RU2609635C1 - Method for production of collagen protein from animal raw materials, collagen products and methods for use thereof - Google Patents

Abstract

FIELD: food industry.

SUBSTANCE: group of inventions relates to food industry. For production of edible collagen powder and fibrous edible collagen, method is implemented as follows. Raw material used is split cattle hide. Method comprises peroxide-alkaline treatment of split hide for 2–6 hours at a ratio of weight of solution and weight of split hide of not less than 1.3 and content of sodium hydroxide in treated mixture of solution and split hide of not less than 15 g/l and hydrogen peroxide 5.2–8.5 g/l. Treated split hide is washed with running water until pH drops to level of 10-11. Split hide is neutralised with citric acid for 2-6 hours to pH 5.0–8.0. Produced material is dried and ground. Further, material is ground to particle size from 50 to 1,200 mcm, followed by fractionation of ground material into at least into two fractions, of which fraction with smaller particle size is powdered collagen, and fraction with large particle size is fibrous collagen. For production of meat product, wherein a composition is prepared for production of mince sausage product or functional mixture, used in mince meat products independently or instead of part of meat raw material, powdered collagen is used. For production of meat product, wherein a composition is prepared for production of chopped semi-product, fibrous collagen is used.

EFFECT: group of inventions widens range of products of collagen in form of fractions with different functional and technological characteristics, increases output of finished product, reduces time of obtaining product.

16 cl, 6 tbl, 3 ex

Description

Field of Invention

The invention relates to the food industry and can be used to obtain functional proteins suitable for use in the production of sausages, chopped semi-finished products and deli meats.

State of the art

Collagen is the main protein of connective tissue. It has a fibrillar structure, which determines its functional properties.

In the food industry, collagen of varying degrees of purification and degradation is in demand. The long-used gelatin is a subunit of collagen α-chains with a molecular weight of 30–40 kD. Gelatin forms gels that melt easily in the mouth. The gel formation begins at a temperature below 30 ° C, and already at 32-35 ° C the gel reversibly melts. In this regard, the scope of gelatin as a moisture-binding protein is limited.

In addition to gelatin, fibrous collagen with a preserved powder structure is used in the food industry. Collagen has a higher degree of hydration than vegetable proteins, it binds water and fat well, is an excellent emulsifier and stabilizer, therefore collagen gels retain their structure during freezing and thawing, improve the texture and juiciness of the finished product. However, high requirements are imposed on a collagen protein with a native structure in that it must retain its technological properties under the influence of various factors, both during long-term storage and during processing.

The technological properties of collagen depend on the method of its production. The authors of the present invention found that the quality of the collagen obtained largely depends on the chemical treatment of collagen raw materials used before the subsequent processes of dehydration and grinding of raw materials.

As a collagen raw material for producing collagen powder, a split saw is used, which is a by-product of leather production. More specifically, in the tanning industry, hides ("goblets") are subjected to operations of salting, soaking, gilding, rituals of goblet, stain and double. After the doubling operation separating the clay into the face layer and split, the face layer is sent to the production of leather, and the waste - clay split - is used to produce collagen powder.

In order to make a cleaved split suitable for producing collagen powder from it, the split must be subjected to additional chemical treatment.

A known method (RF patent No. 2061724), in accordance with which the leather raw materials are crushed, washed in water and pressed to remove excess moisture. Then, the leather raw materials are placed in a solution containing hydrogen peroxide and alkali at their concentrations of 1.0 to 3.0 and 1.5 to 5.0, respectively, for a period of 10 to 22 hours at a temperature of 20 to 25 ^o C and the ratio of solution: raw materials 1.5: 2.0, after which the raw materials are again pressed, washed, pressed again, neutralized with acid for 15-17 hours at a ratio of solution: raw materials of 1.5: 2.0, and finally washed with cold water with periodic stirring. The end of the washing is controlled by the pH of the aqueous extract from the feed, which should be 5.5 - 6.0. Given that each washing of the raw materials lasts several hours, the total duration of the above process of preparing the raw materials for the production of gelatin is at least two days.

