a suitable choice of food product for people with diabetes, as well as people who are following a low carb diet. These factors have contributed to making seed-based beverages a popular alternative to animal-derived milks. Similar to other plant proteins, however, seed protein, such as almond protein or pea/soy protein, tends to suffer from poor dispersibility and stability and have been seen to agglomerate when subjected to heat and/or low pH conditions. This limits the use of the seed-based beverages in, e.g., acidic hot beverages, such as coffee drinks and tea drinks. Deamidation is known to improve the solubility of plant proteins whereby functional properties, such as foaming activity, foaming stability, emulsification activity and emulsification stability, may be improved. E.g. WO 2020/176469 A1 describes the use of protein glutaminase in the production of stable protein solution. To achieve a stable almond milk, a stabilizer (gellan gum) is required. Similarly, WO 2022/045152 A1 describes treatment of commercially available almond milk (Rude Health) with the protein glutaminase "Amano" 500 (Amano Enzyme), followed by heat-inactivating and cooling, before being mixed with a Nescafe decaf coffee solution having pH 5.2. The pH of the decaf coffee solution after addition of the almond milk was 5.8. All of the exemplified milks in WO 2022/045152 A1 are prepared at least by carrying out the deamidation reaction at 50°C for 5 hours. It is an object of the present invention to identify improved methods for producing dairy alternative beverages, in particular seed-based dairy alternative beverages, with improved techno-functional properties, such as, e.g., improved stability to heat and/or low pH. SUMMARY OF THE INVENTION The present inventors have surprisingly found that by treating a slurry of a seed material with a protein deamidase, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of seed material has a protein content of at least 3% (w/w), more protein is solubilized and a seed-based dairy alternative beverage is obtained which has improved dispersibility, reduced risk of flocculation and superior stability, in particular when mixed with an acidic beverage, such as a coffee drink or a tea drink. Also, using the methods as disclosed and claimed herein, a lower dosage of protein deamidase is needed to obtain the improved properties of the seed-based dairy alternative beverage. The invention therefore provides a method for obtaining a seed-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of seed material in water; (b) treating the slurry of seed material in water with a protein deamidase to obtain a slurry of enzymatically deamidated seed material; (c) optionally diluting the slurry of enzymatically deamidated seed material to obtain a diluted slurry of enzymatically deamidated seed material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated seed material to obtain the seed-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of step (a) has a protein content of at least 3% (w/w). The invention also provides a method for obtaining an almond-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of almond material in water; (b) treating the slurry of almond material in water with a protein deamidase to obtain a slurry of enzymatically deamidated almond material; (c) optionally diluting the slurry of enzymatically deamidated almond material to obtain a diluted slurry of enzymatically deamidated almond material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated almond material to obtain the almond-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of step (a) has a protein content of at least 3% (w/w). The methods of the invention enable producers of seed-based dairy alternative beverages, such as producers of almond- or legume-based beverages, to obtain beverages having superior stability and organoleptic properties. Examples of such products include almond- and pea/soy-based drinks for barista applications. Also, the improved dispersibility and stability of the seed-based dairy alternative beverages obtained according to the disclosed methods, can be realized at shorter enzyme incubation times and at lower enzyme incubation temperatures, thus, further allowing manufacturers to save time and energy.. The invention therefore also relates to a seed-based dairy alternative beverage obtainable by any of the methods disclosed herein. The improved stability of the seed-based dairy alternative beverage prepared using methods of the invention further avoids or reduce the need for adding emulsifiers and/or stabilizers during production of the beverages, and, thus, can also meet consumers’ requirements for clean-label dairy alternative beverages. The invention also relates to the use of a protein deamidase in the production of a seed- based dairy alternative beverage. In particular, the invention relates to the use of a protein deamidase in the production of an almond-based or pea/soy-based dairy alternative beverage to improve stability to heat and/or low pH, such as, e.g., to improve stability in acidic beverages. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1 illustrates stability of an almond-based beverage in filter coffee at room temperature after 2 minutes. Figure 2 illustrates stability of an almond-based beverage in filter coffee at room temperature after 50 minutes. Figure 3 illustrates stability of an almond-based beverage in filter coffee at room temperature after 2 minutes. Figure 4 illustrates stability of an almond-based beverage in filter coffee at room temperature after 3 minutes. Figure 5 illustrates stability of almond-based beverages in filter coffee at room temperature after 5 minutes. Figure 6 illustrates stability of almond-based beverages, prepared with enzyme incubation temperatures of 30°C and 60°C, in filter coffee at room temperature after 5 minutes. Figure 7 illustrates stability of almond-based beverages, prepared with enzyme incubation temperature of 30°C, in filter coffee at room temperature after 5 minutes. SEQUENCES SEQ ID NO: 1: Protein deamidase derived from Chryseobacterium viscerum (the strain has formerly been referred to as Chryseobacterium sp-62563) having the mature polypeptide sequence shown as SEQ ID NO: 2. SEQ ID NO: 2: Mature polypeptide sequence of protein deamidase derived from Chryseobacterium viscerum. SEQ ID NO: 3: Protein deamidase derived from Chryseobacterium proteolyticum having the mature polypeptide sequence shown as SEQ ID NO: 4. SEQ ID NO: 4: Mature polypeptide sequence of protein deamidase derived from Chryseobacterium proteolyticum. SEQ ID NO: 5: Protein deamidase derived from Chryseobacterium gambrini having the mature polypeptide sequence shown as SEQ ID NO: 6. SEQ ID NO: 6: Mature polypeptide sequence of protein deamidase derived from Chryseobacterium gambrini. SEQ ID NO: 7: Protein deamidase derived from Chryseobacterium culicis having the mature polypeptide sequence shown as SEQ ID NO: 8. SEQ ID NO: 8: Mature polypeptide sequence of protein deamidase derived from Chryseobacterium culicis. SEQ ID NO: 9: Protein deamidase derived from Chryseobacterium defluvii having the mature polypeptide sequence shown as SEQ ID NO: 10. SEQ ID NO: 10: Mature polypeptide sequence of protein deamidase derived from Chryseobacterium defluvii. DETAILED DESCRIPTION OF THE INVENTION In accordance with this detailed description, the following definitions apply. Note that the singular forms "a," "an," and "the" include plural references unless the context clearly dictates otherwise. As used herein, the terms “drink", “milk” and "beverage" are used interchangeably and have the same meaning unless defined otherwise or clearly indicated by context. Unless defined otherwise or clearly indicated by context, all percentages are percentage by weight (percent w/w or “% (w/w)”). Unless defined otherwise or clearly indicated by context, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. The term “dairy alternative beverage” refers to a food product which can be used as a substitute for a conventional dairy-based food product, such as, e.g., an animal-derived dairy beverage. The dairy alternative beverage according to the invention is a seed-based dairy alternative beverage. In the context of the invention, the term “seed” or “grain” or “bean” means the propagative structure of a plant and when used, e.g., to describe a “seed material” and “seed-based dairy alternative beverage”, means a source of food which can be ingested by humans and animals, including domesticated animals, such as, e.g., companion animals, in its unprocessed and/or processed form. In some embodiments, the seed material is obtained or derived from a nut. Examples of nuts include, but are not limited to, almonds, cashews, coconut, hazelnuts, macadamias, pistachios, peanuts, pecans, and walnuts. In some embodiments, the seed material is derived or obtained from a leguminous material. Examples of leguminous material include, but are not limited to, soy, pea, chickpea, mung bean, fava bean, lupin, and lentil. The seed-based dairy alternative beverage may or may not be combined with additional food ingredients to produce the seed-based dairy alternative beverage. The additional food ingredient which may be added to the seed-based dairy alternative beverage may be any food ingredient deemed useful by a practitioner of skill in the art. The additional food ingredient may be a solid or liquid ingredient. The additional food ingredient may or may not be plant-based. In some embodiments, the additional food ingredient is water. The additional food ingredients which may be added to the seed-based dairy alternative beverage, include, but are not limited to, e.g., lipids, such as oils, in particular plant oils, sugars, such as sucrose, proteins, various forms of synthetic amino acids, dietary fibres, salts, minerals, flavoring agents, vitamins, and any combination thereof. In an embodiment, lipid is added to the seed-based dairy alternative beverage and/or to the slurry of seed material. The lipid may be a plant oil or a mixture of plant oils. The lipid may be selected from rapeseed oil, flaxseed oil, safflower oil, soybean oil, olive oil, sunflower oil, palm oil and combinations thereof. In one embodiment, the lipid is rapeseed oil, sunflower oil or a combination thereof. The selection of suitable lipid may be selected based on the type of seed-based dairy alternative beverage desired. In an embodiment, sugar is added to the seed-based dairy alternative beverage and/or to the slurry of seed material. In one embodiment, the sugar is sucrose and/or fructose. In an embodiment, the additional food ingredient which may be added to the seed-based dairy alternative beverage and/or to the slurry of seed material is selected from the list of sodium chloride, dicalcium carbonate, dicalcium phosphate, tricalcium phosphate, calcium carbonate and any combination thereof. In a preferred embodiment, sodium chloride is added to the slurry of seed material. The person of skill in the art knows how to determine suitable amounts of the additional ingredient to add to the slurry of seed material and/or the seed-based dairy alternative beverage. In one embodiment, sodium chloride is used and in a concentration in the range of 0.05%-0.2% (w/w) based on, e.g., the dairy alternative beverage. In an embodiment, vitamins and/or minerals are added to the seed-based dairy alternative beverage. In another embodiment, vitamins and/or minerals are added to the slurry of seed material. The vitamins may be vitamin A, vitamin C, vitamin D, vitamin E, vitamin B12, thiamine (vitamin B1), riboflavin (vitamin B2), niacin (vitamin B3), vitamin B6, vitamin K, folic acid (vitamin B9, and mixtures thereof. The mineral may be calcium, phosphorous, magnesium, sodium, potassium, chloride, iron, zinc, iodine, selenium, copper and mixtures thereof. The seed-based dairy alternative beverage may be fortified with a plant-based dairy alternative powder, such as, e.g., a soymilk powder, or with concentrated or isolated protein, such as, e.g., a soy or pea protein isolate or a soy or pea protein concentrate. In an embodiment, the seed-based dairy alternative beverage is fortified, such as, e.g., an almond- based drink fortified with a pea protein or a soy protein. In an embodiment, the seed-based dairy alternative beverage is fortified with calcium carbonate (CaCO₃), such as an almond- based beverage fortified with CaCO₃. Also contemplated is a seed-based dairy alternative beverage fortified with both a concentrated or isolated protein and CaCO₃. Optionally, the fortified seed-based dairy alternative beverage may be further formulated with a stabilizer, such as, e.g., a gellan gum. In one embodiment, the seed-based dairy alternative beverage is an almond drink comprising CaCO₃ and gellan gum. In the context of the invention, fortification and formulation of the seed-based dairy alternative beverage is carried out after the methods claimed and disclosed herein, i.e. after the protein deamidase treatment, has been carried out. Thus, in embodiments of the invention, the treatment of the slurry of seed material in water with protein deamidase, the optional dilution and the heat treatment is carried out in the absence of added emulsifiers and/or stabilizers, and the thus obtained seed-based dairy alternative beverage is then fortified, e.g. with CaCO₃ and/or gellan gum. The seed material may be in the form of an aqueous solution or suspension of a seed- based dairy alternative powder. Or the seed material may be any other suitable preparation obtained from a seed, such as, e.g., an aqueous suspension of a flour or the like obtained from a seed. The seed material may be a combination of any of the above. Preferably, the seed-based dairy alternative beverage has a protein content of at least 0.5% (w/w). Preferably, the seed-based dairy alternative beverage has a protein content of at most 8% (w/w). In an embodiment, the seed-based dairy alternative beverage has a protein content of about 0.5% (w/w), 1% (w/w), 1.5% (w/w), 2% (w/w), 2.5% (w/w), 3% (w/w), 3.5% (w/w), or 4% (w/w). In a preferred embodiment, the seed-based dairy alternative beverage has a protein content of about 1% (w/w). Preferably, the seed-based dairy alternative beverage has a lipid content of at least 1% (w/w). Preferably, the seed-based dairy alternative beverage has a lipid content of at most 5% (w/w). The dairy alternative beverage may be standardized and/or homogenized. The dairy alternative beverage may be pasteurized or otherwise heat-treated. The dairy alternative beverage obtained according to the methods disclosed herein does not require the addition of emulsifiers and/or stabilizers to achieve its desirable properties. In particular, using the methods disclosed herein, a seed-based dairy alternative beverage, such as an almond-based beverage, can be obtained which is essentially free of added emulsifiers and/or stabilizers and still has improved stability, in particular improved stability to heat and/or low pH. In an embodiment, "essentially free of" means 0% (w/w). Thus, a seed-based dairy alternative beverage can be obtained which does not flocculate or precipitate even after longer storage or after being mixed with hot and/or acidic beverages, such as, e.g., a coffee drink or tea drink. As used herein, the terms “emulsifier” and “stabilizer” are meant as added emulsifiers and stabilizers, i.e., ingredients not naturally or inherently found in the material used for preparing the seed-based dairy alternative beverage. Examples of such emulsifiers and stabilizers include, but are not limited to, thickening agents, such as, e.g., carboxymethylcellulose, gellan gum, hydroxypropyl starch and agar, and emulsifiers, such as, e.g., monoglyceride and diglyceride. The seed-based dairy alternative beverage obtained in the methods of the invention has improved stability, including improved storage stability. Thus, the dairy alternative beverage may be subjected to storage before being consumed. The storage does not influence the properties of the dairy alternative beverage and it remains substantially free from precipitation and flocculation over time. In the context of the invention, the term “ storage stability” or “storage stable” when used to describe a seed-based dairy alternative beverage, such as, e.g., an almond-based beverage, means the resistance of the beverage to flocculation or precipitation, both immediately after its production and following long-term storage at storage conditions typical