WO2017006926A1 - 乳製品 - Google Patents
乳製品 Download PDFInfo
- Publication number
- WO2017006926A1 WO2017006926A1 PCT/JP2016/069859 JP2016069859W WO2017006926A1 WO 2017006926 A1 WO2017006926 A1 WO 2017006926A1 JP 2016069859 W JP2016069859 W JP 2016069859W WO 2017006926 A1 WO2017006926 A1 WO 2017006926A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- milk
- protein
- dairy product
- amino acid
- acid sequence
- Prior art date
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Images
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
- A23C9/127—Fermented milk preparations; Treatment using microorganisms or enzymes using microorganisms of the genus lactobacteriaceae and other microorganisms or enzymes, e.g. kefir, koumiss
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C19/00—Cheese; Cheese preparations; Making thereof
- A23C19/02—Making cheese curd
- A23C19/032—Making cheese curd characterised by the use of specific microorganisms, or enzymes of microbial origin
- A23C19/0325—Making cheese curd characterised by the use of specific microorganisms, or enzymes of microbial origin using yeasts, alone or in combination with lactic acid bacteria or with fungi, without using other bacteria
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C19/00—Cheese; Cheese preparations; Making thereof
- A23C19/02—Making cheese curd
- A23C19/032—Making cheese curd characterised by the use of specific microorganisms, or enzymes of microbial origin
- A23C19/0326—Rennet produced by fermentation, e.g. microbial rennet; Rennet produced by genetic engineering
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C19/00—Cheese; Cheese preparations; Making thereof
- A23C19/02—Making cheese curd
- A23C19/055—Addition of non-milk fats or non-milk proteins, polyol fatty acid polyesters or mineral oils
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
- A23C9/1203—Addition of, or treatment with, enzymes or microorganisms other than lactobacteriaceae
- A23C9/1209—Proteolytic or milk coagulating enzymes, e.g. trypsine
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
- A23C9/123—Fermented milk preparations; Treatment using microorganisms or enzymes using only microorganisms of the genus lactobacteriaceae; Yoghurt
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING OR TREATMENT THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
- A23C9/13—Fermented milk preparations; Treatment using microorganisms or enzymes using additives
- A23C9/1322—Inorganic compounds; Minerals, including organic salts thereof, oligo-elements; Amino-acids, peptides, protein-hydrolysates or derivatives; Nucleic acids or derivatives; Yeast extract or autolysate; Vitamins; Antibiotics; Bacteriocins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/58—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
Definitions
- the present invention relates to a dairy product having a new texture and a method for producing the same.
- Dairy products can be either liquid or solid.
- Known solid dairy products include cheese and fermented milk (such as yogurt). Yogurt becomes solid as a result of lactic acid fermentation.
- cheese becomes solid due to the action of rennet (an enzyme produced in the stomach of mammals), which is a curdling enzyme, on casein (Patent Document 1).
- rennet an enzyme produced in the stomach of mammals
- Patent Documents 1 and 2 Also known as rennet are microorganism-derived and gene recombinants
- JP 2004-33093 A Japanese Patent Publication No. 2-18834
- dairy products coagulated with rennet have a problem that bitterness occurs.
- yogurt by lactic acid fermentation is often not solid enough, and in consideration of shape retention during distribution and storage, commercially available yogurt may contain a thickener or gelling agent. is there. Therefore, development of a new dairy product having a certain hardness and good flavor is desired.
- the present inventor has predicted that a microorganism belonging to the genus Trichoderma is produced, and a protein whose analog sequence is only predicted and its analogs. It has been found that fermented milk obtained by fermenting together with lactic acid bacteria and yeast has excellent curdling action, has a cheese-like hardness, has no bitter taste, and has a good flavor. The present invention has been completed.
- the present invention provides the following [1] to [8].
- a dairy product comprising a milk-derived raw material containing casein and a protein comprising an amino acid sequence having an identity of 90% or more with the amino acid sequence represented by SEQ ID NO: 1.
- a coagulation component comprising a thickener, a stabilizer, a gelling agent, and a paste.
- a protein comprising an amino acid sequence having 90% or more identity with the amino acid sequence shown in SEQ ID NO: 1 and a lactic acid bacterium are added to a milk-derived raw material containing casein and fermented A method for producing dairy products.
- a dairy coagulant emulsion comprising a protein comprising an amino acid sequence having 90% or more identity with the amino acid sequence represented by SEQ ID NO: 1.
- the dairy product of the present invention has cheese-like hardness and good flavor, and is useful as a dairy product with a new texture.
- the hardness of the dairy product of the present invention can be produced in a range that is harder than conventional yogurt and softer than conventional cheese. it can.
- the temperature dependency of the GODO-TCF-derived protease (SEQ ID NO: 1) is shown.
- 2 shows temperature stability of a GODO-TCF-derived protease (SEQ ID NO: 1).
- 1 shows the pH stability of a GODO-TCF-derived protease (SEQ ID NO: 1).
- 1 shows the pH dependency of a GODO-TCF-derived protease (SEQ ID NO: 1).