However, the known method does not allow to obtain high-quality collagen powder, since the above treatment results in hydrolysis of hydrogen and cross bonds, excessive loosening of the structure and significant loss of protein due to dissolution and deamination. Moreover, the processing process is excessively long, laborious and does not provide the desired purity of the resulting semi-finished product.

The method of chemical purification of collagen with alkaline salt solutions, known from RF patent 2031597, class A23J 1/10, which consists in sequential processing of collagen-containing raw materials with an alkaline salt mixture, hydrochloric acid to neutralize the intermediate product, washing it with running water, using ultrasonic treatment for individual its stages is also long, expensive and leads to excessive loosening of the collagen structure.

Closest to the claimed technical solution according to the technical essence and the technical result achieved is a method for processing collagen-containing raw materials, known from the RF patent 2551195 (class A23J 1/10), including dressing the skins, their trimming and coiling, their chemical treatment in an alkaline medium together with peroxide hydrogen, degreasing raw materials from the inner side to the contained fatty substances 0.05-1%, rinsing with running water to neutral pH, freezing of 6-14 hours at a temperature between -20 ⁰ C and -30 ⁰ C, grinding at the at a temperature of -10 ⁰ C to -20 ⁰ C to a particle size of 2-5 mm, the crushed glue is dehydrated by sublimation to a moisture content of 1-10%, after which it is ground to a powder state and Packed.

More specifically, the dry collagen powder in the prototype is obtained as follows - the skin is dressed, trimmed and skinned, the prepared gooey is treated with a peroxide-alkaline solution containing 5% sodium hydroxide and 0.8% hydrogen peroxide for 18 hours, the gooey is degreased, washed running water until neutral pH, frozen material to a temperature of - 30 ⁰ c in the thickness of the material for 20 hours, pulverized material (via cutting) to 2-5 mm particle size, freeze-dried material at a temperature of - 30 ⁰ c during e 10 hours and ground (crusher) to a homogeneous powder.

The method according to the patent of the Russian Federation 2551195 is aimed at maximizing the protein structure, facilitating the process of subsequent grinding. The low-temperature effect contributes to the further destruction of intermolecular bonds at the tissue level and the maximum weakening of the interaction between the main component of the skin tissue and its accompanying substances, which allows for a more rapid preparation of the final product using lower concentrations of the main ingredients. However, this processing method is lengthy, which reduces the yield of the final product, and freeze-drying is a batch process. The known method allows to obtain only powdered collagen and eliminates the possibility of obtaining fibrous collagen. Thus obtained collagen in the form of a powder has a wide variation in particle size, which reduces the functional and technological properties of the protein. Grinding at low temperatures with control of the thermodynamic state of the feedstock to prevent denaturation processes is difficult to achieve on an industrial scale. The method does not allow continuous production of several collagen fractions for the food industry. The use of low temperatures in the processing of raw materials is very energy intensive. The application of this method is not technologically advanced for the organization of continuous large-tonnage production of collagen for the food industry.

SUMMARY OF THE INVENTION

The present invention provides a method that allows you to expand the range of collagen collagen products, including the so-called fibrous collagen for food applications, while eliminating the above disadvantages of the known method due to the fact that the raw material is used as a split split of cattle skins, alkaline peroxidation is carried out within 2-6 hours when the ratio of the mass of the solution and the mass of the split is not less than 1.3 and the content of sodium hydroxide in the processed mixture of the solution and split does not less than 15 g / l and hydrogen peroxide 5.2-8.5 g / l, the treated split is washed with running water until the pH drops to 10-11, after which the split is neutralized with citric acid for 2-6 hours to pH the split is 5.0-8.0, and after drying and grinding, the resulting dried and ground material is ground to a particle size of 50 to 1200 μm, followed by fractionation of the ground material.