for consumer beverages and beverage additive products and after its combination with acidic beverages, such as coffee or tea drinks. The stability of the dairy alternative beverage may be determined by any method known in the art for evaluation of such, including by visual evaluation and taste testing. The seed-based dairy alternative beverage disclosed herein is largely unaffected by acidic (i.e. low pH) food matrices, such as coffee drinks or tea drinks. Thus, in one embodiment, the seed-based dairy alternative beverage is for use in an acidic beverage, such as a sports drink, a coffee drink or a tea drink. In a preferred embodiment, the seed-based dairy alternative beverage is an almond-based beverage which is suitable for use in barista applications, e.g., to prepare a coffee drink comprising coffee and the almond-based beverage. In another preferred embodiment, the seed-based dairy alternative beverage is a pea/soy-based beverage for use in barista applications. In the context of the invention, a “barista beverage” or “for use in barista applications” means a dairy alternative beverage suitable for mixing with acidic beverages and which may or may not comprise additional ingredients to create a beverage which produces a better foam, with high coherency for consistent pouring and the creation of latte art. Seed-based barista beverages may have more fat and/or more protein compared to standard seed-based dairy alternative beverages. Also contemplated is the use of the seed-based dairy alternative beverage according to the invention in obtaining ready-to-drink beverages. In the context of the invention, an “acid/acidic food matrix” or “acidic beverage” is meant as a sports drink, a coffee drink or a tea drink with a pH in the range of 3-6, such as a pH in the range of 4-6, such as a pH in the range of about 4.5-5.5, e.g., such as a pH in a range of about 4.8-5.1. For example, the acidic beverage may be a coffee having pH below 5.0. The acidic beverage may also be a tea beverage, such as tea beverage based on Chai tea blends, spiced tea blends, black teas, such as, e.g., Assam and Darjeeling black teas, green teas, earl grey, oolong tea, and rooibos tea. Such tea beverages may be used to prepare chai lattes. In an embodiment, the seed-based dairy alternative beverage is stable when added to an acidic beverage having a pH below 5.1. Such acidic beverage may for example be a filter coffee, an espresso drink or the like. Dairy alternative beverages include seed-based beverages, creamers, and the like. Examples of seed-based beverages include almond drinks, cashew drinks, chickpea drinks, coconut drinks, fava bean drinks, hazelnut drinks, lentil drinks, lupin drinks, macadamia drinks, mung bean drinks, pistachio drinks, pea drinks, peanut drinks, pecan drinks, soy drinks, walnut drinks, and drinks comprising any combination thereof. In an embodiment, the dairy alternative beverage is an almond drink, a pea drink, a soy drink or any combination thereof. In a preferred embodiment, the dairy alternative beverage is an almond-based drink. In another preferred embodiment, the dairy alternative beverage is a pea- or soy-based drink. The dairy alternative beverage of the invention is derived or obtained from a seed material, which is or is derived from the edible portions of a plant. In some embodiments, the seed material is derived or obtained from almond, cashew, chickpea, coconut, fava bean, hazelnut, macadamia, mung bean, lentil, lupin, pistachio, pea, peanut, pecan, soy, walnut, or any combination thereof. In a preferred embodiment, the seed material is obtained or derived from almond, pea, soy, or any combination thereof. In some embodiments, the seed material is heat treated. In some embodiments, the seed material is dehydrated. In some embodiments, the seed material is de-hulled, ground, wet milled, and/or dry milled. In some embodiments, the seed material is a flour, such as an almond flour, or a paste, such as an almond paste, or a combination of any thereof. In some embodiments, the seed material is smashed or ground to produce a paste, such as, e.g., an almond paste. In the methods of the invention, the seed material is suspended in water to provide a slurry of seed material and the thus obtained slurry of seed material in water is subjected to enzymatic treatment with a protein deamidase to obtain a slurry of enzymatically deamidated seed material. In the context of the invention, the term “enzymatically deamidated seed material” means a seed material treated with a protein deamidase for deamidation. A person skilled in the art will know of suitable analytical methods to determine enzymatic deamidation of a seed material. One such method is exemplified in Example 1 by the measurement of free ammonium content (NH₄). In one aspect of the invention, the slurry of seed material has a protein content of at least 3% (w/w), such as at least 3.5% (w/w), at least 4% (w/w), at least 4.5% (w/w), at least 5% (w/w), at least 5.5% (w/w), at least 6.5% (w/w), at least 7% (w/w), at least 7.5% (w/w), at least 8% (w/w), at least 8.5% (w/w), at least 9% (w/w), at least 9.5% (w/w) or at least 10% (w/w), during protein deamidase treatment. In preferred embodiments, the slurry of seed material has a protein content in the range of 4-20%, such as about 5-10% (w/w), such as, e.g., a protein content of about 5% (w/w), about 8% (w/w) or about 10% (w/w). In one embodiment, the slurry of seed material has a protein content of at least 5% (w/w) during protein deamidase treatment. In some embodiments, the slurry of enzymatically deamidated seed material is diluted to obtain a diluted slurry of enzymatically deamidated seed material which is heat treated to obtain the seed-based dairy alternative beverage. As used herein, a “diluted slurry of enzymatically deamidated seed material” means a suspension of enzymatically deamidated seed material having a protein content lower than 3% (w/w). The dilution may be obtained by adding a diluent deemed useful by a practitioner of skill in the art. Examples of diluents to use in the methods of the invention includes, but are not limited to, aqueous solutions, such as, e.g., a water, a plant- based dairy alternative drink or a combination thereof. In one embodiment, water is used to dilute the slurry of enzymatically deamidated seed material. In one embodiment, the diluted slurry of enzymatically deamidated seed material has a protein content of at most 2.5% (w/w). In preferred embodiments, the protein content of the diluted slurry of enzymatically deamidated seed material is in the range of 0.1-2.5% (w/w), preferably in the range of 0.5-2% (w/w), more preferably in the range of 1-2% (w/w). In a preferred embodiment, the diluted slurry of enzymatically deamidated seed material has a protein content of about 1% (w/w). In some embodiments, the diluted slurry of enzymatically deamidated seed material has a protein content of about 2.5% (w/w), wherein the seed material is derived or obtained from pea, soy or a combination thereof. In other embodiments, the diluted slurry of enzymatically deamidated seed material has a protein content of about 1.5% (w/w), wherein the seed material is derived or obtained from almond. In an embodiment, a method for obtaining an almond-based dairy alternative beverage is provided, the method comprising the steps of: (a) providing a slurry of almond material in water having a protein content of at least 3% (w/w); (b) treating the slurry of almond material in water with a protein deamidase to obtain a slurry of enzymatically deamidated almond material; (c) diluting the slurry of enzymatically deamidated almond material to obtain a diluted slurry of enzymatically deamidated almond material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated almond material to obtain the almond-based dairy alternative beverage. The inventors have surprisingly found that by treating a slurry of seed material having a protein content of at least 3% (w/w), such as, e.g., a protein content of about 5%, 8% or 10% (w/w), with a protein deamidase followed by diluting to, e.g., a 1% protein content before heat- treatment, e.g. to inactivate the protein deamidase, a seed-based dairy alternative beverage is obtained which when used as a dairy alternative beverage has improved or increased stability towards heat and/or low pH. This has been experimentally confirmed (see Examples 2-5), in that, e.g., an almond-based dairy alternative beverage was obtained which, when prepared according to the methods disclosed herein, had improved stability when mixed with a warm filter coffee drink, both immediately at mixing and after 1 hour. In a preferred embodiment, a method for obtaining a seed-based dairy alternative beverage is provided, which method comprises the steps of: (a) providing a slurry of seed material in water having a protein content 5-20% (w/w); (b) treating the slurry of seed material in water with a protein deamidase to obtain a slurry of enzymatically deamidated seed material; (c) diluting the slurry of enzymatically deamidated seed material to obtain a diluted slurry of enzymatically deamidated seed material having a protein content of 1-2.5% (w/w), such as 1-2% (w/w) ; and (d) heat treating the diluted slurry of enzymatically deamidated seed material to obtain the seed-based dairy alternative beverage. In some embodiments, the methods of the invention further comprise the steps of: (e) separating the seed-based dairy alternative beverage into solid and liquid streams; (f) harvesting the liquid stream as a liquid seed-based dairy alternative beverage; and (g) optionally inactivating the protein deamidase. The inventors have found that for the legume-based substrates, such as, e.g. pea or soy material, the step of diluting the slurry of enzymatically deamidated leguminous material to obtain a diluted slurry of enzymatically deamidated leguminous material can be optionally performed. Thus, the invention provides a method for obtaining a legume-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of leguminous material in water having a protein content of at least 3% (w/w); (b) treating the slurry of leguminous material in water with a protein deamidase to obtain a slurry of enzymatically deamidated leguminous material; (c) optionally, diluting the slurry of enzymatically deamidated leguminous material to obtain a diluted slurry of enzymatically deamidated leguminous material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated leguminous material to obtain the legume-based dairy alternative beverage, wherein the leguminous material is derived or obtained from soy, pea, chickpea, mung bean, fava bean, lupin, lentil, or any combination thereof, preferably soy and/or pea. In a preferred embodiment, the slurry of leguminous material in water of step (a) has a protein content of at least 6% (w/w), even more preferred at least 8% (w/w), such as at least 9% (w/w). In another aspect of the invention, the enzymatic treatment with protein deamidase is in the presence of a chloride salt. In the context of the invention, the term “chloride salt” has the conventional meaning in the art and includes chloride salts relevant for food applications. In preferred embodiments, the chloride salt is selected from potassium chloride and sodium chloride. In preferred embodiments, the chloride salt is sodium chloride. Without wishing to be bound by any particular theory, the inventors believe that the presence of a chloride salt during the treatment of the seed material with the protein deamidase, facilitate the enzymatic deamidation of the proteins in the seed material, while at the same time stabilizing the enzyme and proteins in the slurry. Thus, an embodiment of the invention relates to the use of a protein deamidase and a chloride salt in the production of a seed-based dairy alternative beverage to improve stability and deamidation rate. In the context of the invention, "deamidation rate" refers to the speed or frequency at which the deamidation of the protein in the seed material occurs when incubated with a protein deamidase. The deamidation rate can be evaluated based on the amount of ammonium and/or soluble protein present in the deamidase treated slurry of seed material. Preferably, the amount of chloride salt is at least 0.05% (w/w) based on the slurry of seed material in water. Preferably, the amount of chloride salt is at most 2% (w/w) based on the slurry of seed material in water. In preferred embodiments, the chloride salt is in an amount of 0.10% (w/w) or 0.15% (w/w) based on the slurry of seed material in water. In a preferred embodiment, the chloride salt is sodium chloride and the amount of sodium chloride is about 0.10-0.15% (w/w) based on the slurry of seed material in water. The present inventors have found that by treating a slurry of a seed material in water with a protein deamidase in the presence of a chloride salt, such as sodium chloride and/or potassium chloride, a seed-based dairy alternative beverage, in particular a nut-based beverage, can be obtained, such beverage having not only more solubilized protein, but also improved dispersibility and stability when mixed with acidic beverages, such as coffee or tea drinks. This has been experimentally confirmed (see Example 5), in that, e.g., an almond-based dairy alternative beverage was obtained which, when prepared according to the methods disclosed herein, had improved stability when mixed with a warm filter coffee drink. In the context of the invention, what is meant with stability to heat and/or low pH is that the seed-based dairy alternative beverage can maintain its stability and integrity when exposed to elevated temperatures and pH in the acidic range, as might occur when mixing with a warm acidic beverage, such as, e.g., a coffee drink. A "low pH" in the context of this invention typically refers to a pH value less than 7, preferably less than 5, which signifies an acidic condition. Preferably, the stability of the seed-based dairy alternative beverage is at a pH of less than 5. For example, the maintained stability and integrity of the seed-based dairy alternative beverage can be seen by the beverage not forming any precipitation or flocculation when mixed with warm acidic beverages. Thus, the seed-based dairy alternative beverage of the invention is resistant to flocculation and precipitation in warm, acidic beverages. When the enzymatic deamidation of the seed material is performed in the presence of a chloride salt, it is possible to perform the enzymatic treatment on substrates with lower protein contents, such as, e.g., a protein content of 1% (w/w). Also, a lower dosage of protein deamidase, compared to processes in which no chloride salts are used during enzyme incubation, can be used, thus, significantly reducing costs of manufacturing. The addition of a chloride salt during the enzyme treatment, particularly the protein deamidase treatment, may further preclude the need for additional steps of formulation of the seed-based dairy alternative beverage, thus, further optimizing the overall processes of obtaining the final beverages intended for consumers. In some embodiments, the invention therefore provides a method for obtaining a seed- based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of seed material in water; and (b) treating the slurry of seed material in water with a protein deamidase to obtain the seed-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt. In preferred embodiments, the seed material treated with the protein deamidase in the presence of chloride salt, is derived or obtained from a nut, preferably from almond. The protein deamidase used to treat the slurry of seed material in water is held at a temperature in the range of 10-80°C, such as in the range of 20-65°C so that the seed material is enzymatically deamidated by the protein deamidase to produce an enzymatically deamidated seed material. In some embodiments, the slurry is held at a temperature between 15-40°C, 25- 40°C, 30-45°C, 35-50°C, 40-55°C, 50-60°C, or 50-65°C. In further embodiments, the slurry is held at a temperature of about 20°C, about 25°C, about 30°C, about 35°C, about 40°C, about 45°C, about 50°C, about 55°C, or about 60°C. In some embodiments, the slurry comprising the added protein deamidase is held at 10- 80°C, such as at 20-65°C, for at least 10 minutes to allow for enzymatic deamidation of the seed material. In some embodiments, the slurry is held for about 10, about 15, about 20, about 25, about 30, about 60, about 120, about 