- action with respect to casein of each enzyme in pH5.5 is shown.
- the coagulability of the pH adjusted milk by GODO-TCF is shown.
- a protein derived from a microorganism belonging to the genus Trichoderma is preferable as the protein having an amino acid sequence having 90% or more identity with the amino acid sequence represented by SEQ ID NO: 1 used in the dairy product of the present invention. More specifically, a predicted protein of unknown function derived from Trichoderma reesei QM6a (available bacteria described in NCBI) (100% identical to the amino acid sequence shown in SEQ ID NO: 1), a commercially available cellulase GODO-TCF derived from Trichoderma reesei A hypothetical protein TRIVIDRAFT — 215801 derived from Trichoderma virens Gv29-8 (available bacteria described in NCBI) (94% identical to the amino acid sequence shown in SEQ ID NO: 1) Same: SEQ ID NO: 2), vacuolar protein A derived from Trichoderma atroviride (92% identical to amino acid sequence shown in SEQ ID NO: 1): vacuolar protein derived from Trichoderma aureoviride (amino acid sequence shown in
- a more preferred protein is a protein having 92% or more identity with the amino acid sequence represented by SEQ ID NO: 1, more preferably a protein having 93% or more identity, and further preferably 94% identity.
- the above protein more preferably a protein having the above-mentioned identity of 95% or more.
- the protein used in the present invention may be extracted from a microorganism belonging to the genus Trichoderma or may be produced by a genetic recombination technique.
- the protein includes a protein to which sugar is bound.
- the protein used in the present invention has casein degrading activity, it has protease activity.
- the degradation activity for ⁇ -casein is high, and the degradation activity for ⁇ -casein and ⁇ -casein is weaker than that for ⁇ -casein.
- the protein degrades ⁇ -casein contained in milk-derived raw materials with a slight addition amount. As a result, ⁇ -casein (including degradation products) and ⁇ -casein (including degradation products) aggregate to increase the hardness of the dairy product.
- the protein may be a purified one, or a culture (including a culture solution) of a microorganism belonging to the genus Trichoderma containing the protein, an extract of the culture, or the like.
- a culture including a culture solution
- the cellulase GODO-TCF may be used as it is.
- the milk-derived raw material containing casein used in the dairy product of the present invention may contain casein, and examples thereof include liquids and powders such as milk, goat milk, sheep milk, horse milk, and breast milk. . What is necessary is just to use what mixed with water etc. when using milk powder.
- the milk includes raw milk, low-fat milk, non-fat milk, and processed milk.
- the content of the protein contained in the dairy product of the present invention may be any amount that exhibits curdling activity. Whether to exhibit curdling activity varies depending on the type of milk-derived raw material used, the amount of casein contained in the milk-derived raw material, the production conditions (reaction time, reaction temperature, reaction pH, etc.), and the like. For this reason, the content of the protein cannot be generally specified.
- the curdling activity (casein degrading activity) of the protein when added to a milk-derived raw material is in the range of 20 U to 300 U per 100 g of milk raw material, It becomes easy to obtain the hardness of dairy products that has never existed before. The presence or absence of casein degradation can be confirmed by analyzing the obtained dairy product by SDS-PAGE or the like.
- the acidic protease activity of the protein contained in the dairy product of the present invention is preferably 3000 U or less per 100 g of milk raw material. If the value is exceeded, the flavor of the dairy product may be deteriorated.
- the dairy product of the present invention preferably further contains lactic acid bacteria or yeasts from the viewpoint of flavor and texture. Since the dairy product using the protein and lactic acid bacteria in combination is harder than conventional fermented milk, the dairy product of the present invention more preferably contains lactic acid bacteria.
- lactic acid bacteria belonging to the genus Lactobacillus, Bifidobacterium, Enterococcus, Lactococcus and Leuconostoc can be used as the lactic acid bacteria.
- the content of lactic acid bacteria in the dairy product of the present invention is not particularly limited, but is preferably 1 million / 1 mL or more, more preferably 5 million / 1 mL or more, and further preferably 10 million / 1 mL or more.
- the dairy product of the present invention can be blended with other sweeteners such as syrup and other various food materials, for example, various sugars, emulsifiers, various vitamins and the like, if necessary.
- sugars such as sucrose, glucose, fructose, palatinose, trehalose, lactose, xylose, maltose, sugar alcohols such as sorbitol, xylitol, erythritol, lactitol, palatinit, reduced starch syrup, reduced maltose starch syrup, aspartame, thaumatin , Sucralose, acesulfame K, high-sweetness sweeteners such as stevia, sucrose fatty acid esters, glycerin fatty acid esters, polyglycerin fatty acid esters, sorbitan fatty acid esters, emulsifiers such as lecithin, milk fats such as cream, butter and sour cream, citric acid Acids such
- the dairy product of the present invention has sufficient hardness due to the curdling action of the protein, it is not necessary to contain a coagulation component such as a thickener, a stabilizer, a gelling agent, a paste, and the like. Preferably not.
