KR101698379B1 - Goat milk protein hydrolysates, method for preparing the same and use for food of the same - Google Patents
Goat milk protein hydrolysates, method for preparing the same and use for food of the same Download PDFInfo
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/19—Dairy proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/12—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by hydrolysis, i.e. solvolysis in general
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2200/00—Function of food ingredients
- A23V2200/04—Colour
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Polymers & Plastics (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Mycology (AREA)
- Dairy Products (AREA)
Abstract
Description
The present invention relates to a protein hydrolyzate of goat milk, a process for producing it, and a use thereof in foods. The protein hydrolyzate of goat milk according to the present invention can be used as a protein material in foods such as food for milk allergy prevention and special medical use including silver type because? S-casein and? -Lactoglobulin are reduced while maintaining color and flavor inherent in goat's milk .
Milk is a food that has been used by mankind since ancient times, and is now widely used in various processed foods, and is an important part of infant nutrition as the main ingredient of baby formula. However, on the one hand, milk can also act as a causative agent of allergies, and this can be a major problem for infants whose primary source of milk is milk. Such milk allergy is an immunological disease caused by the difference of protein contained in milk from that of breast milk. It is caused by the fact that the milk protein, which is a heterologous protein, is not sufficiently decomposed in the digestive tract and is absorbed into the body with an antigenic characteristic. Therefore, it is likely to develop in the digestive tract or infants with immune function. Therefore, a method for eliminating the antigenicity of whey protein or casein (casein) protein, which is a milk protein, has been studied.
In this method, for example, a method has been reported in which the milk protein is heated to remove the antigenicity (Ratner et al., 1958, Pediatrics, 22, 653-658). However, in the case of the whey protein, the antigenicity is lowered by heating, but there is no change in the casein protein, and furthermore, by heating, the binding of the? -Lactoglobulin and the lactose is caused by the Maillard reaction (Bleumink et al., 1968, Allergy, 34, 521-543), which is about 100 times more antigenic than the original? -Lactoglobulin. Therefore, heat treatment alone is not effective in removing the antigenicity of milk protein. A method of precipitating ferric chloride as a method for selectively removing beta -lactoglobulin called an important allergen in milk has also been reported. However, since milk allergic infants also respond to β-lactoglobulin, it is difficult to effectively lower the antigenicity by this method.
In addition, a method of reducing antigenicity by hydrolyzing a milk protein using a protease such as trypsin, chymotrypsin, or pancrease has been reported (USP 5,486,461, USP 5,589,357, USP 5,405,637 and USP 4,981,174 ). However, in the case of the enzyme hydrolyzate, since it exhibits a strong bitter taste, it may be a problem to be used as a food material. Particularly, the casein protein in the milk protein is more likely to produce a peptide showing a bitter taste than the whey protein.
Goat milk, on the other hand, has received much interest from the pharmaceutical and food industries due to its unique health promotion function. Goat milk has higher total solid content than cow's milk and contains not only protein, fat and minerals but also digestion and absorption rate. Αs - casein, which is abundant in cow milk, forms a hard lump after solidification in gastric acid to inhibit digestion, but the protein composition of goat milk is very similar to that of breast milk, resulting in a low curd content and a high content of β - casein It is easy to digest and absorb. However, in spite of the excellent health promotion effect of goat milk, the development and research of food materials using goat milk in domestic and foreign countries are scarce.
As a result of efforts to increase the degree of hydrolysis of goat milk protein, the present inventors have found that an enzyme suitable for the degradation of goat milk protein is selected, and the hydrolysis time and temperature of the goat milk protein are controlled to be different, It was confirmed that a protein hydrolyzate powder can be prepared. Further, the present inventors have completed the present invention by confirming that the removal of the precipitate and the solubility of the final product are improved by adjusting the pH during the spray drying of the protein hydrolyzate of goat milk.
According to a first embodiment,
The present invention relates to a method for producing a protein by hydrolyzing a goat's milk protein using a first proteolytic enzyme and a second proteolytic enzyme;
Heating the protein hydrolyzate of goat milk at 80 DEG C or higher for 5 minutes or more;
Adjusting the pH of the goat's milk protein hydrolyzate to 8;
Adjusting the pH of the goat milk protein hydrolyzate to 7; And
And a step of concentrating the protein hydrolyzate of the goat milk, followed by spray drying and recovering the protein hydrolyzate.
In the method for preparing a protein hydrolyzate of goat milk according to the present invention, the first protease may be selected from the group consisting of neutrase, trypsin, flavorzyme, alcalase and protease protamax) can be selected. Preferably, the first protease is an alcalase.