180, or about 240 minutes to allow for enzymatic deamidation of the seed material. In some embodiments, the slurry is held for at least about 10, 30, 60, or 90 minutes. In some embodiments, the slurry is held for 30 minutes. In some embodiments, the slurry is held for 60 minutes. In some embodiments, the slurry is held at 50- 60°C for about 30-60 minutes. In some embodiments, a lipid is added to the slurry. The lipid may be added before, during or after the treatment with the protein deamidase. In one embodiment, the lipid is added before the slurry is treated with protein deamidase. In one embodiment, the lipid is added after the slurry has been treated with protein deamidase. The lipid may be selected from rapeseed oil, flaxseed oil, safflower oil, flaxseed oil, soybean oil, olive oil, sunflower oil, palm oil and combinations thereof. In one embodiment, the lipid is a soybean oil. The method used, including temperature ranges, pH and the length of enzymatic treatment, will vary depending on the seed material and the enzyme added to the slurry. The skilled person will know how to determine the best process parameters based on the seed material and enzymes used. Preferably, the pH is in the range of pH 5-8 during treatment of the slurry of seed material with protein deamidase. After the enzymatic deamidation of the seed material, the protein deamidase may be inactivated. The enzyme may be inactivated at any step after hydrolysis. In some embodiments, the enzyme is inactivated by a heat treatment. In some embodiments, the heat treatment is 85- 95°C for 5-30 minutes. In further embodiments, the heat treatment is 85-95°C for 10 minutes. In some embodiments, the heat treatment is 90°C for 5, 10, 15, 20, 25, or 30 minutes. In some embodiments, the enzyme is inactivated by an Ultra High Temperature (UHT) treatment. The UHT treatment may be direct or indirect. In some embodiments, the UHT treatment is 135-154°C for 1-10 seconds. In further embodiments, the UHT treatment is 140- 150°C for 3, 4, 5, 6, 7, 8, 9, or 10 seconds. In further embodiments, the UHT treatment is 140- 145°C for 3, 4, 5, 6, 7, 8, 9, or 10 seconds. In some embodiments, the UHT treatment is 143°C for 4, 5, 6, 7, or 8 seconds. After the optional enzyme inactivation, the slurry of enzymatically deamidated seed material may be cooled. The enzymatically deamidated seed material may be used directly to obtain the seed-based dairy alternative beverage or it may be separated into a solid and a liquid stream, for example by centrifugation. Centrifugation may occur in a decanter centrifuge. Following centrifugation, the liquid stream may be harvested or collected and used as the aqueous solution comprising enzymatically deamidated seed material. The liquid stream may still comprise some solid matter. In some embodiments, the liquid stream comprises 1-80% solids. In further embodiments, the liquid stream comprises 1-10%, 5-20%, 10-25%, 20-35%, 25-40%, 30-45%, 35-50%, 40-55%, 45-60%, 50-65%, 55-70%, 60-75%, or 65-80% solids. In some embodiments, the liquid stream comprises 10-15% solids. In some embodiments, the liquid stream is further processed to remove water, also referred to as concentrated. Concentration also increases the relative amounts of solids in the concentrated liquid stream. In some embodiments, water removal will concentrate the products of the enzymatic treatment. Concentration may occur by evaporation of the water in the liquid stream. In some embodiments, the concentrated liquid stream comprises 10-100% solids. In further embodiments, the concentrated liquid stream comprises 10-20%, 20-30%, 30-40%, 40- 50%, 50-60%, 60-70%, 70-80%, 80%-90%, or 90-100% solids. In some embodiments, water removal will increase the viscosity of the dairy alternative beverage. In some embodiments, the liquid stream is used directly as a liquid seed-based dairy alternative beverage. Additional food ingredients may be added to the liquid stream to produce the dairy alternative beverage. In some embodiments, the liquid stream is derived from almond, pea or soy material. For example, an almond-, pea- or soy-derived liquid stream may be formulated using for instance sodium chloride (NaCl), sugars and flavoring agents. Also, the liquid stream may be formulated using for instance calcium carbonate, protein, sugars and flavoring agents. It may be homogenized. It may be UHT or ESL treated and aseptically packed. The final product may be sold as a seed-based dairy alternative beverage, such as an almond- based beverage, a pea-based beverage or a soy-based beverage. The slurry of seed material may be subjected to further processing, such as, e.g., treatment with further enzymes, including, e.g., further modifying or hydrolyzing enzymes. Thus, in some embodiment, the slurry of seed material is further treated with one or more hydrolyzing enzymes selected from the group of pectinases, hemicellulases, xylanases, beta-glucanases, mannanases, glucanases, glucoamylases, iso-amylases, alpha-amylases, beta-amylases, and mixtures thereof. In some embodiments, the further modifying or hydrolyzing enzymes are added together with the protein deamidase and the enzymatic treatment is carried out simultaneously. In other embodiments, the modifying or hydrolyzing enzymes are added before or after the protein deamidase and the enzymatic treatments are performed in separate steps of the method. The enzymes used in the methods of the invention may be added to the slurry comprising the seed material in any suitable form, such as in the form of a liquid, in particular a stabilized liquid, or it may be added as a substantially dry powder or granulate. Granulates may be produced, e.g., as disclosed in US Patent No. 4,106,991 and US Patent No. 4,661,452. Liquid enzyme preparations may, for instance, be stabilized by adding a sugar or sugar alcohol or lactic acid according to established procedures. Other enzyme stabilizers are well-known in the art. Additionally, the enzymes may be added to the slurry comprising the seed material in any suitable manner, such as individual components (separate or sequential addition of the enzymes) or addition of the enzymes together in one step or in one composition. Protein deamidase In the methods of the invention, a seed material is treated with a protein deamidase to obtain an enzymatically deamidated seed material. In preferred embodiments of the methods of the invention, a seed material derived or obtained from almond is treated with a protein deamidase to obtain an enzymatically deamidated almond material. In one aspect of the invention, the enzymatic deamidation is carried out using a protein deamidase in the presence of a chloride salt, preferably in the presence of sodium chloride. In the present invention, a protein deamidase refers to an enzyme having an effect of directly acting on an amide group of a side chain of an amino acid that constitutes a protein to cause deamidation and release ammonia without cleaving a peptide bond of the protein and without crosslinking the protein. The term “deamidase” means a protein-glutamine glutaminase (also known as glutaminylpeptide glutaminase) activity, as described in EC 3.5.1.44, which catalyzes the hydrolysis of the gamma-amide of glutamine substituted at the carboxyl position or both the alpha-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L- glutaminylglycine. Thus, deamidases can deamidate glutamine residues in proteins to glutamate residues and are also referred to as protein glutamine deamidase. Deamidases comprise a Cys-His-Asp catalytic triad (e.g., Cys-156, His-197, and Asp-217, as shown in Hashizume et al. “Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex”, Journal of Biological Chemistry, vol. 286, no. 44, pp. 38691– 38702) and belong to the InterPro entry IPR041325. Deamidase may also include a protein asparaginase that directly acts on an amide group of a side chain of an asparagine residue contained in a protein to release ammonia and thus converts the asparagine residue into an aspartate residue. In the present invention, as a protein deamidase, any one of the protein glutaminase and the protein asparaginase can be used, or both can be used in combination. One example of the protein deamidase used in the present invention is a protein glutaminase. A protein deamidase to be used in a method of the present invention may be obtained from microorganisms of any genus. For purposes of the present invention, the term “obtained from” as used herein in connection with a given source shall mean that the polypeptide encoded by a polynucleotide is produced by the source or by a strain in which the polynucleotide from the source has been inserted. In one embodiment, the polypeptide obtained from a given source is secreted extracellularly. The protein deamidase may be obtained from a microorganism by use of any suitable technique. For instance, an enzyme preparation may be obtained by fermentation of a suitable microorganism and subsequent isolation of a protein deamidase preparation from the resulting fermented broth or microorganism by methods known in the art. The protein deamidase may also be obtained by use of recombinant DNA techniques. Such method normally comprises cultivation of a host cell transformed with a recombinant DNA vector comprising a DNA sequence encoding the protein deamidase and the DNA sequence being operationally linked with an appropriate expression signal such that it is capable of expressing the enzyme in a culture medium under conditions permitting the expression of the enzyme and recovering the enzyme from the culture. The DNA sequence may also be incorporated into the genome of the host cell. The DNA sequence may be of genomic, cDNA or synthetic origin or any combinations of these, and may be isolated or synthesized in accordance with methods known in the art. The protein deamidase may be purified. The term "purified" as used herein covers protein deamidase enzyme protein essentially free from insoluble components from the production organism. The term "purified" also covers protein deamidase enzyme protein essentially free from insoluble com-ponents from the native organism from which it is obtained. Preferably, it is also separated from some of the soluble components of the organism and culture medium from which it is derived. More preferably, it is separated by one or more of the unit operations: filtration, precipitation, or chromatography. The types or origins of the protein deamidase used in the present invention are not particularly limited. Examples of the protein deamidase includes protein deamidases derived from Chryseobacterium genus, Flavobacterium genus, Empedobacter genus, Sphingobacterium genus, Aureobacterium genus, or Myroides genus. The protein deamidase may be derived from any of the sources mentioned herein. The term “derived” means in this context that the enzyme may have been isolated from an organism where it is present natively, i.e. the amino acid sequence of the protein deamidase is identical to a native polypeptide. The term “derived” also means that the enzyme may have been produced recombinantly in a host organism, the recombinantly produced enzyme having either an amino acid sequence which is identical to a native enzyme or having a modified amino acid sequence, e.g. having one or more amino acids which are deleted, inserted and/or substituted, i.e. a recombinantly produced enzyme which is a mutant of a native amino acid sequence. Within the meaning of a native enzyme are included natural variants. Furthermore, the term “derived” includes enzymes produced synthetically by, e.g., peptide synthesis. The term “derived” also encompasses enzymes which have been modified e.g. by glycosylation, phosphorylation etc., whether in vivo or in vitro. With respect to recombinantly produced enzymes the term “derived from” refers to the identity of the enzyme and not the identity of the host organism in which it is produced recombinantly. In some embodiments, the protein deamidase may be derived from Chryseobacterium genus, such as Chryseobacterium viscerum, C. gambrini, C. culicis, C. defluvii, or C. proteolyticum. In some embodiments, the deamidase in the methods of the invention is derived from or obtained from Chryseobacterium viscerum. EP1839491 discloses cloning of a protein glutaminase from Chryseobacterium proteolyticum expressed in Corynebacterium glutamicum. Deamidases are also commercially available, e.g., protein glutaminases derived from Chryseobacterium genus, for example, "Amano PG500” (manufactured by Amano Enzyme Inc.). For example, protein deamidases can be obtained from a culture broth of the above- described microorganisms. Protein deamidases are produced by microbial cells in an inactive proform, which comprises a propeptide domain tightly bound to a deamidase domain. The proform is expressed as a fusion protein, which has reduced deamidase activity to protect the viability of the host cell. In nature, the fusion protein is post-processed to remove the propeptide and release the active deamidase outside of the host cell. However, in recombinant expression systems, the fusion protein is secreted outside of the host cell as an inactive proform comprising the propeptide. The propeptide may then be enzymatically cleaved off to separate it from the mature deamidase. The protein deamidases of the methods and compositions of the present invention are mature deamidases where the propeptide has been removed. In some embodiments, the propeptide was cleaved enzymatically by an endopeptidase. In some embodiments, the propeptide may still be present in the composition comprising the mature deamidase. The recombinant, mature protein deamidases used in the methods of the invention comprises the polypeptide of SEQ ID NOs: 2, 4, 6, 8, and 10. Each mature protein deamidase is derived from a deamidase proform polypeptide, which comprises the polypeptide of SEQ ID NO: 1, 3, 5, 7, and 9, respectively. The proform polypeptide comprises a propeptide at the N-terminal end, fused to a deamidase which is the same as that of the polypeptide of SEQ ID NOs: 2, 4, 6, 8, or 10. The propeptide may be enzymatically cleaved from the proform polypeptide to release the mature deamidase. Naturally occurring propeptide sequences are provided in the proform polypeptide. The methods and compositions of the invention include a mature deamidase and optionally a second polypeptide which is derived from the propeptide of a deamidase. The second polypeptides described herein are mutated variants of the naturally occurring propeptides. These variant propeptide sequences have been found to bind less strongly to their corresponding deamidase, so that they are more easily enzymatically cleaved off after recombinant expression and secretion from of the host cell. The polypeptides of SEQ ID NOs: 1 to 10 are derived from Chryseobacterium spp. and are described in PCT application PCT/EP2023/055936; filed March 8, 2023, herein incorporated by reference. After expression of the proform polypeptide in a recombinant expression system, a site- specific endopeptidase is used to cleave off the propeptide, leaving an active, mature deamidase. In some embodiments, the cleaved propeptide is not purified away from the mature deamidase. Therefore, the propeptide may be present in the composition with the mature deamidase. According to a preferred embodiment the protein deamidase applied in the process of the invention is derived from or obtained from a Chryseobacterium species, e.g., Chryseobacterium proteolyticum or Chryseobacterium viscerum. In the context of the present invention, the term “mature polypeptide” means a polypeptide in its mature form following N terminal processing (e.g., removal of signal peptide). A "signal peptide" is a sequence of amino acids attached to the N-terminal portion of a protein, which facilitates the secretion of the protein outside the cell. The mature form of an extracellular protein lacks the signal peptide, which is cleaved off during the secretion process. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NO: 2. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NO: 4. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NO: 6. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NO: 8. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NO: 10. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to a mature polypeptide of SEQ ID NO: 1. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to a mature polypeptide of SEQ ID NO: 3. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to a mature polypeptide of SEQ ID NO: 5. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to a mature polypeptide of SEQ ID NO: 7. In one embodiment the deamidase is selected from a polypeptide having at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to a mature polypeptide of SEQ ID NO: 9. For purposes of the present invention, the sequence identity between two amino acid sequences is determined as the output of “longest identity” using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle pro-gram of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet.16: 276-277), preferably version 6.6.0 or later. The parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix. In order for the Needle program to report the longest identity, the -nobrief option must be specified in the command line. The output of Needle labelled “longest identity” is calculated as follows: (Identical Residues x 100)/(Length of Alignment – Total Number of Gaps in Alignment) In the context of the present invention, the term “variant” means a polypeptide having enzymatic activity comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions. A substitution means replacement of the amino acid occupying a position with a different amino acid; a deletion means removal of the amino acid occupying a position; and an insertion means adding one or more (e.g., several) amino acids, e.g., 1-5 amino acids, adjacent to and immediately following the amino acid occupying a position. The amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding domain. Examples of conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine). Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R. L. Hill, 1979, In, The Proteins, Academic Press, New York. Common substitutions are Ala/Ser, Val/Ile, Asp/Glu, Thr/Ser, Ala/Gly, Ala/Thr, Ser/Asn, Ala/Val, Ser/Gly, Tyr/Phe, Ala/Pro, Lys/Arg, Asp/Asn, Leu/Ile, Leu/Val, Ala/Glu, and Asp/Gly. Alternatively, the amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered. For example, amino acid changes may affect the thermal stability of the polypeptide, alter the substrate specificity, change the pH optimum, and the like. Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis or alanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are intr0oduced at every residue in the molecule, and the resultant mutant molecules are tested for enzymatic activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem.271: 4699-4708. The active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labelling, in conjunction with mutation of putative contact site amino acids. See, for ex-ample, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64. The identity of essential amino acids can also be inferred from an alignment with a related polypeptide. Single or multiple amino acid substitutions, deletions, and/or insertions can be made and tested using known methods of mutagenesis, recombination, and/or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241: 53-57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95/17413; or WO 95/22625. Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991, Biochemistry 30: 10832-10837; U.S. Patent No.5,223,409; WO 92/06204), and region-directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner et al., 1988, DNA 7: 127). Mutagenesis/shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules that encode active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide. A protein deamidase to be used in the methods of the invention may be added at a concentration of 0.01-20 IPA(U)/g substrate protein, such as 0.1-15 IPA(U)/g substrate protein, 0.5-10 IPA(U)/g substrate protein. In some embodiments, the protein deamidase to be used in the methods of the invention is added at a concentration in the range of 2.0-6.5 IPA(U)/g substrate protein, such as 2.5-5 IPA(U)/g substrate protein. In preferred embodiments, the dosage of protein deamidase used in the methods of the invention is less than if the same method was used but without the addition of chloride salt, preferably sodium chloride, during the step of enzymatic treatment with protein deamidase. In another preferred embodiment, the dosage of protein deamidase used in the methods of the invention is less than if the same method was used but wherein the slurry of seed material in water does not have a protein content of at least 3%(w/w). Without wishing to be bound by any particular theory, the inventors believe that the addition of a chloride salt, in particular a sodium chloride, during protein deamidase treatment and/or the use of high protein content slurries (>3% (w/w)), not only results in improved deamidation of the slurry of seed material, but also enables obtaining a seed-based dairy alternative beverage which has improved stability to heat and low pH, in particular improved stability in warm acidic beverages, such as coffee drinks. Deamidase (protein glutaminase) activity was measured using the assay described in Example 1. The activity assay consists of two separate de-coupled parts: (1) an enzymatic step wherein ammonia is formed by the catalytic action of the protein deamidase; and (2) a non- enzymatic detection step, wherein the ammonia formed in step (1) is derivatized to a blue indophenol compound with an absorption maximum at 630 nm. The amount of enzyme producing 1 μmol ammonia per minute at 37°C is defined as 1 unit (given in Indophenol Assay Unit: IPA(U)). The activity may be determined relative to a standard of declared strength. The enzymes dosage will depend on parameters such as the temperature, the incubation time and the dairy alternative recipe. The skilled person will know how to determine the optimal enzyme dosage. Without wishing to be bound by any particular theory, the inventors believe that use of protein deamidase to yield an enzymatically deamidated seed material for use in the production of seed-based dairy alternative beverages contribute to the superior benefits reported herein, including, but not limited to, an improved stability of seed-based dairy alternative beverages to heat and/or low pH. The invention is further defined by the following numbered embodiments: Embodiment 1. A method for obtaining a seed-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of seed material in water; (b) treating the slurry of seed material in water with a protein deamidase to obtain a slurry of enzymatically deamidated seed material; (c) optionally diluting the slurry of enzymatically deamidated seed material to obtain a diluted slurry of enzymatically deamidated seed material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated seed material to obtain the seed-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of step (a) has a protein content of at least 3% (w/w). Embodiment 2. Method of embodiment 1, wherein the treatment of step (b) is carried out at a temperature in the range of 10-80°C, such as in the range of 10-65°C, 25-40°C, 30-45°C, 35-50°C, 40-55°C, 50-65°C or 50-60°C. Embodiment 3. Method of any of the preceding embodiments, wherein the treatment of step (b) is carried out at a temperature in the range of 20-60°C, such as in the range of 50- 60°C. Embodiment 4. Method of any of the preceding embodiments, wherein the treatment of step (b) lasts for at least 10 minutes, at least 30 minutes or at least 60 minutes. Embodiment 5. Method of any of the preceding embodiments, wherein the treatment of step (b) is carried out for 15-90 minutes, such as for 30-60 minutes. Embodiment 6. Method of any of the preceding embodiments, wherein the treatment of step (b) is carried out at 50-60°C for 30-60 minutes. Embodiment 7. Method of any of the preceding embodiments, wherein the chloride salt is selected from potassium chloride and sodium chloride. Embodiment 8. Method of any of the preceding embodiments, wherein the chloride salt is sodium chloride. Embodiment 9. Method of any of the preceding embodiments, wherein the chloride salt is in an amount of 0.05-2% chloride salt (w/w) based on the slurry, preferably in an amount of 0.07-0.2% (w/w) based on the slurry, such as about 0.10% (w/w) or about 0.15% (w/w) based on the slurry. Embodiment 10. Method of any of the preceding embodiments, wherein the chloride salt is in an amount of 0.1-0.15% chloride salt (w/w) based on the slurry. Embodiment 11. Method of any of the preceding embodiments, wherein the slurry of seed material in water has a protein content in the range of 0.1-3% (w/w), such as in the range of 0.1-2.5% (w/w), 0.5-1.5% (w/w) or 1-2% (w/w), such as about 1% (w/w). Embodiment 12. Method of any of embodiments 1-10, wherein the slurry of seed material in water has a protein content in the range of 4-20% (w/w), preferably in the range of 5- 15% (w/w), more preferably in the range of 5-10% (w/w), and the diluted slurry of enzymatically deamidated seed material has a protein content of at most 2.5% (w/w), preferably wherein the protein content of the diluted slurry of enzymatically deamidated seed material is in the range of 0.1-2.5% (w/w), such as in the range of 0.5-2% (w/w), such as in the range of 1-2% (w/w), such as about 1% (w/w). Embodiment 13. Method of any of the preceding embodiments, further comprising the addition of a lipid during step (a) or (b), or after step (b), optionally wherein the slurry or dairy alternative beverage has a lipid content of 1-5 % (w/w). Embodiment 14. Method of embodiment 13, wherein the lipid content is 3% (w/w). Embodiment 15. Method of any of embodiments 13 or 14, wherein the lipid is an oil, such as a plant oil selected from the group of rapeseed oil, sunflower oil, or a mixture thereof. Embodiment 16. Method of any of the preceding embodiments, wherein a stabilizer and/or emulsifier is not present during steps (a), (b), (c) and/or (d). Embodiment 17. Method of any of the preceding embodiments, wherein a stabilizer and/or emulsifier is not present during any of steps (a), (b), (c) and (d). Embodiment 18. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage is essentially free of added emulsifiers and/or stabilizers. Embodiment 19. Method of any of the preceding embodiments, wherein the diluted slurry of enzymatically deamidated seed material is obtained by diluting the slurry of enzymatically deamidated seed material with an aqueous suspension, such as, e.g., a water, a plant-based dairy alternative drink or a combination thereof. Embodiment 20. Method of any of the preceding embodiments, wherein the seed material is obtained or derived from almond, cashew, chickpea, coconut, fava bean, hazelnut, lentil, lupin, macadamia, mung bean, pistachio, pea, peanut, pecan, soy, walnut or any combination thereof. Embodiment 21. Method of any of the preceding embodiments, wherein the seed material is obtained or derived from almond, pea, soy, or any combination thereof. Embodiment 22. Method of any of the preceding embodiments, wherein the seed material is obtained or derived from almond. Embodiment 23. Method of any of embodiments 1-21, wherein the seed material is obtained or derived from pea, soy or a combination thereof. Embodiment 24. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage is an almond drink, a cashew drink, a chickpea drink, a coconut drink, a fava bean drink, a hazelnut drink, a lentil drink, a lupin drink, a macadamia drink, a mung bean drink, a pistachio drink, a pea drink, a peanut drink, a pecan drink, a soy drink, a walnut drink, or any combination thereof. Embodiment 25. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage an almond drink, a pea drink, a soy drink, or any combination thereof. Embodiment 26. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage is an almond drink. Embodiment 27. Method of any of embodiments 1-25, wherein the seed-based dairy alternative beverage is a pea- or soy-based drink. Embodiment 28. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage is for use in an acidic beverage, such as a sports drink, a coffee drink or a tea drink, preferably a coffee drink. Embodiment 29. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage is for use in barista applications and/or for ready-to-drink beverages. Embodiment 30. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage comprises one or more additional food ingredients selected from the group of lipids, sugars, proteins, vitamins, minerals, amino acids, flavoring agents, dietary fibres, salts, water, and any combinations thereof. Embodiment 31. Method of embodiment 30, wherein the additional food ingredient is a lipid, such as an oil, preferably a plant oil, and/or a sugar, such as a sucrose, and/or calcium carbonate. Embodiment 32. Method of any of the preceding embodiments, further comprising the steps of: (e) separating the seed-based dairy alternative beverage into solid and liquid streams; (f) harvesting the liquid stream as a liquid seed-based dairy alternative beverage; and (g) optionally inactivating the protein deamidase. Embodiment 33. Method of any of the preceding embodiments, wherein the protein deamidase is inactivated by a heat treatment, such as an Ultra-High Temperature (UHT) treatment. Embodiment 34. Method of any of the preceding embodiment, wherein the protein deamidase is derived from or obtained from a Chryseobacterium species, such as from Chryseobacterium proteolyticum or Chryseobacterium viscerum. Embodiment 35. Method of any of the preceding embodiments, wherein the protein deamidase comprises a polynucleotide sequence with at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NOs: 2, 4, 6, 8, or 10. Embodiment 36. Method of any of the preceding embodiments, wherein the protein deamidase comprises the polynucleotide sequence of SEQ ID NOs: 2, 4, 6, 8, or 10. Embodiment 37. Method of any of the preceding embodiments, wherein the seed material is further modified by treatment with further modifying and/or hydrolyzing enzymes. Embodiment 38. Method of any of the preceding embodiments, wherein the seed-based dairy alternative beverage has an increased stability to heat and/or low pH compared to a seed- based dairy alternative beverage obtained using the same method but without a protein deamidase, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of step (a) has a protein content of at least 3% (w/w). Embodiment 39. Method of any of the preceding embodiments, wherein a lower dosage of protein deamidase is used compared to when the same method is used but the protein deamidase treatment is in the absence of a chloride salt and/or the slurry of step (a) does not have a protein content of at least 3% (w/w). Embodiment 40. Seed-based dairy alternative beverage obtainable by a method of any of the preceding embodiments. Embodiment 41. Seed-based dairy alternative beverage of embodiment 40 characterized by having improved stability to heat and/or low pH compared to a seed-based dairy alternative beverage obtained using the same method but without a protein deamidase. Embodiment 42. Seed-based dairy alternative beverage of embodiment 40 characterized by having improved stability to heat and/or low pH compared to a seed-based dairy alternative beverage obtained using the same method but without a protein deamidase and a chloride salt. Embodiment 43. Seed-based dairy alternative beverage of any of embodiments 40-42 for use in an acidic beverage, such as a sports drink, a coffee drink or a tea drink, preferably a coffee drink. Embodiment 44. Seed-based dairy alternative beverage of any of embodiments 40-43 for use in barista applications or in a ready-to-drink beverage. Embodiment 45. Seed-based dairy alternative beverage of any of embodiments 40-44, further comprising a protein deamidase. Embodiment 46. Seed-based dairy alternative beverage of any of embodiments 40-45, wherein the protein deamidase comprises a polypeptide sequence with at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NOs: 2, 4, 6, 8, or 10. Embodiment 47. Seed-based dairy alternative beverage of any of embodiments 40-46, further comprising a chloride salt, preferably wherein the chloride salt is sodium chloride. Embodiment 48. Use of a protein deamidase in the production of a seed-based dairy alternative beverage to improve stability. Embodiment 49. Use according to embodiment 48, wherein the improved stability is improved stability to stability to heat and/or low pH. Embodiment 50. Use according to any of embodiments 48-49, wherein the seed-based dairy alternative beverage is obtained using a method as embodied in any of embodiments 1- 39. Embodiment 51. Use according to any of embodiments 48-50, wherein the protein deamidase