- the dairy product of the present invention is produced by blending the milk-derived raw material and the protein and curdging, or by blending the milk-derived raw material, the protein and lactic acid bacteria or yeast, and producing according to a normal method for producing fermented foods can do.
- a method for producing a fermented food a method in which the milk-derived raw material and the protein are blended, inoculated with lactic acid bacteria or yeast, cultured, homogenized, and then added with optional components such as syrup, flavor, and the like Is mentioned.
- the dairy product obtained according to the present invention has a unique texture that it has a solidity higher than that of solid yogurt, without adding a thickener, etc., and has a good taste with no bitterness. .
- Such a texture is a characteristic effect of the protein.
- the breaking stress in the 2-byte method is 5500 Pa or more, and the fracture adhesion is preferably 800 J / m 3 or more from the viewpoint of texture, and the breaking stress is more preferably 5500 to 12000 Pa, The adhesion is more preferably 800 to 1200 J / m 3 .
- dairy product of the present invention include fermented milk, cheese, ice cream, ice milk, and lact ice, with fermented milk and cheese being more preferred. Furthermore, as fermented milk, the form of solid yogurt is particularly preferable.
- the protein is useful as a coagulation emulsion for dairy products because it acts on casein and exhibits a coagulation action.
- Production Example 1 (1) (Separation of protease from GODO-TCF) 100 mL of GODO-TCF (manufactured by Godo Shusei Co., Ltd., Trichoderma reesei QM6a) was concentrated to about 50 mL with UF pencil type module API-0013 (molecular weight cut off 6000), and 150 mL of 20 mM MES buffer (pH 6. 0) was added. This procedure was repeated 4 times. The resulting concentrate is applied to a Giga Cap Q-650M (TOYOPEARL) column equilibrated with 20 mM MES buffer (pH 6.0) and contains curdling activity eluted with a linear gradient of 0-0.5 M NaCl.
- TOYOPEARL Giga Cap Q-650M
- PCR primer 5′-tacaagaggctggtttcctagcttcgtc-3 ′ (Forward: SEQ ID NO: 4), 5′-taggactgtctttccgctctcaactgc-3 ′ (Reverse: SEQ ID NO: 5) is designed as M
- the target gene was amplified using EX Taq (TaKaRa) using as a template.
- the amplified DNA fragment of about 1600 bp was excised, purified using FastGene Gel / PCR Extraction (Nippon Genetics), DNA sequence information was obtained, and amino acid sequence was determined by a translation program.
- the obtained amino acid sequence was shown as SEQ ID NO: 1.
- the amino acid sequence was 100% identical with the amino acid sequence of Trihoderma reesei QM6a.
- the temperature stability is determined by incubating the enzyme solution at 4, 20, 30, 40, 50, 60, 70 for 2 hours and then diluting it twice with 100 mM MES buffer (pH 5.5, rt). The chymosin activity was measured according to the activity measurement method described above.
- the pH stability is determined by adjusting the enzyme solution to pH 3.0, 3.5, 4.0, 4.5, 5.0, 5.5, 6.0, 6.5, 7.2, 7.5, 8.
- Each buffer of 0, 8.5, and 9.0 pH 3.0 to 6.0: 0.2M citric acid-Na citrate buffer, pH 6.0 to 8.0: 0.2M phosphoric acid-Na phosphate buffer , PH 7.2 to 9.0: Tris-HCl buffer
- pH 3.0 to 6.0 0.2M citric acid-Na citrate buffer
- pH 6.0 to 8.0 0.2M phosphoric acid-Na phosphate buffer
- PH 7.2 to 9.0 Tris-HCl buffer
- the pH dependency was evaluated by the acid-soluble peptide release activity method.
- a substrate solution 1.2 g of milk casein (CALBIOCHEM) was weighed, 20 mL of distilled water and 20 mL of 0.1 M Tris solution were added and dissolved, and heated in a boiling bath at 60 ° C. for 10 minutes. Thereafter, 500 mM of each buffer (pH 3.0 to 6.0: 0.2 M citric acid-Na citrate buffer, pH 6.0 to 8.0: 0.2 M phosphoric acid-Na phosphate buffer, pH 7.2 to 9 0.0: Tris-HCl buffer) was added to each pH with 1N hydrochloric acid or sodium hydroxide, and the volume was adjusted to 200 mL with distilled water.
- each buffer pH 3.0 to 6.0: 0.2 M citric acid-Na citrate buffer, pH 6.0 to 8.0: 0.2 M phosphoric acid-Na phosphate buffer, pH 7.2 to 9 0.0: Tris-HCl buffer
- reaction 0.5 mL of the enzyme solution was pre-incubated at 50 ° C. for 3 minutes, 2.5 mL of the substrate solution was added and stirred well, and the reaction was performed at 50 ° C. for 10 minutes. Thereafter, 1.8 g of trichloroacetic acid, 11.45 g of acetic anhydride and 21 mL of acetic acid were mixed, 2.5 mL of a precipitation reagent adjusted to 1 L with distilled water was added, and the mixture was allowed to stand at room temperature for about 5 minutes. Thereafter, ADVANTEC No.