In the method for preparing the protein hydrolyzate of goat milk according to the present invention, the second protease may be selected from the group consisting of neutrase, trypsin, flavorzyme, alcalase, protamax) can be selected. Preferably, the second protease is neutrase.
In the method for preparing the protein hydrolyzate of goat milk according to the present invention, the hydrolysis may be performed at 50 ° C to 70 ° C for 20 minutes to 40 minutes. Preferably, the hydrolysis can be carried out at 60 DEG C for 30 minutes.
In the method for preparing the protein hydrolyzate of goat milk according to the present invention, the concentration of the first protease and the second protease may be 0.3 to 0.5 parts by weight and 0.01 to 0.03 parts by weight based on 100 parts by weight of the goat milk protein. Preferably, the first protease and the second protease may be 0.4 part by weight and 0.01 part by weight based on 100 parts by weight of the goat milk protein.
According to a second embodiment,
And to provide a goat's milk protein hydrolyzate produced according to the first embodiment.
According to a third embodiment,
It is intended to provide the use of the goat's milk protein hydrolyzate according to the second embodiment in food for preventing allergy or special medical use including silver.
As used herein, the term " food for preventing allergy "means food used as a protein source of infants, pregnant women, and patients whose immune function has deteriorated for the purpose of preventing allergy. For example, the goat's milk protein hydrolyzate according to the present invention can be used in a prepared milk or a prepared milk powder obtained by using a protein derived from an animal's milk as a raw material protein.
As used herein, the term "food for special medical purposes, etc." is intended to be included in special-purpose foods, and is intended to encompass the general public and physiological Means foods prepared and processed to be supplied to them through oral or landscape food for the purpose of replacing part or all of the meal of a person with a different nutritional requirement.
The protein hydrolyzate of goat milk according to the present invention can be used as a protein material in foods such as food for milk allergy prevention and special medical use including silver type because? S-casein and? -Lactoglobulin are reduced while maintaining color and flavor inherent in goat's milk .
Fig. 1 shows the hydrolysis degree of the goat milk protein hydrolyzate irradiated by the OPA method according to Experimental Example 1. Fig.
Fig. 2 shows the hydrolysis degree of the goat milk protein hydrolyzate irradiated by the NPN method according to Experimental Example 1. Fig.
3 shows the proteolytic activity of goat's milk protein by SDS-PAGE according to Experimental Example 1. M, marker GP, goat milk protein a, as-casein b,? -Casein c, β-lactoglobulin; e, α-lactalbumin)
4 shows the proteolytic degradation behavior of goat milk on SDS-PAGE according to the mixing treatment of the alcalase and the Ntrastase according to Experimental Example 1 (M, marker, MP, milk protein, GP, ?, casein, c,? -casein, d,? -lactoglobulin, e,
FIG. 5 shows the degradation pattern of the goat milk protein by RP-HPLC according to Experimental Example 1 (A, goat milk protein; B, goat milk protein hydrolyzate)
6 shows the protein hydrolyzate of goat's milk protein produced by combined protease treatment and spray drying according to Experimental Example 2. Fig.
Hereinafter, the present invention will be described in more detail with reference to Examples. It is to be understood by those skilled in the art that these examples are for illustrative purposes only and that the scope of the present invention is not construed as being limited by these examples.
<Examples>
Example 1. Selection and hydrolysis of enzymes for producing protein hydrolyzate of goat milk
Proteolytic hydrolysis of goat 's milk was performed on selected commercial enzymes such as Alcalase, Nutraceutical, Flavobaim, and Protemax. In the preliminary test, the ability to selectively hydrolyze αs-casein and β-lactoglobulin was investigated for each enzyme. Hydrolysis time and temperature conditions were set in order to find the optimum decomposition conditions for the production of the enzyme. Experiments were conducted with different amounts. After the hydrolysis, the solution was heated at 90 ° C for 10 minutes. To prevent clogging in the pilot during spray drying, pH was raised to 8 using NaOH and HCl to improve the solubility of the final product. After concentration and concentration, the hydrolyzate was recovered by spray drying.
Example 2. Examination of general components and microorganisms
General components and microorganisms of goat's milk protein hydrolyzate were tested by Chungbuk Livestock Research Institute.
Example 3. Investigation of hydrolysis rate using O-phthalaldehyde
The hydrolysis rate of the sample was determined by measuring the absorbance at 340 nm using the color development reaction between the amino group and o-phthaldialdehyde (OPA) occurring in the presence of dithiotreitol according to the method of Nielsen et al, (2001) Respectively.