comprises a polypeptide sequence with at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or at least 99% sequence identity to SEQ ID NOs: 2, 4, 6, 8, or 10. Embodiment 52. Use according to any of embodiments 48-51, wherein the seed-based dairy alternative beverage is an almond-based beverage, a pea-based beverage, a soy-based beverage, or a drink comprising any combination thereof, preferably an almond-based beverage, a pea-based beverage or a soy-based beverage for barista applications. Embodiment 53. Use according to any of embodiments 48-52, wherein the seed-based dairy alternative beverage has improved stability to heat and/or low pH compared to a seed- based dairy alternative beverage obtained without the use of a protein deamidase. Embodiment 54. Use of a protein deamidase and a chloride salt in the production of a seed-based dairy alternative beverage to improve stability. Embodiment 55. Use according to embodiment 54, wherein the improved stability is improved stability to stability to heat and/or low pH. Embodiment 56. Use of a protein deamidase and a chloride salt in the production of a seed-based dairy alternative beverage to improve stability and/or deamidation degree. Embodiment 57. Use according to any of embodiments 54-56, wherein the chloride salt is selected from potassium chloride and sodium chloride, preferably wherein the chloride salt is sodium chloride. Embodiment 58. Use according to any of embodiments 54-57, wherein the amount of chloride salt in the seed-based dairy alternative beverage is 0.05-2% chloride salt (w/w), preferably 0.07-0.2% (w/w). Embodiment 59. Use according to any of embodiments 54-58, wherein the amount of chloride salt in the seed-based dairy alternative beverage is about 0.10% (w/w) or about 0.15% (w/w). Embodiment 60. Use according to any of embodiments 54-59, wherein the seed-based dairy alternative beverage is obtained using a method as embodied in any of embodiments 1- 39. Embodiment 61. Use according to any of embodiment 54-60, wherein the seed-based dairy alternative beverage has improved stability to heat and/or low pH compared to a seed- based dairy alternative beverage obtained without the use of a protein deamidase and a chloride salt. Embodiment 62. Use according to any of embodiments 54-61, wherein the seed-based dairy alternative beverage is an almond drink, a pea drink, a soy drink, or any combination thereof. Embodiment 63. Use according to any of embodiments 54-62, wherein the seed-based dairy alternative beverage is an almond drink. Embodiment 64. A method for obtaining a seed-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of seed material in water having a protein content of at least 3% (w/w); (b) treating the slurry of seed material in water with a protein deamidase to obtain a slurry of enzymatically deamidated seed material; (c) diluting the slurry of enzymatically deamidated seed material to obtain a diluted slurry of enzymatically deamidated seed material; and (d) heat treating the diluted slurry of enzymatically deamidated seed material to obtain the seed-based dairy alternative beverage. Embodiment 65. Method of the preceding embodiment, further comprising the addition of chloride salt during step (a) and/or (b). Embodiment 66. Method of the preceding embodiment, wherein the chloride salt is selected from potassium chloride and sodium chloride, preferably wherein the chloride salt is sodium chloride. Embodiment 67. Method of any of embodiments 65-66, wherein the concentration of chloride salt is in the range of 0.05%-0.2% (w/w), such as about 0.10% (w/w) or about 0.15% (w/w), based on the seed-based dairy alternative beverage. Embodiment 68. Method of any of embodiments 64-67, wherein the diluted slurry of enzymatically deamidated seed material has a protein content of at most 2.5% (w/w). Embodiment 69. Method of any of embodiments 64-68, wherein the protein content of the diluted slurry of enzymatically deamidated seed material is in the range of 0.1-2.5% (w/w). Embodiment 70. Method of any of embodiments 64-69, wherein the protein content of the diluted slurry of enzymatically deamidated seed material is in the range of 0.5-2% (w/w). Embodiment 71. Method of any of embodiments 64-79, wherein the protein content of the diluted slurry of enzymatically deamidated seed material is in the range of 1-2%, such as about 1% (w/w). Embodiment 72. Method of any of embodiments 64-71, wherein the protein content of the slurry of enzymatically deamidated seed material is in the range of 4-20% (w/w). Embodiment 73. Method of any of embodiments 64-72, wherein the protein content of the slurry of enzymatically deamidated seed material is in the range of 5-15% (w/w). Embodiment 74. Method of any of embodiments 64-73, wherein the protein content of the slurry of enzymatically deamidated seed material is in the range of 5-10% (w/w), such as about 5%, 8% or 10% (w/w). Embodiment 75. Method of any of embodiments 64-74, wherein the seed material is ob- tained or derived from almond, cashew, chickpea, coconut, fava bean, hazelnut, lentil, lupin, macadamia, mung bean, pistachio, pea, peanut, pecan, soy, walnut, or any combination there- of. Embodiment 76. Method of any of embodiments 64-75, wherein the seed material is ob- tained or derived from almond, pea, soy, or any combination thereof. Embodiment 77. Method for obtaining an almond-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of almond material in water having a protein content of at least 3% (w/w); (b) treating the slurry of almond material in water with a protein deamidase to obtain a slurry of enzymatically deamidated almond material; (c) diluting the slurry of enzymatically deamidated almond material to obtain a diluted slurry of enzymatically deamidated almond material; and (d) heat treating the diluted slurry of enzymatically deamidated almond material to obtain the almond-based dairy alternative beverage. Embodiment 78. Method of embodiment 77, wherein the protein content of the diluted slurry of enzymatically deamidated almond material is in the range of 0.1-2.5% (w/w), preferably in the range of 0.5-2% (w/w), more preferably in the range of 1-2% (w/w), most preferably about 1% (w/w). Embodiment 79. Method of any of embodiments 77-78, wherein the protein content of the diluted slurry of enzymatically deamidated almond material is in the range of 1-2% (w/w), such as about 1% (w/w). Embodiment 80. Method of any of embodiments 77-79, wherein the protein content of the slurry of enzymatically deamidated almond material is 4-20% (w/w), preferably in the range of 5-15% (w/w), more preferably in the range of 5-10% (w/w). Embodiment 81. Method of any of embodiments 77-80, wherein the protein content of the slurry of enzymatically deamidated almond material is in the range of 5-10% (w/w), such as about 5%, 8% or 10% (w/w). Embodiment 82. A method for obtaining a legume-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of leguminous material in water having a protein content of at least 3% (w/w); (b) treating the slurry of leguminous material in water with a protein deamidase to obtain a slurry of enzymatically deamidated leguminous material; (c) optionally diluting the slurry of enzymatically deamidated leguminous material to obtain an optionally diluted slurry of enzymatically deamidated leguminous material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated leguminous material to obtain the legume-based dairy alternative beverage. Embodiment 83. A method for obtaining a legume-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of leguminous material in water having a protein content of at least 3% (w/w); (b) treating the slurry of leguminous material in water with a protein deamidase to obtain a slurry of enzymatically deamidated leguminous material; (c) diluting the slurry of enzymatically deamidated leguminous material to obtain a diluted slurry of enzymatically deamidated leguminous material; and (d) heat treating the diluted slurry of enzymatically deamidated leguminous material to obtain the legume-based dairy alternative beverage. Embodiment 84. Method of embodiment 82 or 83, wherein the protein content of the slurry of leguminous material in water is in the range of 5-10% (w/w), such as about 5%, 8% or 10% (w/w). Embodiment 85. Method of any of embodiments 82-84, wherein the protein content of the diluted slurry of enzymatically deamidated almond material is in the range of 0.1-2.5% (w/w). Embodiment 86. Method of any of embodiments 82-85, wherein the leguminous material is derived or obtained from pea, soy or a combination thereof. Embodiment 87. A method for obtaining a seed-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of seed material in water; (b) treating the slurry of seed material in water with a protein deamidase to obtain a slurry of enzymatically deamidated seed material, wherein the treatment with the protein deamidase is in the presence of a chloride salt. Embodiment 88. Method of the preceding embodiment, wherein the seed-based dairy alternative beverage has an improved stability to heat and/or low pH compared to a seed-based dairy alternative beverage obtained using a similar method but without a protein deamidase and a chloride salt. Embodiment 89. Method of any of embodiments 87-88, wherein the treatment in step (b) is performed using a lower enzyme dosage of protein deamidase compared to when the same method is used without the addition of a chloride salt in step (b). Embodiment 90. Method of any of embodiments 87-89, wherein the seed-based dairy alternative beverage is an almond drink. Embodiment 91. Method of any of embodiments 87-90, wherein the chloride salt is selected from potassium chloride and sodium chloride, preferably sodium chloride. Embodiment 92. Method of any of embodiments 87-91, wherein the chloride salt is in an amount of 0.05-2% chloride salt (w/w) based on the slurry, preferably in an amount of 0.07-0.2% (w/w) based on the slurry, such as 0.10% (w/w) or 0.15% (w/w) based on the slurry. Embodiment 93. Method of any of embodiments 87-92, wherein the slurry of seed material in water has a protein content in the range of 0.1-3% (w/w), such as in the range of 0.5- 2% (w/w), such as about 1% (w/w) or 1.5% (w/w). Embodiment 94. Method of any of embodiments 87-93, wherein the treatment in step (b) is carried out at a temperature in the range of 10-65°C, such as in the range of 15-40°C, such as 20-30°C. Embodiment 95. Method of any of embodiments 87-94, wherein the treatment in step (b) is carried out at a temperature in the range of 50-65°C. Embodiment 96. Method of any of embodiments 87-95, wherein the treatment of step (b) is carried out for at least 10 minutes, preferably for 15-90 minutes, such as for 30-60 minutes. Embodiment 97. Method for obtaining an almond-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of almond material in water; and (b) treating the slurry of almond material in water with a protein deamidase to obtain the almond-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt. Embodiment 98. Method of embodiment 97, wherein the chloride salt is selected from potassium chloride and sodium chloride, preferably sodium chloride. Embodiment 99. Method of any of embodiments 97-98, wherein the chloride salt is in an amount of 0.05-2% chloride salt (w/w) based on the slurry, preferably in an amount of 0.07-0.2% (w/w) based on the slurry, such as 0.10% (w/w) or 0.15% (w/w) based on the slurry. Embodiment 100. Method of any of embodiments 97-99, wherein the slurry of almond material in water has a protein content in the range of 0.1-3% (w/w), such as in the range of 0.5- 2% (w/w), such as about 1% (w/w) or 1.5% (w/w). The invention described and claimed herein is not to be limited in scope by the specific embodiments herein disclosed, since these embodiments are intended as illustrations of several aspects of the invention. Any equivalent embodiments are intended to be within the scope of this invention as well as combinations of one or more of the embodiments. Various references are cited herein, the disclosures of which are incorporated by reference in their entireties. The present invention is further described by the following examples which should not be construed as limiting the scope of the invention. EXAMPLES Materials Enzymes The following enzymes are used throughout the examples: Protein deamidase: Protein glutaminase derived from Chryseobacterium sp-62563 having the mature polypeptide sequence shown as SEQ ID NO: 2. Cleavage of the propeptide was achieved by treating the deamidase of SEQ ID NO: 1 with a site-specific endopeptidase. The site-specific endopeptidase used was a glutamyl endopeptidase from Bacillus licheniformis. The resulting active deamidase after maturation was the polypeptide shown in SEQ ID NO: 2. The Chryseobacterium sp-62563 strain was isolated from a soil sample collected in Sibhult, Sweden in September 2013. Example 1: Protein deamidase activity assay The protein deamidase activity assay consists of two separate de-coupled parts: 1) An enzymatic step wherein ammonia is formed by the catalytic action of the protein deamidase; and 2) A non-enzymatic detection step wherein the ammonia formed in step (1) is derivatized to a blue indophenol compound with an absorption maximum at 630 nm. In step (1), the ammonia is developed by the deamidating action of the protein deamidase. In step (2), the generated ammonia reacts with phenol to form dioxyphenylamine under alkaline conditions. The reaction is catalyzed by sodium pentacyanonitrosylferrate(III) (sodium nitroprusside). “Color Reagent solution A” contains phenol and sodium nitroprusside. “Color Reagent Solution B” provides alkaline reaction conditions. The intermediate is then oxidized by addition of sodium hypochlorite (“Color Reagent Solution C”) to form indophenol blue. This compound absorbs visible light at 630 nm. The enzyme activity is then calculated using a standard curve. Assay Procedure: Step (1) Enzymatic step with ammonia formation Reagents: Assay dilution solution: 0.2 M Na-phosphate buffer, 0.01% Triton X-100, pH 6.5. Assay buffer: Same as above. Used to prepare stock solution and diluted sample of protein deamidase (referred to in the following as “enzyme”). Substrate solution: 30 mM Z-Gln-Gly (Merck C6154-1G) in assay dilution solution (check pH after dissolution). Stop solution: 0.4M TCA. Standard: NH₄Cl (Ammonium Standard for IC, Merck 59755-100ML, 1000 mg/L NH₄ ⁺ in water) diluted in assay dilution solution (see also “Standard curve” section). Dissolve/dilute enzyme product in assay buffer and prepare suitable dilution resulting in a linear assay response. Incubation: 1. Add 10 μL of diluted enzyme samples in triplicates to the wells of a 96-well microtiter plate (MTP). 2. Add 100 μL of substrate solution to each well. 3. For blank samples add 100 μL 0.4M TCA solution. 4. Seal the plate using transparent plate sealer. 5. Incubate the plate for 10 minutes at 37°C, 500 rpm, on a thermomixer equipped with a lid heating function. 6. To stop the reaction, carefully add 100 μL 0.4M TCA solution (except for the blank samples, which already contain TCA). Total reaction volume: 210 μL Step (2) Ammonia detection step Reagents: Color reagent A: 4% (w/v) Phenol, 0.015% (w/v) sodium pentacyanonitrosylferrate(III) dihydrate (sodium nitroprusside) (Na₂[Fe(CN)₅NO]∙2H₂O). Color reagent B: 5% (w/v) Potassium hydroxide. Color reagent C: 28% (w/v) Potassium carbonate, 6% (v/v) sodium hypo-chlorite (Sigma- Aldrich 239305-25ml, < 5% available Cl₂). Incubation: 1. Transfer 15 μL from each well from step (1) into a new 96-well MTP. 2. Transfer 45 μL Milli-Q water to each well. 3. To each well, add 30μL of color reagent B (on lab table, shake gently by hand to mix). 4. To each well, add 60μL of color reagent A (on lab table, shake gently by hand to mix). 5. To each well, add 60μL of color reagent C (on lab table, shake gently by hand to mix). 6. Color development: Carefully seal the plate and leave it on lab table for 30 minutes. 7. Carefully transfer the MTP to a plate reader and measure absorbance at 630 nm. Total reaction volume: 210 μL Standard curve: Standard stock solution: 1000 mg NH₄ ⁺/L. The standard curve is prepared by adding dilutions of the ammonium standard in the assay dilution buffer in the ammonia detection step. That is, mixing 15 μL diluted ammonia standard with 45 μL water and then adding the color reagents in the order given above; B, A, and C. The amount of enzyme producing 1 μmol ammonia per minute at 37°C is defined as 1 unit Unit; IPA(U)):