- the absorbance of the filtrate filtered through 4A filter paper was measured at 275 nm, and the amount of enzyme that produced an acid-soluble low molecular weight degradation product corresponding to 1 ⁇ g of tyrosine per minute was defined as 1 unit, and the activity value was calculated. .
- FIG. 1 shows temperature dependency of the protease derived from GODO-TCF (protease shown in SEQ ID NO: 1)
- FIG. 2 shows temperature stability
- FIG. 3 shows pH stability
- FIG. 4 shows pH dependency.
- . 1 to 4 the GODO-TCF-derived protease showed the maximum activity around 60 ° C., and maintained a residual activity of 80% or more at pH 3.5 to 6.5 and 60 ° C.
- the pH dependence it is estimated that the drims pH of chymosin activity is more acidic than 5.5, whereas the acid-soluble peptide releasing activity is around pH 6.5.
- the GODO-TCF-derived protease has high specificity for ⁇ -casein at pH 5.5 (FIG. 5), but also acts on ⁇ , ⁇ -casein near pH 7.2 (FIG. 6). ). It was confirmed that chymosin has high specificity for ⁇ -casein and pepsin has a thin band as a whole. When comparing the GODO-TCF-derived protease with the other two proteases, it was found that the specificity of the GODO-TCF milk-clotting protease was ⁇ -casein> ⁇ -casein.
- Example 1 The pH was adjusted to 5.9 with 10% lactic acid in 10 mL of milk. Next, 0.1 mL (1%) of GODO-TCF and 0.9 mL of sterilized water or 1 mL (10%) were added to 10 mL of this milk, and the mixture was allowed to stand at 43 ° C. for 60 minutes.
- GODO-TCF was diluted 4 times with distilled water and then heated at 100 ° C. for 120 minutes.
- 0.4 mL (1% in terms of pre-dilution conversion) of GODO-TCF and heat-treated after dilution and 0.6 mL of sterilized water were added.
- Example 2 10 g of milk (delicious milk, manufactured by Meiji Dairies) was weighed into a 15 mL assist tube, 0.2 g (2%, w / w) of skim milk was added and stirred well to dissolve, boiled in boiling water for 5 minutes and sterilized. Thereafter, the cooled milk was preincubated by boiling at 43 ° C., and 0.1 mL (1%, w / v) of TCF sterilized by 0.2 ⁇ m filter filtration in a clean bench and 0.3 mL of sterile MilliQ water were aseptically added.
- milk delicious milk, manufactured by Meiji Dairies
- a solution diluted with MilliQ water 4 times and added with 1.2 mL of TCF boiled in boiling water for 2 hours and a solution added with 1.2 mL of sterile MilliQ water were prepared. Thereafter, 0.5 g (5%, w / w) of a starter (Bulgarian yogurt, manufactured by Meiji Dairy Cow) was aseptically added to each tube in a clean bench, and gently agitated by inversion 2-3 times. Seven samples were prepared for each sample, and fermentation was stopped every hour from immediately after the starter was added to 6 hours later, and the pH was measured.
- Example 3 Weigh 55.8 g of milk (delicious milk, manufactured by Meiji Dairies) into a jam bottle (Jam 90ST, Toyo Glass Co., Ltd.), add 1.2 g (2%, w / w) of skim milk, dissolve well, and dissolve in boiling water. Boiled for 5 minutes and sterilized. Thereafter, the cooled milk was preincubated at 43 ° C., and 6 mL (1%, w / v) of GODO-TCF sterilized by filtration with a 0.2 ⁇ m pore size filter in a clean bench was aseptically added.
- Hardness Maximum load when a load is applied. For semi-solid foods, the stress is divided by the jig cross-sectional area.
- Brittleness B
- Adhesive strength C
- Adhesiveness A3: The amount of whether it is difficult to be separated when it has adhesiveness.
- Cohesiveness (A2 / A1) ratio of compression energy of the first stroke to the second stroke, deformation amount.
- Elasticity T2 / T1: The ratio of the first stroke to the second stroke of the amount of change up to the maximum peak. Gum properties (hardness ⁇ cohesiveness): The higher the value, the harder and more rubbery. Chewing (hardness ⁇ cohesiveness ⁇ elasticity): It can be said that the higher the value, the more energy is required for chewing.
- the GODO-TCF-added sample had a break point increased by 0.03 N and the fracture strain ratio decreased by 4.4% compared to the sample without additive (FIG. 9, Table 1).
- the maximum stress at the time of surface compression [1], [3]
- the cohesiveness and adhesion [2]
- the stress at break increased in the GODO-TCF added sample ([4]).
- the waveform representing the breaking stress inside the card ([5], [7]) was relatively smooth in the sample added with GODO-TCF, while several break points were confirmed in the sample without additive. Furthermore, in the cohesiveness and adhesion ([6], [8]), the sample with GODO-TCF was higher than the sample without addition. In the waveform of the adhesion ([6], [8]) at the time of drawing, it was found that the sample added with GODO-TCF was pulled out smoothly, whereas the waveform without addition was disordered and resistance was applied.