Example 4. Measurement of non-protein nitrogen (NPN)
Samples and 24% trichloroacetic acid solution were mixed in the same volume, allowed to stand for 30 minutes, centrifuged at 3,500 rpm for 30 minutes, and then the supernatant was collected and analyzed by NPN. Solution A was prepared by dissolving 2% sodium carbonate in 0.1 N sodium hydroxide, and solution B was prepared by mixing 0.5% copper sulfate in 1% sodium citrate. Solution A and B were mixed in a ratio of 50: 1 and alkaline copper reagent . 5 ml of reagent prepared in 1 ml of sample was mixed and allowed to stand at room temperature for 15 minutes. 0.5 ml of phenol reagent was added to induce a color reaction for 30 minutes, and the absorbance was measured at 750 nm.
Example 5. Protein quantitation
Proteins were quantified using Quick Start TM Bradford 1x Dye Reagent (Biorad, USA). The concentration of Bovine serum albumin was diluted to 1 mg / ml, 0.75 mg / ml, 0.5 mg / ml, 0.25 mg / ml, 0.125 mg / ml and 0.0625 mg / ml and used as a standard. Dilute the sample with distilled water Respectively. 20 μl of standard and sample were dispensed into each cuvette, 1 ml of bradford dye reagent was dispensed, and reacted for 10 minutes. Absorbance was measured at 595 nm.
Example 7. SDS-PAGE
Were performed using Mini-Protean® Tetra System (Biorad) and PowerPac ™ HV (Biorad) according to the method of Laemmli (1970). The same amount of skim milk and hydrolyzate were mixed in 2X sample buffer (0.125 M TrisCl, 4% SDS, 20% glycerol, 2% β-mercaptoethanol, pH 6.8) and heated at 95 ° C for 10 minutes to use as an electrophoresis sample. 12.5% separating gel and 4% stacking gel were prepared, and the mixture was incubated for 1 hour, and 10 μl of each gel was loaded and electrophoresed at 20 mA per gel for 1 hour. After electrophoresis, gel was stained with coomassie blue solution for 1 hour, discolored, and images were taken using a Molecular Imager® GelDoc ™ XR plus imaging system (Biorad). The results were analyzed using Image Lab TM Software 5.1 (Biorad), and the degree of reduction of αs-casein and β-lactoglobumin was measured by referring to the respective band concentrations and the amount of protein quantified.
Example 8. Reversed-Phase HPLC
Samples were mixed in the same volume with sample buffer (pH 6.8; 0.1 M BisTris buffer, 6 M GdnHCl, 5.37 mM sodium citrate, 19.5 mM DTT) and incubated at room temperature for 1 hour. After centrifugation at 12,000 rpm for 5 minutes, Was recovered and diluted and used as an RP-HPLC sample to confirm the decomposition of goat's milk protein hydrolyzate. Table 1 shows the RP-HPLC conditions.
B: 90% Acetonitrile with 0.1% trifluoroacetic acid
<Experimental Example>
Experimental Example 1. Hydrolysis of protein hydrolyzate of goat milk
Among the four proteases, Alcalase was the most effective and Neutrase was the main enzyme. The enzyme concentration, hydrolysis time, and hydrolysis temperature were varied to determine the hydrolysis conditions of the alcalase used as the main enzyme for proteolytic hydrolysis of goat milk. However, the coenzyme Nutra was added in an amount of 0.01%. The hydrolysis rate of the hydrolyzed solution was measured by o-phthalaldialdehyde and non-protein nitrogen. SDS-PAGE and RP-HPLC were used to confirm the decomposition rate. The results are shown in Figs. 1 to 5, respectively.
Referring to FIGS. 1 to 3, when the concentration of the alkaline agent was 0.4%, the optimum degree of hydrolysis was shown. When the concentration of the alkaline agent was more than 0.4%, a significant change in the degree of hydrolysis Not observed. The optimum degree of hydrolysis was observed when the reaction was carried out for 30 minutes. When the reaction time was more than 30 minutes, no significant change in the degree of hydrolysis was observed. In addition, the alcholase exhibited the optimum degree of hydrolysis at 60 ° C, and no significant change in the degree of hydrolysis was observed when the temperature of the reaction reached 60 ° C or higher. Thus, as a result of this experiment, alkalase and nuclease were added at 0.4% and 0.01%, respectively, based on the weight of the goat milk protein, and showed optimal hydrolysis rate when reacted at 60 ° C for 30 minutes and 10 minutes, respectively .