where • ^^^^ _{^^^^ ^^^^4+} is the ammonia concentration in the reaction solution derived from the ammonium standard curve (i.e., taking into account the dilution of the prediluted ammonium standard solution in the ammonia derivatization step). • 18.04 is the molecular mass of ammonium used for the standard solution. • ^^^^ _{^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^} is the reaction volume in the well when ammonia is generated (210 μL). • ^^^^ _{^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^} is the volume of enzyme solution added to the well when ammonia is generated (10 μL). • ^^^^ _{^^^^ ^^^^3} ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ ^^^^ is the reaction volume in the well when ammonia is detected (210 μL). Example 2: Testing protein deamidase in production of almond beverages at 1, 2.5, 5, and 10% protein Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in water (deionized) to final protein concentrations of 1%, 2.5%, 5% or 10% and mixed in a Thermomixer. Protein deamidase was added in concentrations of 0, 2.7, or 4 IPA(U)/g protein and the mix was held at 60°C for 1 hour. After incubation, samples at 1% protein were heat- treated for enzyme inactivation directly at 90°C for 15 min, while samples at 2.5%, 5% or 10% protein were split and either heat-treated directly or diluted to 1% protein before heat-treatment (90°C/15 min). Samples were then homogenized using an Ultra-turrax at 14,000 rpm for 1 min to produce the final beverage samples. Beverage stability, soluble protein, viscosity and stability of the final beverage in coffee were then measured. Soluble protein was measured in the supernatant of the beverage sample after centrifugation at 21,000g for 10 min. Protein determination was done using a LECO analyzer (Dumas determination of nitrogen after combustion, reduction and detection of N2 using a conductivity detector). Protein factor was 5.18. Viscosity was measured using an Anton Paar Modular Compact Rheometer, MCR 302. For this, 21 g beverage sample was weighed into cups and placed in the measuring cell (C- ETD160/ST-SN81248612, paddle: ST24-2D/2V/2V-30-SN29679. Analysis was run at 20°C using the “low viscosity” program. Stability of the beverages were evaluated visually. Stability of the beverage samples in coffee was assessed using warm filter coffee (pH ~ 4.95-5.01, temp: 58-63°C), mixing 4 parts of coffee with 1 part cold beverage sample, leaving the mix for 5-10 min, and evaluating curdling/precipitate visually. Results: All blank beverage samples (no enzyme; See Figures 1-4, samples marked “0 U” indicate no protein deamidase added) were unstable showing a creaming layer in the top, sedimentation at the bottom and a clearer, not turbid middle layer. All samples with enzyme were more stable having a creaming layer in the top, no/little sediment, and a milky middle layer with colloidal stable protein. Samples heat-treated at more than 1% protein concentration were very viscous or solid. Soluble protein, viscosity and stability of the beverage samples in coffee is given in Table 1 below. Stability in coffee is also illustrated in the photos in Figures 1 and 2, wherein samples not diluted after deamidase treatment are marked “1%”, whereas the samples diluted after deamidase treatment are marked “2.5% to 1%”, “5% to 1%” or “10% to 1%”. Table 1: Viscosity, soluble protein, and stability in coffee of the beverage samples. Samples incubated at 5% or 10% protein and heat-treated directly were too viscous to be analyzed (‘n.a.’ in table). Protein concentration, Enzyme Diluted to, % Soluble % w/w in Sample dose, w/w in solution protein, % Viscosity, Stable in solution no. IPA(U)/g before 90°C w/w in mPa*s coffee? during protein heat-treatment solution enzyme treatment 1 1 0 Not diluted 0.23 2.26 NO 2 1 2.7 Not diluted 0.70 2.22 NO 3 1 4 Not diluted 0.86 2.40 NO 4 2.5 0 Not diluted 0.54 12.21 n.a. 5 2.5 2.7 Not diluted 1.98 6.27 n.a. 6 2.5 4 Not diluted 1.97 5.56 n.a. 7 5 0 Not diluted n.a. Thick, n.a. n.a. 8 5 2.7 Not diluted n.a. Thick, n.a. n.a. 9 5 4 Not diluted n.a. Thick, n.a. n.a. 10 10 0 Not diluted n.a. Solid, n.a. n.a. 11 10 2.7 Not diluted n.a. Solid, n.a. n.a. 12 10 4 Not diluted n.a. Solid, n.a. n.a. 4.2 2.5 0.28 Diluted to 1% 0.28 3.91 NO 5.2 2.5 0.80 Diluted to 1% 0.80 2.21 NO 6.2 2.5 0.78 Diluted to 1% 0.78 2.16 NO 7.2 5 0.24 Diluted to 1% 0.24 3.62 NO 8.2 5 0.85 Diluted to 1% 0.85 2.12 YES 9.2 5 0.86 Diluted to 1% 0.86 2.29 YES 10.2 10 0.24 Diluted to 1% 0.24 3.74 NO 11.2 10 0.81 Diluted to 1% 0.81 2.00 YES 12.2 10 0.85 Diluted to 1% 0.85 2.05 YES As seen from the results, incubating almond paste at 5-10% protein with the protein deamidase (2.7 or 4 IPA(U)/g protein) at 60°C for 60 min followed by dilution to 1% protein before heat treatment at 90°C for 15 min resulted in a final beverage with low viscosity and good stability in coffee (no curdling) (sample no. 8.2 & 9.2, 11.2 & 12.2). Samples prepared without the use of the protein deamidase curdled (sample no.7.2 & 10.2). If diluting initially to 1% protein and incubating with protein deamidase at 60°C for 60 min followed by heat treatment at 90°C for 15 min the final beverage had a low viscosity, but was not stable in coffee, i.e. the sample curdled (sample no.2 & 3). Blank sample (prepared without the use of the protein deamidase) also curdled (sample no.1). Incubating almond paste at 2.5% protein with the protein deamidase (2.7 or 4 IPA(U)/g protein) at 60°C for 60 min followed by dilution to 1% protein before heat treatment at 90°C for 15 min resulted in a final beverage with low viscosity, but the stability in coffee was not good (sample no. 5.2 & 6.2). Sample prepared without the use of protein deamidase also curdled (sample no.4.2). If incubating the almond paste at 5-10% protein with protein deamidase at 60°C for 60 min followed by heat treatment at 90°C for 15 min the final beverage was very thick or even solid (sample no.7-12). When comparing soluble protein concentration in the different samples they were quite similar in all samples at 1% protein, showing that the protein deamidase had worked at all tested protein concentrations. Same trend was seen for the viscosity, wherein results were comparable between all enzyme-treated samples at final protein of 1%. Blank samples (prepared without protein deamidase) tended to be higher in viscosity when incubated at high protein and diluted to 1% before heat-treatment. Example 3: Testing protein deamidase in production of almond beverages at 1%, 2.5%, 5%, and 8% protein Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in deionized water to final protein concentrations of 1%, 2.5%, 5% or 8% and mixed in a Thermomixer. Protein deamidase was added in concentrations of 0, 2.7 or 4 IPA(U)/g protein and the mix held at 60°C for 1 hour. After incubation, samples at 1% protein were heat-treated for enzyme inactivation directly at 90°C for 15 min, while samples at 2.5%, 5% or 8% protein were diluted to 1% protein before heat-treatment (90°C/15 min). Samples were then homogenized using an Ultra-turrax at 14,000 rpm for 1 min. Beverage stability, total and soluble protein, viscosity, and stability in coffee of the final beverage were measured as described in Example 2. Results: All blank beverage samples (no enzyme; See Figures 1-4, samples marked “0 U” indicate no protein deamidase added) were unstable showing a creaming layer in the top, sedimentation at the bottom and a clearer not turbid middle layer. All samples treated with the protein deamidase were more stable having a creaming layer in the top, no/little sediment, and a milky middle layer with colloidal stable protein. Soluble protein, viscosity and stability in coffee are given in Table 2. Stability in coffee is also illustrated in the photos in Figures 3 and 4, wherein samples not diluted after deamidase treatment are marked “1%” (Figure 3), whereas the samples diluted after deamidase treatment are marked “2.5% to 1%”, “5% to 1%”, “8% to 1%” or “10% to 1%” (Figure 4). Table 2: Viscosity, soluble protein, and stability in coffee of the final almond beverages. Protein Diluted to, concentration, Enzyme % w/w in Soluble Sample % w/w in dose, solution protein, % Viscosity Stable in no. solution during IPA(U)/g before 90°C w/w in mPa*s coffee? enzyme protein heat- solution treatment treatment 1 1 0 Not diluted 0.24 3.14 NO 2 1 2.7 Not diluted 0.79 2.40 NO 3 1 4 Not diluted 0.85 2.07 NO 4 2.5 0 Not diluted 0.40 9.01 n.a. 5 2.5 2.7 Not diluted 2.04 5.39 n.a. 6 2.5 4 Not diluted 2.15 5.56 n.a. 4.2 2.5 0 Diluted to 1% 0.22 3.91 NO 5.2 2.5 2.7 Diluted to 1% 0.84 2.14 NO 6.2 2.5 4 Diluted to 1% 0.85 2.19 NO 7.2 5 0 Diluted to 1% 0.21 3.58 NO 8.2 5 2.7 Diluted to 1% 0.88 2.23 YES 9.2 5 4 Diluted to 1% 0.89 2.18 YES 10.2 8 0 Diluted to 1% 0.21 3.52 NO 11.2 8 2.7 Diluted to 1% 0.92 2.14 YES 12.2 8 4 Diluted to 1% 0.93 2.20 YES Overall results confirm what was seen in Example 2, in this case testing at 8% protein instead of 10%. Incubating with protein deamidase at higher protein content (5% or 8%) and diluting to 1% before doing heat-inactivation improved the stability in coffee, while keeping other parameters like soluble protein and viscosity comparable to samples that were incubated at 1% protein. Example 4: Testing protein deamidase at lower dosages in production of almond beverages at 1%, 5%, and 8% protein and measuring NH₄ production Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in deionized water to final protein concentrations of 1%, 5% or 8% and mixed in a Thermomixer. Protein deamidase was added in concentrations of 0, 0.7, 1.3, 2.7, or 4 IPA(U)/g protein and the mix held at 60°C for 1 hour. After incubation, samples at 1% protein were heat-treated for enzyme inactivation directly at 90°C for 15 min, while samples at 5% or 8% protein were diluted to 1% protein before heat-treatment (90°C/15 min). Samples were then homogenized using an Ultra- turrax at 14,000 rpm for 1 min. Beverage stability, soluble protein, and stability in coffee of the final beverage were measured as described in Example 2. NH₄ production was measured using the ammonia detection step as described in Example 1 (step 2 of the Assay procedure). Results: All blank beverage samples (no protein deamidase added) were unstable showing a creaming layer in the top, sedimentation at the bottom and a clearer not turbid middle layer. All samples with enzyme were more stable having a creaming layer in the top, no/little sediment, and a milky middle layer with colloidal stable protein. Soluble protein, NH₄ produced and stability in coffee are given in Table 3. Table 3: Soluble protein, and stability in coffee of the final almond beverages Protein concentration, Enzyme Diluted to, % Soluble Stable in NH Sample % w/w in dose, w/w in solution protein, % ₄ coffee produced, no. solution during IPA(U)/g before 90°C w/w in after 5 mg/L enzyme protein heat-treatment solution min? treatment 1 1 0 Not diluted 0.22 7.8 NO 2 1 0.7 Not diluted 0.55 24.7 NO 3 1 1.3 Not diluted 0.61 30.1 NO 4 1 2.7 Not diluted 0.68 41.8 NO 5 1 4 Not diluted 0.71 48.4 NO 6 5 0 Diluted to 1% 0.20 7.2 NO 7 5 0.7 Diluted to 1% 0.64 29.5 NO 8 5 1.3 Diluted to 1% 0.70 39.7 NO 9 5 2.7 Diluted to 1% 0.75 51.5 NO 10 5 4 Diluted to 1% 0.76 56.5 YES 11 8 0 Diluted to 1% 0.21 7.6 NO 12 8 0.7 Diluted to 1% 0.69 32.5 NO 13 8 1.3 Diluted to 1% 0.75 45.3 NO 14 8 2.7 Diluted to 1% 0.77 62.0 YES 15 8 4 Diluted to 1% 0.78 68.1 YES Similar to the previous Examples 2 and 3, incubation at 1% protein and direct heat- treatment resulted in an almond beverage that was not stable in coffee. However, incubating at 5% or 8% protein followed by diluting to 1% protein before heat-treatment resulted in beverages that were stable in coffee for the samples obtained using higher enzyme dosages (sample no. 10, 14, 15). Soluble protein was a little higher in samples made with the same enzyme dosage but incubated at higher protein, while NH₄ production was clearly higher in these (for example sample no. 15 vs. 10, vs. 5), indicating that the enzyme performed better at higher protein concentration. Example 5: Testing protein deamidase in production of almond beverages at 1% protein with and without NaCl Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in deionized water to a final protein concentration of 1% and mixed in a Thermomixer. Protein deamidase was added in increasing dosages as indicated in Table 4A, and the mix held at 60°C for 1 hour. After incubation, samples were heat-treated at 90°C for 15 min for enzyme inactivation. Beverage stability, soluble protein, and stability in coffee of the final beverage was measured as described in Example 2. A similar set of samples were made except that 0.15% NaCl was added to the almond suspensions before incubation as indicated in Table 4B. Almond paste used was 24.5 % protein. Results: The blank beverage samples (no protein deamidase added) were unstable showing a creaming layer in the top, sedimentation at the bottom and a clearer not turbid middle layer. All of the samples treated with protein deamidase were more stable having a creaming layer in the top, no/little sediment, and a milky middle layer with colloidal stable protein. Blank sample (no protein deamidase added) with NaCl had a larger precipitation and less creaming layer than blank samples without NaCl. Soluble protein and stability in coffee are shown in Table 4A and 4B. Table 4A: Soluble protein, and stability in coffee of the final almond beverages without NaCl Enzyme Soluble Stable in Sample dose, protein, % coffee no. IPA(U)/g w/w in after 10 protein solution min? 1 0 0.26 NO 2 0.7 0.59 NO 3 1.3 0.67 NO 4 2.7 0.74 NO 5 4.0 0.77 NO 6 5.3 0.79 NO 7 6.7 0.81 NO 8 8 0.81 NO/YES 9 9.3 0.82 YES Table 4B: Soluble protein, and stability in coffee of the final almond beverages with 0.15% NaCl. Sample Enzyme NaCl, % Soluble Stable in no. dose, w/w on protein, % coffee IPA(U)/g beverage w/w in after 5 protein solution min? 1 0 0 0.23 NO 2 0 0.15 0.21 NO 3 0.7 0.15 0.54 NO 4 1.3 0.15 0.63 NO 5 2.7 0.15 0.70 NO/YES 6 4.0 0.15 0.76 YES 7 5.3 0.15 0.76 YES 8 6.7 0.15 0.77 YES 9 8 0.15 0.78 YES 10 9.3 0.15 0.77 YES Based on the results shown in Table 4A and 4B, it can be concluded that the addition of NaCl in the process according to the invention improves the stability of the final beverage in coffee. At the same time, there was a trend that NaCl reduced the level of soluble protein slightly. To test the relevance of timing of the addition of the chloride salt, a second experiment was conducted. For this, a 1% almond protein slurry was prepared by mixing one (1) part almond base (25% protein) and 24 part distilled water. The slurry was then aliquoted into 13 samples of each 80g. The slurry was mixed well and protein deamidase and sodium chloride (NaCl) added in the dosages according to Table 5. Samples were incubated at 60°C for 60 minutes in the presence of protein deamidase alone (samples 2 to 7 in Table 5) or in the presence of protein deamidase and NaCl (samples 8 to 13 in Table 5). Sample 1 in Table 5 was included as blank control, containing no protein deamidase or NaCl. Following incubation, the samples were heat-treated at 90°C for 15 minutes to inactivate the enzyme, and subsequently cooled down using iced water. Samples were homogenized using Ultra-turrax set at 14,000 rpm for 1 minute. Samples were then stored cold until further analysis. Table 5: Samples treated with different concentrations of protein deamidase and with or without the addition of NaCl during enzyme incubation. Sample PD, IPA(U)/g no. _protein ^{NaCl in % w/w based on slurry} 1 0 0 2 0 0.15% added with enzyme 3 0.7 0.15% added with enzyme 4 1.4 0.15% added with enzyme 5 2.7 0.15% added with enzyme 6 4.1 0.15% added with enzyme 7 5.4 0.15% added with enzyme 8 0 0.15% added after incubation before heat treatment 9 0.7 0.15% added after incubation before heat treatment 10 1.4 0.15% added after incubation before heat treatment 11 2.7 0.15% added after incubation before heat treatment 12 4.1 0.15% added after incubation before heat treatment 13 5.4 0.15% added after incubation before heat treatment Soluble protein was determined in the supernatant after spinning at 14,000 rpm for 10 minutes using a LECO analyzer (Dumas determination of nitrogen after combustion, reduction and detection of N2 using a conductivity detector). Protein factor was 5.18. Ammonium content (NH₄) was also determined in supernatant after spinning at 14,000 for 10 minutes using the ammonia detection step as described in Example 1 (step 2 of the Assay procedure). Samples were diluted 3x. Stability of the beverage samples were evaluated visually. Stability of the beverage samples in coffee was assessed using warm filter coffee (medium roasted, pH:~4.95-5.01, temperature: 58-63°C), mixing four parts of coffee with one part cold beverage sample, leaving the mix for 5 minutes, and evaluating curdling/precipitation visually. Table 6: Soluble protein, ammonium content and stability in coffee of the beverage samples of Table 5. Protein Soluble Sodium Ammonium Stability in Sample deamidase, protein, % chloride, 0.15% content coffee, 5 no IPA(U)/g w/w in w/w on slurry (NH₄) minutes protein beverage 1 0 0 0.20 3.3 NO 2 0 Before incubation 0.19 5.6 NO 3 0.7 Before incubation 0.53 35.5 NO 4 1.3 Before incubation 0.67 62.2 NO 5 2.7 Before incubation 0.73 