- Example 4 According to the fermented milk preparation method of Example 3, fermented milk samples were prepared on a 200 g scale. Sumiteam C (manufactured by Shin Nippon Kagaku Kogyo Co., Ltd.) was diluted with the chymosin activity method described in Production Example 1 (3) so as to have chymosin activity equivalent to that of GODO-TCF. As for Blank, 0.6 mL (1%) of 50 mM citrate buffer (pH 5.2, rt) was added. As the analyzer, a taste recognition device TS-5000Z (Insent) was used. As the sample for taste sensor analysis, a fermented milk sample diluted twice (w / w) with purified water was used. As a control for analysis, a Bulgarian yogurt (Meiji) diluted in the same manner was used. The sensor used for the analysis was a blend membrane, a plus membrane, a minus membrane, and GL1 (sweetness sensor).
- the results of taste sensor analysis are shown in Table 2. Each analysis value is shown as a relative value based on the analysis value of Bulgarian yogurt.
- sweetness and bitter taste were reduced as compared with the sample added with control, 0.1% GODO-TCF, and citrate buffer.
- the sample added with 0.1% GODO-TCF had almost the same result as the sample added with citrate buffer.
- the bitter taste and general bitterness of the Sumiteam C added sample increased. From the above results, it was found that, except for the influence of salts and buffer components, taste changes other than bitter taste and sweet taste do not occur. It was also found that even when GODO-TCF-derived protease is allowed to act on milk protein, bitterness is unlikely to occur.
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Abstract
Description
従って、一定の固さを有し、かつ風味の良好な新たな乳製品の開発が望まれている。
〔2〕前記タンパク質が、トリコデルマ属に属する微生物に由来するタンパク質である〔1〕記載の乳製品。
〔3〕さらに乳酸菌又は酵母を含む〔1〕又は〔2〕記載の乳製品。
〔4〕発酵乳又はチーズである〔1〕~〔3〕のいずれか1項に記載の乳製品。
〔5〕2バイト法における破断応力が5500Pa以上であり、破断付着性が800J/m3以上である〔1〕~〔4〕のいずれか1項に記載の乳製品。
〔6〕増粘剤、安定剤、ゲル化剤及び糊料からなる凝固成分を実質的に含有しない〔1〕~〔5〕のいずれか1項に記載の乳製品。
〔7〕カゼインを含有する乳由来原料に、配列番号1で示されるアミノ酸配列との同一性が90%以上であるアミノ酸配列からなるタンパク質と、乳酸菌とを添加し、発酵させることを特徴とする乳製品の製造方法。
〔8〕配列番号1で示されるアミノ酸配列との同一性が90%以上であるアミノ酸配列からなるタンパク質を含有する乳製品用凝乳剤。
より好ましいタンパク質は、配列番号1で示されるアミノ酸配列との同一性が92%以上のタンパク質であり、さらに好ましくは前記同一性が93%以上のタンパク質であり、さらに好ましくは前記同一性が94%以上のタンパク質であり、さらに好ましくは前記同一性が95%以上のタンパク質である。
前記タンパク質は、わずかな添加量で乳由来原料に含まれるκ-カゼインを分解する。これによって、α-カゼイン(分解物を含む)及びβ-カゼイン(分解物を含む)が凝集するため、乳製品の固さが増す。
カゼイン分解の有無は、得られた乳製品をSDS-PAGE等により分析することで確認することができる。
当該値を超えると、乳製品の風味が悪くなるおそれがある。
ここで乳酸菌としては、ラクトバシラス属、ビフィドバクテリウム属、エンテロコッカス属、ラクトコッカス属、リューコノストック属に属する乳酸菌を用いることができる。
本発明の乳製品は、前記タンパク質の凝乳作用により十分な固さを有するため、増粘剤、安定剤、ゲル化剤、糊料等の凝固成分を含有させる必要がなく、実質的に含有しないのが好ましい。