Food collagen must meet the general requirements for food purity and safety. The method should provide the necessary purity of the final product and the absence of the risk of infection with transmissible spongiform encephalopathy of cattle.

The requirements for animal raw materials and methods of processing them for the production of gelatin and collagen, which ensure safety, are established by law, including the EU Directives. To meet these requirements, collagen raw materials must be subjected to chemical cleaning procedures for ballast impurities, as well as to decontamination procedures by microorganisms and pathogenic prions.

The basis of the present invention is the creation of an improved method for processing collagen raw materials, which allows to obtain a safe and high-quality final product with minimal production costs.

The problem is solved as follows:

The bovine cattle split is subjected to alkaline peroxidation, intensive washing with water, followed by neutralization with acid and final washing, and alkaline peroxidation is carried out for 2-6 hours at a solution: split ratio of at least 1.3 and sodium hydroxide content the processed mixture of the solution and the split is at least 15 g / l and hydrogen peroxide 5.2-8.5 g / l, and the neutralization of the split is carried out with citric acid for 2-6 hours to a pH of 5.5 -8.0.

The resulting cattle cleavage, suitable for producing collagen powder from it, is mainly the reticular part of the dermis with a pH of 12-13, which is largely loosened during the ashen process, containing, by dry matter, about 90% protein and small amount the amount of fat, about one weight percent.

The glue split also contains residues of the reagents used in the gelling: calcium hydroxide, sodium sulfide, surfactants.

The essence of the invention lies in the fact that the cattle strips after zollenie, curing and doubling are subjected to a short alkaline-alkaline treatment at a temperature optimal for soaking-ash processes, intensive washing with running water, neutralization with citric acid and finishing washing with drinking water.

The processing time and component content are determined by several factors:

1. The content of sodium hydroxide in the reaction medium should be at least 15 g / l, pH at least 12, processing time at least 2 hours. This mode reduces the risk of contamination by pathogenic prions to an acceptable level. Relatively low alkali content and short processing time maximally preserves the native collagen structure, avoids protein loss, and at the same time provides a fairly effective cleaning of ballast substances.

2. The content of peroxide and methods of dosing it are determined by the features of mass transfer processes in the equipment used. When carrying out the processing of a split split in industrial drums or mixers with a capacity of 2-8 tons of raw materials during rotation at a speed of 2-4 rpm, the peroxide content in the reaction medium should be 5.2-8.5 g / l. Such a peroxide content in the presence of sodium hydroxide provides sufficient loosening of the collagen structure, improved diffusion of components and effective removal of impurities.

3. The ratio of the mass of the solution and the mass of the processed raw materials (LC) is also determined by the mass transfer characteristics of the equipment used. For liquid processes in the leather industry, carried out in drums or mixers, LCD 1.3-1.5 is traditionally used. This coefficient allows the efficient use of equipment and at the same time provides the necessary mass transfer.

4. Intensive rinsing with water is ensured by the flow regime of water supply during rotation of the drum (mixer). The duration of washing is determined by the mass transfer characteristics of the equipment used. The main purpose of the flushing at this stage is the maximum reduction in the concentration of ballast substances, including calcium hydroxide, as well as the maximum reduction in the concentration of sodium hydroxide before subsequent neutralization. The pH range after washing is 10.2-10.8.

5. Neutralization can be carried out with citric acid in the form of a solution, or by loading the calculated amount of dry citric acid into the reaction medium. Depending on the mass transfer characteristics of the equipment used, the duration of neutralization is from 2 to 6 hours. Achieving a pH of 5.5-8.0 in the reaction medium allows us to conclude that the recharging of amino groups in collagen is complete.

6. The final rinse with drinking water is carried out in flow mode. The purpose of washing is to remove soluble salts and suspensions to the maximum.

7. Grinding the washed split with moisture up to 70% to a granule size of 8 mm.

8. Drying the granules to a moisture content of 10-15% at a temperature of 40-70 ⁰ C. Preferably, the drying is carried out using microwave radiation (microwave) under reduced pressure from 5 to 10 mbar.