69.2 NO 6 4.0 Before incubation 0.76 70.2 YES 7 5.4 Before incubation 0.78 80.0 YES 8 0 After incubation 0.21 4.6 NO 9 0.7 After incubation 0.39 27.5 NO 10 1.3 After incubation 0.53 36.0 NO 11 2.7 After incubation 0.59 40.9 NO 12 4.0 After incubation 0.65 51.6 NO 13 5.4 After incubation 0.67 56.4 NO Analyzed total protein in the samples ranged from 1.05 to 1.09 %. Stability in coffee is also illustrated in the photos in Figure 5. As clearly supported by the data presented herein, it has been found that adding small amounts of chloride salts, such as 0.15% sodium chloride (NaCl), to a 1% protein almond slurry during treatment of the slurry with protein deamidase (samples 2-7) improves the efficiency of the enzyme resulting in more NH₄ produced and a higher content of soluble protein compared to a sample where NaCl was added after enzyme incubation (samples 8-13). Also stability in coffee was improved in samples with NaCl added before incubation at enzyme dosages at 4 IPA(U)/g protein and above, showing that the effect of NaCl is related to enzyme performance and not some kind of stabilizing effect of the almond protein in the coffee. Example 6: Testing protein deamidase and phosphate/citrate salts in production of almond beverages at 1% protein Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in deionized water to a final protein concentration of 1% and mixed in a Thermomixer. The slurry was then aliquoted into smaller samples of each 50 grams. K₂HPO₄ or NaCl was added to the samples according to the Table 7 below. Protein deamidase was added in dosages as indicated in the table (Table 7), and the mix held at 60°C for 1 hour. After incubation, the samples were heat- treated for enzyme inactivation at 90°C for 15 minutes. NH₄ production and stability in coffee of the final beverage were measured as described in Example 1 and 3, respectively. NH₄ produced and stability in coffee are shown in Table 7. Table 7: NH₄ produced and stability in coffee of the final almond beverages. Enzyme Sample dosage, K₂HPO₄, % NaCl, % w/w NH g w/w on on Stability in no. IPA(U)/ almond produced, almond drink dr coffee, 5 min protein ink mg/L 1 0 0 0 0.4 NO 2 1.4 0 0 27.5 NO 3 2.7 0 0 38.7 NO 4 4.1 0 0 51.4 NO 5 0 0.15 3.9 NO 6 0 0.5 4.8 NO 7 0 1 3.8 NO 8 1.4 0.15 25.8 NO 9 1.4 0.5 36.1 YES 10 1.4 1 35.1 YES 11 2.7 0.15 38.4 NO 12 2.7 0.5 37.2 YES 13 2.7 1 44.8 YES 14 4.1 0.15 46.5 YES 15 4.1 0.5 45.9 YES 16 4.1 1 55.0 YES 17 0 0.1 1.7 NO 18 0 0.15 0.9 NO 19 1.4 0.1 39.4 NO 20 1.4 0.15 39.8 NO 21 2.7 0.1 51.1 NO 22 2.7 0.15 63.5 NO 23 4.1 0.1 67.0 YES 24 4.1 0.15 82.5 YES When comparing NH₄ generation in the samples treated with protein deamidase, it was clearly seen that addition of NaCl again improved the overall enzyme performance resulting in a higher NH₄ generation in samples with NaCl (sample Nos 19-24) than in samples with only protein deamidase added (sample Nos 2-4) or in samples where K₂HPO₄ was added (sample Nos 8-16). When comparing the stability in coffee of the different samples, the deamidation achieved with protein deamidase and NaCl (sample Nos 19-24) was sufficient at the highest enzyme dosage. Samples with K₂HPO₄ added at or above 0.5% were stable at low and medium enzyme dosage; at the highest enzyme dosage only 0.15% K₂HPO₄ was needed for stability in coffee. Overall the results show that adding NaCl in concentrations of 0.1-0.15% (w/w) in combination with protein deamidase improves enzyme performance as shown by the higher degree of deamidation. This same effect was not observed when using K₂HPO₄. The effect on coffee stability is probably caused by different mechanisms, i.e., addition of NaCl improves enzyme performance resulting in a higher degree of deamidation and hereby improved stability of the protein, while addition of K₂HPO₄ not directly affect the enzyme but act as a buffer, increasing pH, and hereby improving protein stability. Since sodium chloride is often used in the fortification of the final dairy alternative beverages, it is thus beneficial to use sodium chloride already during the enzymatic treatment with the protein deamidase. Additionally, the effect of sodium chloride enables manufacturers to use an alternative salt than for example K₂HPO₄, thereby enabling a simplified production method for clean-label seed-based dairy alternative beverages, preferably for barista applications. Example 7: Testing protein deamidase in production of almond beverages at 1% and 8% protein at 30°C and 60°C Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in water (deionized) to final protein concentrations of 1% or 8% and mixed in a Thermomixer. The mix was aliquoted into smaller batches with 50 g/bottle and protein deamidase added in concentrations of 0 - 1.3 - 2.7 – 5.4 - 10.8 IPA(U)/g protein. Incubation was done at 30°C or 60°C for 1 hour. After incubation, samples at 1% protein were heat-treated for enzyme inactivation directly at 90°C for 15 minutes, while samples at 8% protein were diluted to 1% protein before heat-treatment at 90°C for 15 minutes. Samples were then homogenized using an Ultra-turrax at 14,000 rpm for 1 min. Soluble protein, NH₄ production and stability in coffee of the final beverage were measured. Soluble protein was measured in the supernatant of a sample after centrifugation at 21,000g for 10 min. Protein determination was done using a LECO analyzer (Dumas determination of nitrogen after combustion, reduction and detection of N2 using a conductivity detector). Protein factor was 5.18. Ammonium content (NH₄) was determined using the ammonia detection step as described in Example 1 (step 2 of the Assay procedure). Stability in coffee was measured using warm coffee (pH: ~ 4.95-5.01, temperature: 58- 63°C), wherein four (4) parts coffee was mixed with one (1) part cold almond beverage, the mix was left for 5-10 minutes, and then evaluated curdling/precipitation visually. Soluble protein, NH₄ production and stability in coffee are given in Table 8 below. Stability in coffee is also illustrated in the photos in Figure 6. Table 8: Total and soluble protein, NH₄ concentration and stability in coffee of the almond beverages Sample Protein Temp., Enzyme Total Soluble NH Stability in no. conc., % °C dose, protein, % protein, % produced, coffee, 5 w/w in IPA(U)/g w/w in w/w in mg/L min solution protein solution solution 1 8 60 0 1.03 0.24 5.5 NO 2 8 60 1.4 1.03 0.75 69.7 NO 3 8 60 2.7 n.a. 0.78 82.4 YES 4 8 60 5.4 n.a. 0.80 94.5 YES 5 8 60 10.8 n.a. 0.81 101.5 YES 6 1 60 0 1.01 0.20 6.1 NO 7 1 60 1.4 1.03 0.50 32.3 NO 8 1 60 2.7 n.a. 0.61 45.2 NO 9 1 60 5.4 n.a. 0.69 75.7 NO 10 1 60 10.8 n.a. 0.74 73.6 NO 11 8 30 0 1.06 0.25 6.7 NO 12 8 30 1.4 1.00 0.58 36.5 NO 13 8 30 2.7 n.a. 0.73 49.4 NO 14 8 30 5.4 n.a. 0.78 65.1 YES 15 8 30 10.8 n.a. 0.80 80.2 YES 16 1 30 0 1.03 0.20 6.5 NO 17 1 30 1.4 1.00 0.42 25.9 NO 18 1 30 2.7 n.a. 0.57 38.4 NO 19 1 30 5.4 n.a. 0.68 44.5 NO 20 1 30 10.8 n.a. 0.74 56.3 NO As seen from the results in Table 8, the positive effect of doing enzyme treatment at higher protein concentration (8% protein vs.1% protein) observed at 60°C was also seen if the enzyme incubation was carried out at lower temperature (such as 30°C). That is, the enzyme is more efficient when incubated at the higher protein concentration, resulting in higher soluble protein, more NH₄ produced and better stability in coffee is observed. For the samples incubated at 8% protein, 60°C enzyme incubation gave stability of the resulting beverage in coffee at an enzyme dosage of or above 2.7 IPA(U)/g protein. At 30°C enzyme incubation, stability was observed at or above 5.4 IPA(U)/g protein. All samples incubated at 1% protein were unstable in coffee. At same enzyme dosage, soluble protein was higher (10-50%) in samples incubated at 8% protein compared to 1%, especially in the lower enzyme dosage range, while NH₄ production was clearly higher (40-100%) in all samples at the higher protein concentration. As expected, enzyme performance was lower at 30°C compared to 60°C as seen from the NH produced. Example 8: Testing protein deamidase in production of almond beverages at 1% protein with NaCl added before or after enzyme incubation at 30°C Almond paste (Almond paste from KoRo, 21-25% protein) was suspended in deionized water to a final protein concentration of 1% and mixed in a Thermomixer. The slurry was then aliquoted into 13 samples of each 80g. 0.15% NaCl was added to samples 2-7 (NaCl added before enzyme incubation). Protein deamidase was added in increasing dosages as indicated in Table 9, and the mix held at 30°C for 1 hour. After incubation, samples 1-7 were heat-treated for enzyme inactivation at 90°C for 15 minutes. To samples 8-13, 0.15% NaCl was added (NaCl added after incubation) just before heat inactivation. Soluble protein, NH4 production and stability in coffee of the final beverage were measured as described in Examples 1 and 2. Soluble protein, NH4 produced and stability in coffee are shown in Table 9. Stability in coffee is also illustrated in the photos in Figure 7. Table 9: Soluble protein and stability in coffee of the almond beverage samples. Sample Enzyme NaCl, % Soluble NH Stability no. dose, w/w on protein, % produced, in coffee, IPA(U)/g almond w/w in mg/L 10 min protein drink solution 1 0 0 0.20 5.4 NO 2 0 0.15 before 0.20 6.6 NO 3 1.3 0.15 before 0.41 27.7 NO 4 2.7 0.15 before 0.63 41.3 NO 5 4.0 0.15 before 0.70 48.7 NO 6 5.4 0.15 before 0.74 55.4 NO 7 6.7 0.15 before 0.76 58.0 YES 8 0 0.15 after 0.20 7.3 NO 9 1.3 0.15 after 0.28 25.2 NO 10 2.7 0.15 after 0.55 38.8 NO 11 4.0 0.15 after 0.59 47.1 NO 12 5.4 0.15 after 0.63 44.8 NO 13 6.7 0.15 after 0.67 50.3 NO Looking at the results NaCl clearly improved overall enzyme performance showing much higher soluble protein and NH4 generation in samples with NaCl added during incubation (samples 2-7) compared to samples where NaCl was added after incubation (samples 8-13). Also stability in coffee was improved in samples with NaCl added before incubation at highest tested enzyme dosage of 6.7 IPA(U)/g protein, showing that the effect of NaCl is related to enzyme performance and not an interaction or stabilization with the protein in the coffee. Compared to Example 5, the improved effect of NaCl on overall enzyme performance was also observed at 30°C. However, as could be expected a slightly higher enzyme dosage is needed at enzyme incubation of 30°C compared to 60°for the same performance. Example 9: Testing protein deamidase on dairy alternative beverages based on pea protein isolate at 2.45%, 4.9% and 9.8% protein Enzyme reaction Pea protein isolate (Roquette Nutralys S85F 2.0, protein concentration 82%) was suspended in tap water to a final protein concentration of 2.45%, 4.9% or 9.8% and mixed with magnetic stirrer. Protein deamidase was added in concentrations of 0, 0.67, 2, or 6 IPA(U)/g protein, and the mixtures were incubated at 60°C for 1 hour in a FINEPCR combi-D24 Rotisserie with rotation speed set at 7. After incubation, the samples were heat treated at 85°C for 10 minutes for enzyme inactivation. Then protein solubility, deamidation degree and coffee stability of the samples were analyzed. Protein solubility measurement Protein solubility was measured in the supernatant of each sample after centrifugation at 15,000g for 10 minutes. Then protein content determination was done using a LECO analyzer (Dumas determination of nitrogen after combustion, reduction and detection of N2 using a conductivity detector). Protein factor was 6.25. Protein deamidation measurement Deamidation degree was measured with ammonia test kit from HACH (HACH, High Range Ammonia Test N Tube Rgt (0-50 mg/L N)). The amount of ammonia released from deamidated pea protein isolate (PPI) (2.45%, 4.9% or 9.8% protein concentration) with and without protein deamidase treatment as well the total ammonia released from PPI by acid hydrolysis were measured using the HACH Kit and the procedure described below. The procedure was as below: 1. For the deamidation degree test, the 9.8% PPI pasteurized solution was diluted to 6% protein concentration using DI water. The 2.45% PPI and 4.9% PPI pasteurized solution were tested directly without dilution. 2. Used the HACH KIT to test deamidation degree for original solution 2.45%, 4.9% and diluted solution of 6%. 3. The total ammonia released was measured by drawing 1000 µL control sample solution, then adding 500 µL 6M HCl and treating at 100°C for 3h to analyze the total ammonia released. After acid hydrolysis, 28 mL pH7.0 buffer (0.1M citric acid-0.2M Na₂HPO₄ buffer) and 550 µL 6M NaOH were added to adjust pH of hydrolysis mixture to 7.0 and diluted 30 times in total. The ammonia released was determined by HACH kit. 4. The free ammonia released was measured by drawing 1000 µL deamidase treated- sample solutions and centrifuging at ambient temperature at 12,000 rpm for 10 minutes. Then pH7.0 buffer (0.1M citric acid-0.2M Na2HPO4 buffer) was added to the supernatant followed by dilution 2-10 times in total according to ammonia releasing level. Then drew 100 µL for free ammonia amount analysis. 5. The deamidation degree was defined as the ratio between free ammonia amount released by deamidase reaction (step 4 measurements) and the total ammonia amount (from both glutamine and asparagine, step 3 measurements) released by hydrochloric acid protein hydrolyzation. HACH, AmVer Salicylate Test’N Tube method: 1. Start program 343 N, Ammonia HR TNT. 2. Prepare the blank: Add 0.1 mL of ammonia-free water to one AmVer™ Diluent Reagent Test 'N Tube for High Range Ammonia Nitrogen. 3. Prepare the sample: Add 0.1 mL of sample to one AmVer™ Diluent Reagent Test 'N Tube for High Range Ammonia Nitrogen. 4. Add the contents of one Ammonia Salicylate Reagent Powder Pillow for 5 mL samples to each vial. 5. Add the contents of one Ammonia Cyanurate Reagent Powder Pillow to each vial. 6. Put the caps on both vials. Shake thoroughly to dissolve the powder. 7. Start the instrument timer. A 20 minute reaction time starts. 8. Clean the blank vial. 9. Insert the blank vial into the 16 mm cell holder. 10. Push ZERO. The display shows 0.0 mg/L NH3–N. 11. Clean the sample vial. 12. Insert the sample vial into the 16 mm cell holder. 13. Push READ. Results show in mg/L NH3–N. Coffee stability evaluation Stability in coffee was measured using warm instant Nescafe gold coffee. The instant coffee was prepared according to instructions, which suggest mixing 2 grams of instant coffee powder with 150 mL 85°C boiled tap water (tap water 11dH, pH 6.5-6.8). The PPI solutions were adjusted to 2.45% protein concentration before mixing with the prepared coffee. Then the PPI solutions were mixed with hot (85°C) coffee according to recipe, the mix left for 5-10 minutes, and then evaluated visually for curdling/precipitation. Results As can be seen from the results shown in Tables 10-12 below, at the same enzyme dosage, but with different initial pea protein concentration, the deamidation degree was improved with the pea protein concentration level, especially for 9.8% pea protein level (Table 11). The deamidation degree was improved from 11.7% to 15.1% at enzyme dosage of 2 IPA(U)/g protein and from 15.9% to 19.5% at enzyme dosage of 6 IPA(U)/g protein (Table 11). The solubility improvement (Table 10) was more significant at high dry matter deamidation also the deamidation degree was significantly improved at 9.8% dry matter compared to low dry matter. Similarly, when deamidation was performed at high protein concentration, the coffee stability could be significantly improved compared to low protein concentration (Table 12). At 0.67 IPA(U)/g protein, the deamidated pea protein solution with 9.8% protein concentration was stable at isolate:coffee ratio of 1:3, whereas the 2.45% and 4.9% pea protein concentrations were not. Also, at 6 IPA(U)/g protein, only the deamidated pea protein with 9.8% protein concentration was stable at the isolate:coffee ratio of 1:7. Similarly, at the enzyme dosage of 2 IPA(U)/g protein, the deamidated pea protein with 4.9% protein concentration or above was stable at the isolate:coffee ratio of 1:4, while the deamidated pea protein solution with 2.45% protein concentration was not stable. Table 10: Solubility improvement of different PPI samples Enzyme dose, 2.45% pea 4.9% pea protein 9.8% pea protein IPA(U)/g protein protein Solubility Deamidation degree Deamidation degree 0 47% 51% 55% 0.67 54% 60% 65% 2 61% 64% 70% 6 63% 67% 74% Table 11: Deamidation degree of different PPI samples Enzyme dose, 2.45% pea protein 4.9% pea protein 9.8% pea protein IPA(U)/g protein Deamidation degree Deamidation degree Deamidation degree 0 1.9% 2.1% 2.3% 0.67 7.1% 8.7% 8.5% 2 11.6% 11.7% 15.1% 6 15.3% 15.9% 19.5% Table 12: Coffee stability of different PPI samples 2.45% pea protein 4.9% pea protein 9.8% pea protein deamidated deamidated deamidated Undiluted for coffee Diluted to 2.45% Pea Diluted to 2.45% pea stability protein for coffee stability protein for coffee stability Ratio Enzyme dose, IPA(U)/g Enzyme dose, IPA(U)/g Enzyme dose, IPA(U)/g (w/w) protein protein protein of PPI: 0 0.67 2 6 0 0.67 2 6 0 0.67 2 6 coffee 1:2 NO YES YES YES NO YES YES YES NO YES YES YES 1:3 NO NO YES YES NO NO YES YES NO YES YES YES 1:4 NO NO NO YES NO NO YES YES NO YES YES YES 1:5 NO NO NO YES NO NO NO YES NO NO NO YES 1:7 NO NO NO NO NO NO NO NO NO NO NO YES