本発明乳製品の2バイト法における破断応力は5500Pa以上であり、破断付着性は800J/m3以上であるのが、食感の点で好ましく、さらに破断応力は5500~12000Paがより好ましく、破断付着性は800~1200J/m3がより好ましい。
(1)(GODO-TCFからプロテアーゼの分離)
GODO-TCF(合同酒精株式会社製、Trichoderma reesei QM6aの変異株)100mLを、UFペンシル型モジュールAPI-0013(分画分子量6000)にて約50mLまで濃縮し、150mLの20mM MES緩衝液(pH6.0)を加えた。この手順を4回繰り返した。
得られた濃縮物を、20mM MES緩衝液(pH6.0)にて平衡化したGiga Cap Q-650M(TOYOPEARL)カラムに供し、0-0.5M NaClのリニアグラジエントにより溶出した凝乳活性を含む画分を回収した。回収した活性画分に終濃度が0.5Mとなるように硫酸アンモニウム(以下、AS)を加えた後、0.5M ASを含む20mM MES緩衝液(pH6.0)にて平衡化したButyl-650M(TOYOPEARL)カラムに供し、0.5-0M ASのリニアグラジエントにより溶出した。その後、活性画分を回収し、Amicon UltraTM-30K(分画分子量30kDa)により濃縮後(4000×g、120分間)、0.15M NaClを含む20mM MES緩衝液(pH6.0)にて平衡化したHiprep 16/60Sephacryl S-200 HR カラム(GE Healthcare)に供し、活性画分を回収した。
当該活性画分をSDS-PAGEに供したところ、約33kDaに単一バンドを確認した。
(1)に記載した精製工程のButyl-650Mカラムクロマトグラフィーにより溶出した活性化画分を、SDS-PAGEに供し、約33kDaの目的酵素バンドを切り出した後、ペプチド断片の配列からMascot seachプログラムによりNCBInr データベースよりアミノ酸配列の相同性が高かったpredictedprotein[Trichoderma reesei QM6a]の遺伝子配列情報を取得した。取得した遺伝子情報を基に、PCRプライマー5‘-tacaaagaggctggttcctagcttcgtc-3‘(Foward:配列番号4)、5‘-taggactgtcttccgctctcaaactgc-3‘(Reverse:配列番号5)を設計し、Trichoderma reesei QM9414株のゲノムDNAを鋳型としてEX Taq(TaKaRa)を用いて目的遺伝子の増幅を行った。増幅した約1600bpのDNA断片を切り出し、FastGene Gel/PCR Extraction(日本ジェネティクス)を用いて精製し、DNA配列情報を取得し、翻訳プログラムによりアミノ酸配列を決定した。得られたアミノ酸配列を配列番号1として示した。当該アミノ酸配列は、Trihoderma reesei QM6aのアミノ酸配列と100%一致した。
(方法)
(1)に記載した精製工程中の、Butyl-650Mの活性溶出画分の酵素サンプルを使用した。温度依存性は、20、30、40、45、50、55、60、65℃でのキモシン活性を指標とした。キモシン活性測定は、国際標準法を一部改変した方法で行った。基質溶液はLow-heat,Low-fat spray dried milk powderを、11g/100mLの濃度で溶解し、CaCl2を終濃度が3mMになるように添加したのち、1規定塩酸にてpHを5.5に調整した。測定温度にてプレインキュベートした酵素液0.1mLに、同じくプレインキュベートした基質溶液5mLを加え、泡立てないように撹拌した。その後、各温度で反応を行いながら、約1分おきに試験管を傾け、壁面に凝乳が付着するかを確認し、初めて付着する時間を測定した。測定値既知の標準品と同時に測定し、それぞれの凝乳時間を調べ、活性値を算出した。
温度安定性は、酵素液を4、20、30、40、50、60、70にて2時間インキュベートした後、100mM MES buffer(pH5.5,r.t.)にて2倍希釈後の残存したキモシン活性を前記した活性測定法に準じて測定した。
pH安定性は、酵素液をpH3.0、3.5、4.0、4.5、5.0、5.5、6.0、6.5、7.2、7.5、8.0、8.5、9.0の各Buffer(pH3.0~6.0:0.2Mクエン酸-クエン酸Na buffer、pH6.0~8.0:0.2Mリン酸-リン酸Na buffer、pH7.2~9.0:Tris-HCl buffer)にて3倍希釈したものを、4℃で6時間静置した。その後、100mM MES buffer(pH5.5,r.t.)にて2倍希釈し、残存したキモシン活性を前記した活性測定法に準じて測定した。
pH依存性は、酸可溶性ペプチド遊離活性法により評価した。基質溶液は、ミルクカゼイン(CALBIOCHEM)を1.2g秤取し、蒸留水20mLと0.1MTris溶液を20ml加えて溶解させ、60℃、10分間沸騰浴中で加熱した。その後、500mMの各緩衝(pH3.0~6.0:0.2Mクエン酸-クエン酸Na buffer、pH6.0~8.0:0.2Mリン酸-リン酸Na buffer、pH7.2~9.0:Tris-HCl buffer)を100mL加え、1規定の塩酸または水酸化ナトリウムにて各pHに調整後、蒸留水にて200mLにメスアップし、調製した。反応は、酵素液0.5mLを50℃で3分間プレインキュベートし、基質溶液を2.5mL加えてよく撹拌し、50℃にて10分間反応を行った。その後、トリクロロ酢酸を1.8g、無水酢酸を11.45g、酢酸を21mL混合し、蒸留水にて1Lに調整した沈殿試薬を2.5mL加え、室温で5分程度放置した。その後、ADVANTECNo.4Aろ紙にて濾過した濾液を、275nmにおける吸光度を測定し、1分間に1μgのチロシンに相当する酸可溶性低分子分解物を生じる酵素量を1単位とし、活性値を算出した。。