9. Grinding granules in a grinder, particle size 0.5-1 mm.

10. Grinding and drying to a moisture content of 8%, fractionation, particle size from 50 microns to 1200 microns.

The product thus obtained is characterized by a high protein content, low content of impurities (ash and fat), sufficient thermal stability, is white to light cream in color, odorless or has a very weak characteristic odor, the native collagen structure is preserved.

Table 1

Characteristics of the collagen obtained according to the invention

No. Indicators
one Color White 2 Smell Neutral 3 Moisture content,%, no more 8.0 four pH 5% extract 7.1 5 Protein content (in terms of solids),%, not less than (N * 6.25) 99.0 6 Fat content (in terms of solids),%, no more 1,0 7 Ash content (in terms of solids),%, no more 2.0 8 The content of heavy metals (in terms of solids), mg / kg
1,5 9 The chromium content (in terms of solids), mg / kg Not found

Examples of the method according to the invention

Examples 1-3 were carried out with the parameters shown in Table 2. Otherwise, the examples were carried out as follows:

After gilding, the skins of cattle were mezdril and the front layer was separated in dairy machines. The resulting goal split was cut into large pieces of approximately 50x50 cm.

The cut split was loaded into the drum and treated with a peroxide-alkaline solution for a certain period while rotating at a constant speed. In the examples, various ratios of the mass of the solution and the mass of the split (“FA”) were used, as well as various amounts of sodium hydroxide and hydrogen peroxide in the filled solution.

After treatment, the peroxide-alkaline solution was drained and the split was washed with running water at a drum rotation speed of 4 rpm for about an hour.

The washed goblet was neutralized with citric acid at a drum rotation speed of 2 rpm until neutralization (pH 5.5-8.0) for approximately three hours. The neutralized intermediate was washed with running water for approximately half an hour at a drum rotation speed of 4 rpm. Water was allowed to drain as much as possible and the peeled split was unloaded into transport containers.

The prepared split was ground, the obtained granules were dried, crushed, fractionated and packaged depending on the particle size of the fractions.

Fractionation was carried out on a sieve with a mesh size of 600 μm or first on a sieve with a mesh size of 600 μm, and then on a sieve with a mesh size of 250 μm. Thus, two fractions were obtained - up to 600 μm and more than 600 μm, or three fractions - up to 250 μm, 250-600 μm and more than 600 μm (usually in the range of 600-1200 μm).

The resulting food collagen fractions with different particle sizes met the food safety requirements and had a protein content of at least 99%.

table 2

The parameters of the method according to the invention used in examples 1-3

Example 1 Example 2 Example 3 LCD 1.3 LCD 1.5 LCD 2.5 The concentration of sodium hydroxide in a mixture of 13 g / l The concentration of sodium hydroxide in a mixture of 20 g / l
The concentration of sodium hydroxide in a mixture of 25 g / l The concentration of hydrogen peroxide in a mixture of 5.2 g / l The concentration of hydrogen peroxide in a mixture of 7.0 g / l The concentration of hydrogen peroxide in a mixture of 8.5 g / l PH values after neutralization
pH 5.2 PH values after neutralization
pH 7.0 PH values after neutralization
pH 8.0 Peroxide-alkaline treatment time
6 o'clock Peroxide-alkaline treatment time
4 hours Peroxide-alkaline treatment time
2 hours Total time of receipt of the finished product
16 hours Total time of receipt of the finished product
14 hours Total time of receipt of the finished product
12 hours The output of the finished (ASV),% -89.9 The output of the finished (ASV),% -92.1 The output of the finished (ASV),% -91.0