4 and 5, β-lactoglobulin found in the goat milk was not found in the goat milk protein hydrolyzate, and it was confirmed that the amount of αs-casein was reduced by about 40% or more as compared with the goat milk. On the other hand, the reason for not hydrolyzing all the? S-casein was determined in view of the fact that the powder was easily formed as the residual amount of? S-casein was present in the powder during spray drying. In addition, the pH adjustment of the hydrolysis solution before powder drying is an important part of this study as means for facilitating spray drying by removing the precipitate of the degradation solution due to the characteristics of the milk protein.
a : based on protein content
Experimental Example 2. Production of spray dried powder of protein hydrolyzate of goat milk
The mass-production process was set up using the degreasing and spray drying plant of the plant and spray drying was performed to prevent protein loss other than? S-casein and? -Lactoglobulin due to excessive hydrolysis. The temperature of the spray drying was 95 ° C and was carried out for about 20 minutes on the basis of 10 L of crude oil. The hydrolysis solution was pulverized through spray drying after adjusting the pH, so that high solubility was maintained even when redissolving. The protein hydrolyzate of the powdered goat milk was shown in Fig. 6, and the recovery rate was about 4.8% after three trials.
Experimental Example 3. General components and microorganism test of hydrolyzate
The sensory properties and general component results of the hydrolyzate are shown in Tables 3 and 4 below. Escherichia coli, Staphylococcus aureus, Salmonella and the like are shown in FIG.
As can be seen from Tables 3 to 5, it was confirmed that the protein hydrolyzate of goat's milk according to the present invention maintained the color and flavor inherent in goat's milk. In addition, it is expected that it will be judged to be negative by the result of the examination of harmful bacteria and commercialized.
It will be understood by those skilled in the art that various changes in form and details may be made therein without departing from the spirit and scope of the invention as defined by the appended claims. Therefore, the presented embodiments should be considered in an illustrative rather than a restrictive sense. The scope of the present invention is defined by the appended claims rather than by the foregoing description, and all differences within the scope of equivalents thereof should be construed as being included in the present invention.
Claims (9)
Heating the protein hydrolyzate of goat milk at 80 DEG C or higher for 5 minutes or more;
Adjusting the pH of the goat's milk protein hydrolyzate to 8;
Adjusting the pH of the goat milk protein hydrolyzate to 7; And
A method for preparing a goat's milk protein hydrolyzate, comprising the step of concentrating the goat's milk protein hydrolyzate followed by spray drying.
Wherein the first proteolytic enzyme is an alcalase.
Wherein said second proteolytic enzyme is neutrase.
Wherein the hydrolysis is carried out at 50 DEG C to 70 DEG C for 20 minutes to 40 minutes.
Wherein the concentration of the first protease and the second protease is 0.3 to 0.5 parts by weight and 0.01 to 0.03 parts by weight based on 100 parts by weight of the goat milk protein.
Hydrolyzing the goat milk protein at 60 DEG C for 30 minutes using an alkalase and a nuclease;
Heating the protein hydrolyzate of goat milk at 80 DEG C or higher for 5 minutes or more;
Adjusting the pH of the goat's milk protein hydrolyzate to 8;
Adjusting the pH of the goat milk protein hydrolyzate to 7; And
Concentrating the goat's milk protein hydrolyzate and spray drying it to recover,
Wherein the alkalase and the nuclease are added in an amount of 0.4 part by weight and 0.01 part by weight based on 100 parts by weight of the goat milk protein.
Protein hydrolyzate of goat's milk for use in foods, such as food for allergies or special medical applications.
Protein hydrolysates of goat milk for use in formula or formula.
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| KR102009732B1 (en) * | 2019-04-15 | 2019-08-12 | 주식회사 쎌바이오텍 | Method of Preparing Lactic Acid Bacteria Having Dual Coating Through Cell Mass Enrichment Process |
| KR102009731B1 (en) * | 2019-04-15 | 2019-08-12 | 주식회사 쎌바이오텍 | Method of Preparing Lactic Acid Bacteria Having Dual Coating By Using Protein Hydrolysate |
| KR102508665B1 (en) * | 2022-11-07 | 2023-03-15 | 주식회사 보부상바이오팜 | Preparation method for protein preparations with improved digestion |
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| KR102009732B1 (en) * | 2019-04-15 | 2019-08-12 | 주식회사 쎌바이오텍 | Method of Preparing Lactic Acid Bacteria Having Dual Coating Through Cell Mass Enrichment Process |
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| US11920124B2 (en) | 2019-04-15 | 2024-03-05 | Cell Biotech Co., Ltd. | Method of producing lactic acid bacteria dual-coated with protein and polysaccharide by using protein hydrolysate |
| KR102508665B1 (en) * | 2022-11-07 | 2023-03-15 | 주식회사 보부상바이오팜 | Preparation method for protein preparations with improved digestion |
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