(1)GODO-TCF由来プロテアーゼ(配列番号1で示されるプロテアーゼ)の温度依存性を図1に、温度安定性を図2に、pH安定性を図3に、pH依存性を図4に示す。図1~図4より、GODO-TCF由来プロテアーゼは、60℃付近で最大活性を示しpH3.5~6.5、60℃まで80%以上の残存活性を維持した。pH依存性では、キモシン活性の至滴pHは5.5より酸性側にあると推察されるのに対し、酸可溶性ペプチド遊離活性はpH6.5付近であることが分かる。
牛乳10mLに10%乳酸にてpHを5.9に調整した。次いで、この牛乳10mLにGODO-TCF 0.1mL(1%)と滅菌水0.9mL、又は1mL(10%)を添加し、43℃で60分静置した。一方、比較例としてGODO-TCF中のプロテアーゼ活性を失活させるため、GODO-TCFを蒸留水で4倍希釈後、100℃120分加熱処理した。pHを5.9に調整した牛乳に、希釈後加熱処理したGODO-TCFを0.4mL(希釈前換算で1%)と滅菌水を0.6mL添加した。
牛乳10g(おいしい牛乳、明治乳業製)を15mLアシストチューブに量り取り、スキムミルク0.2g(2%,w/w)を加えよく攪拌し溶解させ、沸騰水中にて5分間煮沸し、滅菌した。その後、冷却した牛乳を43煮沸でプレインキュベートし、クリーンベンチ内で0.2μmフィルターろ過滅菌したTCF0.1mL(1%,w/v)と、滅菌MilliQ水0.3mLを無菌的に添加した。コントロールとして、MilliQ水にて4倍希釈し、沸騰水中で2時間煮沸したTCF 1.2mLを添加したもの、および、滅菌MilliQ水1.2mLを添加したものを作成した。その後、クリーンベンチ内でスターター(ブルガリアヨーグルト、明治乳牛製)0.5g(5%,w/w)を各チューブに無菌的に添加し、2~3回静かに転倒攪拌した。各サンプルについてそれぞれ7本作成し、スターター添加直後から6時間後まで1時間ごとに発酵を停止し、pHを測定した。
(方法)
牛乳55.8g(おいしい牛乳、明治乳業製)をジャム瓶(ジャム90ST、東洋ガラス株式会社)に量り取り、スキムミルク1.2g(2%,w/w)を加えよく攪拌し溶解させ、沸騰水中にて5分間煮沸し、滅菌した。その後、冷却した牛乳を43℃でプレインキュベートし、クリーンベンチ内で孔径0.2μmフィルターにてろ過滅菌したGODO-TCF6mL(1%,w/v)を無菌的に添加した。Blankとして、50mM クエン酸緩衝液(pH5.2,r.t.)を0.6mL(1%)添加した。その後、クリーンベンチ内でスターター(ブルガリアヨーグルト、明治乳業製)3g(5%,w/w)を各チューブに無菌的に添加し、2~3回静かに転倒攪拌し、43℃にて4時間発酵を行った。発酵乳サンプルは、容器ごとテクスチャー分析に供した。
分析装置には、クリープメータ RE-33005C(山電)を用いた。破断強度解析は、治具No.3を用いて、4℃、アンプ倍率10倍、格納ピッチ750、測定歪率60%、測定速度10mm/sec、サンプル厚さ自動測定の条件で測定した。非破断条件におけるテクスチャー解析は、No.3を用いて、4℃、アンプ倍率10倍、格納ピッチ875、測定歪率5%、測定速度3mm/sec、戻り距離30mmサンプル厚さ自動測定の条件で測定した。破断条件におけるテクスチャー解析は、No.3を用いて、4℃、アンプ倍率10倍、格納ピッチ875、測定歪率50%、測定速度10mm/sec、戻り距離30mmサンプル厚さ自動測定の条件で測定した。
硬さ(H):負荷を与えた際の最大荷重。
半固形食品では治具断面積で割った応力になる。
脆さ(B):圧縮時、一部的に破壊が起こった時のその果汁の落ち込み量。
粘着力(C):圧縮後、戻りの引張時に粘着した最大負荷値。
半固形食品では治具断面積が考慮される。
付着性(A3):粘着性を持っている場合に引き離されにくいかどうかの量。
凝集性(A2/A1):1ストローク目と2ストローク目の圧縮エネルギーの比、変形量。
弾力性(T2/T1):最大ピークに至る変化量の1ストローク目と2ストローク目の比。
ガム性(硬さ×凝集性):値が高いほど硬く、ゴム的であるといえる。
そしゃく性(硬さ×凝集性×弾力性):値が高いほどそしゃくにエネルギーを要するといえる。
非破断のテクスチャー解析では(図10)、表面圧縮時の最大応力は([1]、[3])GODO-TCF添加サンプルが0.5N増加した。また、凝集性、付着性([2])に関してはGODO-TCF添加サンプルでは減少していた。
破断のテクスチャー解析では(図11)、GODO-TCF添加サンプルでは破断時の応力が増加した([4])。また、カード内部の破断応力を表す波形は([5]、[7])、GODO-TCF添加サンプルでは比較的なめらかであるのに対し、無添加サンプルでは破断点が数か所確認できた。さらに、凝集性、付着性では([6]、[8])GODO-TCF添加サンプルは無添加と比べ高かった。引き抜き時の付着性([6]、[8])の波形では、GODO-TCF添加サンプルはなめらかに引き抜かれるのに対し、無添加は波形が乱れ、抵抗がかかることが分かった。
(方法)
実施例3の発酵乳調整方法に準じて、200gスケールで発酵乳サンプルを調整した。スミチームC(新日本科学工業製セルラーゼ製剤)は、製造例1(3)に記載したキモシン活性法にて、GODO-TCFと同等のキモシン活性になるように希釈したものを用いた。Blankは、50mM クエン酸緩衝液(pH5.2,r.t.)を0.6mL(1%)添加した。
分析装置は味認識装置TS-5000Z(Insent)を使用した。味覚センサー分析用サンプルは、発酵乳サンプルを精製水にて二倍希釈(w/w)したものを用いた。分析のコントロールとして、ブルガリアヨーグルト(明治)を同様に希釈したものを用いた。分析に使用したセンサーは、ブレンド膜、プラス膜、マイナス膜、GL1(甘味センサー)を使用した。