Claims

CLAIMS 1. A method for obtaining a seed-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of seed material in water; (b) treating the slurry of seed material in water with a protein deamidase to obtain a slurry of enzymatically deamidated seed material; (c) optionally diluting the slurry of enzymatically deamidated seed material to obtain a diluted slurry of enzymatically deamidated seed material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated seed material to obtain the seed-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of step (a) has a protein content of at least 3% (w/w).

2. The method of claim 1, wherein the treatment of step (b) is carried out at a temperature in the range of 10-80°C, such as in the range of 20-60°C, 15-40°C, 20-30°C, or 50-60°C, preferably wherein the treatment of step (b) is carried out for 15-90 minutes, such as for 30-60 minutes.

3. The method of any of the preceding claims, wherein the chloride salt is selected from potassium chloride and sodium chloride, preferably sodium chloride.

4. The method of any of the preceding claims, wherein the chloride salt is in an amount of 0.05- 2% chloride salt (w/w) based on the slurry, preferably in an amount of 0.07-0.2% (w/w) based on the slurry, such as about 0.10% (w/w) or about 0.15% (w/w) based on the slurry. 5. The method of any of the preceding claims, wherein the slurry of seed material in water has a protein content in the range of 0.1-3% (w/w), such as in the range of 0.1-2.5% (w/w), 0.5-1.

5% (w/w) or 1-2% (w/w), such as about 1% (w/w).

6. The method of any of claims 1-4, wherein the slurry of seed material in water has a protein content in the range of 4-20% (w/w), preferably in the range of 5-15% (w/w), more preferably in the range of 5-10% (w/w), and the diluted slurry of enzymatically deamidated seed material has a protein content of at most 2.5% (w/w), preferably wherein the protein content of the diluted slurry of enzymatically deamidated seed material is in the range of 0.1-2.5% (w/w), such as in the range of 0.5-2% (w/w), such as in the range of 1-2% (w/w), such as about 1% (w/w).

7. The method of any of the preceding claims, wherein a stabilizer and/or emulsifier is not present during steps (a), (b), (c) and/or (d).

8. The method of any of the preceding claims, wherein the seed material is obtained or derived from almond, cashew, chickpea, coconut, fava bean, hazelnut, lentil, lupin, macadamia, mung bean, pistachio, pea, peanut, pecan, soy, walnut or any combination thereof, preferably from almond, pea, soy or any combination thereof.

9. The method of any of the preceding claims, wherein the seed-based dairy alternative beverage is an almond drink, a cashew drink, a chickpea drink, a coconut drink, a fava bean drink, a hazelnut drink, a lentil drink, a lupin drink, a macadamia drink, a mung bean drink, a pistachio drink, a pea drink, a peanut drink, a pecan drink, a soy drink, a walnut drink, or any combination thereof, preferably an almond drink, a pea drink, a soy drink, or any combination thereof.

10. The method of any of the preceding claims, wherein the seed-based dairy alternative beverage is for use in an acidic beverage, such as a sports drink, a coffee drink or a tea drink, preferably a coffee drink.

11. The method of any of the preceding claims, wherein the protein deamidase is derived from or obtained from a Chryseobacterium species, such as from Chryseobacterium proteolyticum or Chryseobacterium viscerum.

12. The method of any of the preceding claims, wherein the seed-based dairy alternative beverage has an increased stability to heat and/or low pH compared to a seed-based dairy alternative beverage prepared using the same method but without a protein deamidase.

13. The method of any of the preceding claims, wherein a lower dosage of protein deamidase is used compared to when the same method is used but the protein deamidase treatment is in the absence of a chloride salt and/or the slurry of step (a) does not have a protein content of at least 3% (w/w).

14. A method for obtaining an almond-based dairy alternative beverage, the method comprising the steps of: (a) providing a slurry of almond material in water; (b) treating the slurry of almond material in water with a protein deamidase to obtain a slurry of enzymatically deamidated almond material; (c) optionally diluting the slurry of enzymatically deamidated almond material to obtain a diluted slurry of enzymatically deamidated almond material; and (d) heat treating the optionally diluted slurry of enzymatically deamidated almond material to obtain the almond-based dairy alternative beverage, wherein the treatment with the protein deamidase is in the presence of a chloride salt and/or the slurry of step (a) has a protein content of at least 3% (w/w).

15. A seed-based dairy alternative beverage obtainable by the method of any of claims 1-14.

16. Use of a protein deamidase in the production of a seed-based dairy alternative beverage to improve stability, preferably wherein the seed-based dairy alternative beverage is an almond beverage, a pea beverage, a soy beverage or any combination thereof.