Table 3

Characteristics of collagen products obtained according to examples 1-3

Example 1

The microstructure of finished products: the native structure of collagen
Microbiological purity:
The number of mesophilic aerobic and facultative anaerobic microorganisms, CFU / g - not found
E. coli bacteria (coliforms) - not detected
Pathogenic (including salmonella) - not detected
Mass fraction of moisture,%, 5.6
Mass fraction of protein (a.s.v.),% - 98.8
Mass fraction of fat (a.s.w.),% -0.7
Mass fraction of ash (a.s.v.),% - 0.5
The content of toxic elements - in accordance with TR TS 021/2011 Example 2

The microstructure of finished products: the native structure of collagen
Microbiological purity:
The number of mesophilic aerobic and facultative anaerobic microorganisms, CFU / g - not found
E. coli bacteria (coliforms) - not detected
Pathogenic (including salmonella) - not detected
Mass fraction of moisture,%, 5.6
Mass fraction of protein (a.s.w.),% - 99.2
Mass fraction of fat (a.s.w.),% -0.4
Mass fraction of ash (a.s.v.),% - 0.3
The content of toxic elements - in accordance with TR TS 021/2011 Example 3

The microstructure of finished products: the native structure of collagen
Microbiological purity:
The number of mesophilic aerobic and facultative anaerobic microorganisms, CFU / g - not found
E. coli bacteria (coliforms) - not detected
Pathogenic (including salmonella) - not detected
Mass fraction of moisture,%, 5.6
Mass fraction of protein (a.s.w.),% - 99.5
Mass fraction of fat (a.s.w.),% -0.2
Mass fraction of ash (a.s.v.),% - 0.3
The content of toxic elements - in accordance with TR TS 021/2011

Table 4

Comparison of the prior art method with the method of the invention

The method according to the patent of the Russian Federation 2551195 The method according to the invention The period of receipt of the finished product - 70-72 hours The period of receipt of the finished product - 13 hours Yield (a.s.v.) - 84% Output (a.s.v.) - 90% Mass fraction of protein (a.s.w.) -96% Mass fraction of protein (a.s.w.) -99.5% Product Type:
Particle size powder
up to 500 microns Product Type:
1st fraction - powder, particle size up to 250 microns;
2nd fraction - powder, particle size from 250 to 600 microns;
3rd fraction - fiber, particle size over 600 microns

The obtained collagen fractions were used as a structure-forming and stabilizing protein ingredient in the production of minced meat products (cooked sausages, ham, semi-smoked, cooked smoked, raw smoked, liver and blood sausages, pastes, semi-finished products and canned food), as well as boiled, smoked-boiled, boiled-smoked, baked, smoked-baked) to obtain the following technical results:

- improving the functional and technological properties of raw meat (increasing the pH value, increasing the proportion of soluble protein, increasing the moisture-binding and gel-forming abilities);

- reduce thermal losses, increase the yield of finished products, reduce costs;

- Improvement of structural and mechanical characteristics, including density and solidity of the finished product;

- improving the organoleptic characteristics of the product, including improving the consistency;

- improving the stability of consumer characteristics of finished products during storage;

- reduce the risk of marriage associated with the appearance of broth-fat edema, separation of moisture from the product in a vacuum package.

- reducing calories;

- facilitate removal of the shell and improve the cutability of the finished product.

The collagen protein fractions of the invention are preferably used with meat raw materials with normal or reduced functional properties (PSE meat, thawed raw materials, mechanically deboned meat, etc.)

Table 5

Functional and technological characteristics of collagen fractions obtained in examples 1-3

Name of indicator
The value of indicators Particle Size ≤250 μm Particle size
250-600 μm Particle size
≥ 600 μm Water binding capacity
in cold water
in hot water
1: 9
1:20
1: 8
1:14
1: 6
1:13 Fat emulsifying ability 1: 9: 10 1: 7: 8 1: 5: 6 Gelling ability 1: 9 1: 8 1: 5 Solubility*
in cold water


in hot water
++
light precipitate
+++
a small amount of flocculent
foam
++
light precipitate
+++
cereal foam
+
sediment

+
flocculent sediment

* Note: + low solubility; ++ satisfactory solubility; ++ good solubility; +++ high solubility.