1%GODO-TCF添加サンプルは、コントロール、0.1%GODO-TCF、クエン酸緩衝液添加サンプルと比較して甘味、苦味雑味が減少した。0.1%GODO-TCF添加サンプルは、クエン酸緩衝液添加サンプルとほぼ同様の結果であった。また、スミチームC添加サンプルは、苦味雑味および一般苦味が上昇した。
以上の結果より、塩類や緩衝液成分の影響を除くと苦味雑味、甘味以外の味覚の変化は起こらないことが分かった。またGODO-TCF由来プロテアーゼを乳タンパク質に作用させても苦味が発生しにくいことが分かった。
Claims (8)
- カゼインを含有する乳由来原料と、配列番号1で示されるアミノ酸配列との同一性が90%以上であるアミノ酸配列からなるタンパク質とを含有する乳製品。
- 前記タンパク質が、トリコデルマ属に属する微生物に由来するタンパク質である請求項1記載の乳製品。
- さらに乳酸菌又は酵母を含む請求項1又は2記載の乳製品。
- 発酵乳又はチーズである請求項1~3のいずれか1項に記載の乳製品。
- 2バイト法における破断応力が5500Pa以上であり、破断付着性が800J/m3以上である請求項1~4のいずれか1項に記載の乳製品。
- 増粘剤、安定剤、ゲル化剤及び糊料からなる凝固成分を実質的に含有しない請求項1~5のいずれか1項に記載の乳製品。
- カゼインを含有する乳由来原料に、配列番号1で示されるアミノ酸配列との同一性が90%以上であるアミノ酸配列からなるタンパク質と、乳酸菌とを添加し、発酵させることを特徴とする乳製品の製造方法。
- 配列番号1で示されるアミノ酸配列との同一性が90%以上であるアミノ酸配列からなるタンパク質を含有する乳製品用凝乳剤。
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WO2021210539A1 (ja) * | 2020-04-13 | 2021-10-21 | 合同酒精株式会社 | 発酵乳及びその製造方法、並びに脱リン酸乳 |
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US20020160445A1 (en) * | 2001-02-09 | 2002-10-31 | Marianne Harboe | Method of providing polypeptide preparations with reduced enzymatic side activities |
FR2836014B1 (fr) * | 2002-02-15 | 2004-07-23 | Gervais Danone Sa | Nouveau procede de fabrication de produits laitiers fermentes mettant en oeuvre des enzymes d'origine bacterienne |
FR2836015B1 (fr) * | 2002-02-15 | 2004-10-01 | Gervais Danone Sa | Nouveau procede de fabrication de produits laitiers fermente |
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CN111500474B (zh) * | 2009-12-18 | 2023-10-03 | 诺维信股份有限公司 | 用于在木霉属的蛋白酶缺陷突变体中产生多肽的方法 |
EP2852610B1 (en) * | 2012-05-23 | 2018-07-11 | Glykos Finland Oy | Production of fucosylated glycoproteins |
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- 2016-07-05 WO PCT/JP2016/069859 patent/WO2017006926A1/ja active Application Filing
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JPH0218834B2 (ja) * | 1982-04-08 | 1990-04-26 | Meito Sangyo Kk | |
JP2004033093A (ja) * | 2002-07-02 | 2004-02-05 | Daisuke Yasogawa | 細菌由来凝乳酵素及び当該酵素を用いたチーズの製造 |
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Cited By (3)
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WO2021210539A1 (ja) * | 2020-04-13 | 2021-10-21 | 合同酒精株式会社 | 発酵乳及びその製造方法、並びに脱リン酸乳 |
JPWO2021210539A1 (ja) * | 2020-04-13 | 2021-10-21 | ||
CN115397247A (zh) * | 2020-04-13 | 2022-11-25 | 合同酒精株式会社 | 发酵乳及其制造方法、以及脱磷酸乳 |
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TW201703638A (zh) | 2017-02-01 |
US20180199583A1 (en) | 2018-07-19 |
JPWO2017006926A1 (ja) | 2018-04-19 |
EP3320781B1 (en) | 2020-06-10 |
JP6785765B2 (ja) | 2020-11-18 |
EP3320781A1 (en) | 2018-05-16 |
EP3320781A4 (en) | 2019-02-20 |
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