JP2002034591A - Method for producing protein hydrolyzate - Google Patents

Abstract

PROBLEM TO BE SOLVED: To provide a novel protein hydrolyzate from which coloring, unfavorable flavor and the like and its causative substances are removed to obtain a protein hydrolyzate in which coloring by heating and generation of unfavorable flavor are suppressed. A manufacturing method is provided. SOLUTION: The protein raw material is decomposed with a protease,
A method for producing a protein hydrolyzate, comprising deactivating the enzyme by heating, filtering, heating at 65 to 90 ° C., and then performing an activated carbon treatment and an ultrafiltration treatment. Performing an ultrafiltration treatment, using an ultrafiltration membrane having a cut-off molecular weight of 2,000 to 6,000,
It is a desirable embodiment to perform by collecting the permeated fraction, and to perform the activated carbon treatment by collecting the adsorbed fraction using activated carbon activated by chemicals.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

[0001] The present invention relates to a method for producing a protein hydrolyzate from which coloring, unfavorable flavor and the like and its causative substances have been removed. More specifically, the present invention comprises decomposing a protein material with a protease, deactivating the enzyme by heating, filtering, heating at 65 to 90 ° C., and then performing activated carbon treatment and ultrafiltration. The present invention relates to a method for producing a characteristic protein hydrolyzate. As used herein, percentages are
Unless otherwise specified, it is indicated by weight.

[0002]

2. Description of the Related Art Activated carbon, which has been widely used in the food industry and chemical industry for decolorization and deodorization, etc. for decolorization and deodorization of protein hydrolysates [Hiroshi Yanai, "Activated Carbon Reader," 162 pages, 166 pages, Nikkan Kogyo Shimbun,
[April 20, 1979], and the like using an adsorbent (hereinafter referred to as prior art 1).

[0003] Also, a method for producing a flavorful whey protein hydrolyzate characterized by decomposing a protein raw material with a protease, deactivating the enzyme by heating, and subjecting the enzyme to ultrafiltration (Patent No. 2)
959747. Hereinafter, this is referred to as Conventional Technique 2. )
It has been known.

[0004]

As disclosed in the above prior art, in order to produce a protein hydrolyzate from which coloring, undesired flavor and the like have been removed, activated carbon treatment or ultrafiltration treatment is performed independently. Was known to do in.

[0005] However, the protein hydrolyzate obtained by the above-mentioned conventional production method still has insufficient coloring, unfavorable flavor and the like, and the removal of its causative substances is insufficient.
As is clear from the test examples described later, there was a problem that coloring and unfavorable flavor occurred due to heating.

In view of the above prior art, the present inventors have set forth one of the test examples described below for the purpose of providing a method for producing a protein hydrolyzate in which coloring due to heating and generation of an undesirable flavor are suppressed. As described in the section, combinations of various processes, coloring, unfavorable flavor, and the like and conditions for removing the causative substances were tested.

As a result, the present inventors have combined activated carbon treatment and ultrafiltration treatment with other heating treatments and the like.
A protein hydrolyzate characterized by decomposing a protein material with a protease, deactivating the enzyme by heating, filtering, heating at 65 to 90 ° C., and then performing activated carbon treatment and ultrafiltration. The production method of the above solves the above problems, coloring, unpleasant flavor and the like and a pigment that is a causative substance thereof,
The present inventors have found that it is possible to provide a method for producing a protein hydrolyzate in which high-molecular substances such as polysaccharides and enzymes are removed, and coloring and unfavorable flavor due to heating can be suppressed, thereby completing the present invention.

[0008] It is an object of the present invention to provide a novel protein hydrolyzate which is capable of removing a color, an undesirable flavor and the like, and a causative substance thereof, and obtaining a protein hydrolyzate in which coloring by heating and generation of an undesirable flavor are suppressed. It is to provide a manufacturing method.