The main stages of meat production using collagen fractions correspond to generally accepted technological schemes and are carried out in accordance with the current regulatory and technical documentation approved in the established manner.

In the manufacture of all types of minced meat products, collagen fractions can be used independently or in exchange for parts of raw meat.

Depending on the assortment of manufactured meat products and production conditions, collagen powders and fibrous collagen are used:

- when salting meat raw materials;

- during the extrusion and massaging of raw meat in the composition of brines;

- when making minced meat in hydrated form, in the form of gels, emulsions and granules, in dry form.

Table 6

The use of powdered and fibrous collagen according to the invention in various types of meat products

Group
homogeneous products Recommended amount of collagen powder
kg per 100 kg of basic raw materials Cooked sausages, ham products 0.5-2.0 Smoked and cooked smoked sausages 0.5-1.0 Chopped semi-finished products 0.5-1.5 Raw sausages 0.3-0.7

Claims (19)

1. A method of obtaining food collagen from waste leather raw materials, including peroxidation treatment of the specified raw materials, washing the processed raw materials with running water, drying and grinding the dried material, characterized in that as a raw material use a glue split of cattle skins, The alkaline peroxidation treatment of the split is carried out for 2-6 hours at a ratio of the mass of the solution and the mass of the split of at least 1.3 and the sodium hydroxide content in the processed mixture of the solution and split of at least 15 g / l and hydrogen peroxide of 5.2-8.5 g / l the treated split is washed with running water until the pH drops to 10-11, after which the split is neutralized with citric acid for 2-6 hours to a pH of 5.0-8.0, and after drying and grinding, the resulting dried and ground material grind to a particle size of from 50 to 1200 μm, followed by fractionation of the crushed material into at least two fractions, of which the fraction with a smaller particle size is powdered collagen, and the fraction with a larger particle size is fibrous collagen. 2. The method according to claim 1, characterized in that before peroxide-alkaline treatment, the split heels are cut into pieces. 3. The method according to claim 1, characterized in that prior to the peroxo-alkaline treatment, the glued split is washed with running water for 15-20 minutes. 4. The method according to claim 1, characterized in that the neutralized split is subjected to grinding before drying, and the grinding of the dried material is carried out by heating at a temperature of 40-70 ° C to a moisture content of 10-15%. 5. The method according to claim 1, characterized in that the moisture removal on the drying unit occurs using microwave radiation under reduced pressure to completely disinfect the product. 6. The method according to claim 1, characterized in that the moisture removal is achieved by the coolant in a convective drying installation under vacuum, which allows you to save the native collagen structure. 7. The method according to claim 1, characterized in that the washing of the split after peroxide-alkaline treatment to lower the pH of the split is carried out for 0.5-2 hours 8. The method according to claim 1, characterized in that the milled material is fractionated on at least one sieve to obtain at least two fractions of the milled material. 9. The method according to claim 1, characterized in that fractions with a particle size of less than 600 microns are used as powdered collagen, and fractions with a particle size of 600 microns or more are used as fibrous collagen. 10. Powdered food collagen obtained by the method according to any one of claims 1 to 9. 11. Fibrous food collagen obtained by the method according to any one of claims 1 to 9. 12. A method of manufacturing meat products, which prepare a composition for the manufacture of minced sausage products or a functional mixture used in minced meat products on their own or instead of part of the meat raw materials, which use the powdered collagen of claim 10. 13. The method according to item 12, in which the particle size of the specified powdered collagen is in the range of 250-600 microns. 14. The method according to item 12, in which in the manufacture of smoked or raw smoked sausage or brine for the extrusion of meat products using powdered collagen with a particle size of up to 250 microns. 15. A method of manufacturing meat products, in which a composition is prepared to obtain a chopped semi-finished product, which uses fibrous collagen according to claim 11.  16. The method according to clause 15, in which the particle size of the specified fibrous collagen is in the range of 600-1200 microns.