[0009]

The present invention to solve the above-mentioned problems is to decompose a protein material with a protease, deactivate the enzyme by heating, filter, and heat at 65 to 90 ° C.
A method for producing a protein hydrolyzate characterized by performing an activated carbon treatment and an ultrafiltration treatment, wherein the ultrafiltration treatment is performed after the activated carbon treatment (hereinafter referred to as embodiment 1), and the ultrafiltration is performed. The treatment was performed with a molecular weight cutoff of 2000 to 600
A non-adsorbed fraction is collected by using an ultrafiltration membrane of 0 to collect the permeated fraction (hereinafter, referred to as Embodiment 2), and using activated carbon activated by activated carbon treatment. (Hereinafter referred to as aspect 3).
Is also a desirable mode.

[0010]

Next, the present invention will be described specifically. The protein raw material used in the method of the present invention is animal protein derived from animal milk, egg, fish meat, animal meat, soybean, soybean,
It is a plant protein derived from wheat or the like, a microbial protein derived from mold, yeast, bacteria, or the like, or an arbitrary mixture thereof, and is not particularly limited. In addition, protein concentrates obtained by concentrating these proteins by treatment with ultrafiltration, ion exchange resin or the like can also be used. Furthermore, a starting material may be a hydrolyzate obtained by hydrolyzing the above-mentioned protein slightly in advance and having a relatively large molecular weight.

The protein material is dispersed and dissolved in water or hot water. The concentration of the lysis solution is not particularly limited, but usually,
A protein concentration of about 5 to 15% is desirable from the viewpoint of efficiency and operability. Then, the protein solution was added to 65
Heat sterilization at a temperature of from 90 to 90 ° C. for from about 10 seconds to about 30 minutes is desirable from the viewpoint of preventing spoilage due to contamination by various bacteria.

In the decomposition treatment of the protein raw material of the present invention with a protease, hydrolysis conditions such as the kind, amount, temperature, pH, hydrolysis time and the like of the enzyme which can be adjusted to a desired degree of protein decomposition are prepared. It can be performed by setting in an experiment and then preparing a protein hydrolyzate.

The protease used in the method of the present invention is derived from animals (for example, pancreatin, trypsin,
Endoproteases and exoproteases (peptidases) derived from plants (for example, papain, bromelain, etc.), microorganisms (for example, lactic acid bacteria, yeasts, molds, Bacillus subtilis, actinomycetes, etc.), crude purified products thereof And crushed cells.

The amount of proteolytic enzyme used with respect to the raw material varies depending on the substrate concentration, enzyme titer, reaction temperature and reaction time.
enzyme alone at a rate of 50 to 10000 activity units per gram,
Alternatively, hydrolysis is performed by adding a plurality of combinations. The enzyme may be added all at once, or divided into small amounts or each type, and added sequentially.

The pH of the protein hydrolysis reaction is adjusted by adding an acid or an alkali agent to a desired pH within the range of pH 2 to 10, corresponding to the optimum pH of the enzyme used. In this case, examples of the acid include hydrochloric acid, citric acid, and phosphoric acid, and examples of the alkaline agent include sodium hydroxide, potassium hydroxide, potassium carbonate, magnesium carbonate, and potassium phosphate.

The temperature of the protein hydrolysis reaction is not particularly limited, and is selected from a range that can be put to practical use, including an optimum temperature range in which the enzyme action is exhibited, that is, a range of usually 30 to 70 ° C. Temperature lower or higher than the optimal temperature of the enzyme,
For example, by maintaining the temperature in the range of 50 to 60 ° C., spoilage during protein hydrolysis can be prevented.

Since the progress of the protein hydrolysis reaction varies depending on the reaction conditions such as the type and combination of the enzymes used, the reaction temperature, and the initial pH, the desired protein degradation rate set in the preliminary experiment as described above. It is necessary to determine the reaction duration within the range described below.

The heat inactivation of the enzyme of the present invention is performed by inactivating the enzyme when the degree of hydrolysis reaches a desired rate of protein degradation based on the hydrolysis conditions set in the preliminary experiment. Do to stop. The deactivation operation can be performed by a heat treatment (for example, at 85 ° C. for 10 minutes).

[0019] The filtration treatment of the present invention can be carried out by an operation such as diatomaceous earth (for example, celite), microfiltration (microfiltration), ultrafiltration, etc., after inactivation of the enzyme in the decomposition solution. This treatment removes the precipitate from the decomposition solution.

The heating treatment of the present invention can be carried out at a heating temperature in the range of 65 to 90 ° C., as will be apparent from the test examples described later, by coloring the protein hydrolyzate as the final product. It is necessary to remove undesired flavor and the like and substances causing the undesired flavor, and to suppress coloring by heating and generation of undesired flavor. The heating time is usually from 5 minutes to 1
Perform within a time range. In addition, after the heating treatment, the heating treatment liquid is evaporated, reverse osmosis, or nano-sized for the purpose of reducing the amount of the liquid, or concentrating the coloring, an unfavorable flavor and its causing substance, and increasing the efficiency of the adsorption treatment. It can also be concentrated by a treatment such as filtration.

The activated carbon used in the method of the present invention is defined by the Food Sanitation Law, and if it can adsorb and remove the corresponding coloring, unfavorable flavor and the like, and its causative substances, powdered carbon, crushed charcoal, Any product such as a granular carbon, a composite product in which activated carbon is bonded to cellulose fiber, or the like may be used. For example, commercially available products such as Shirasagi M, Shirasagi P, carboraffin, strong Shirasagi, granular Shirasagi KL, and granular Shirasagi LH (All manufactured by Takeda Pharmaceutical Company), SD, BA, ZN, CL-
K, CL-H, and GS-A (all manufactured by Ajinomoto Fine-Techno), Diahope S80B (Mitsubishi Chemical), GLC (Kuraray), Ecosorb S-405,
Examples include S-407, S-410, and S-415 (all manufactured by U.S.A. Graver Chemical Co.).

According to the type of the activated carbon to be used, the activated carbon treatment is performed by a batch treatment when powdered carbon is used, a column passing treatment when crushed or granular carbon is used, or an activated carbon bonded to cellulose fiber or the like. In the case of using the prepared composite product, an adsorption filtration treatment using a filter such as a filter press is usually employed.

When powdered carbon is used, 1 to 5% of activated carbon based on the solid content in the solution is added, and 1 to 24%
After performing the adsorption treatment for a long time, the activated carbon added is removed by a filtration treatment, and a non-adsorbed fraction is collected. The treatment temperature and the treatment time can be set as appropriate, but when performing the adsorption treatment for 5 hours or more, the temperature is desirably 10 ° C. or less to prevent bacterial growth. The amount of activated carbon added is 1%
If it is less than 5%, the reduction of coloring, undesired flavor, etc. and its causative substances are not sufficient, and if it exceeds 5%, the cost increases and the amount of residue increases, so that the filtration process becomes inefficient. Not desirable.

When crushed or granular coal is used, the same batch treatment as for powdered charcoal, or a certain amount of activated carbon is packed in a column, and a certain amount of solution is passed through this column to remove the non-adsorbed fraction. The column is passed through to be collected. In the case of passing through a column, the time during which the solution and the activated carbon are in contact with each other is referred to as the space volume (hereinafter referred to as SV).
(/ H)), SV is in the range of 0.5 to 10 / h, preferably in the range of 1 to 5 / h. If the SV is less than 0.5, the reduction of coloring, unfavorable flavor and its causative substances is sufficient, but the production efficiency is poor, and the SV is less than 10%.
Exceeding the coloration, undesired flavor, etc., and the reduction of the causative substances thereof become insufficient, which are not desirable. The treatment temperature and the amount of the treatment solution can be appropriately set within a range in which the reduction of coloring, unfavorable flavor and its causative substances is sufficient. However, when passing the solution requires 5 hours or more, in order to prevent bacterial growth, 10 ° C. It is desirable to set the following temperature.

In the case of using a composite product in which activated carbon is bonded to cellulose fiber or the like, 1 to 5% of the composite product based on the liquid amount is added in a batch system, and then filtered by a filtration device such as a filter press. To remove the residue and the adsorbed fraction to recover the non-adsorbed fraction, or to pre-coat a composite product of 1 to ¹⁰ kg per 1 m ² of a leaf area of a filtration device such as a filter press, and then apply a solution to the pre-coated layer. And a filtration treatment is carried out to collect a non-adsorbed fraction in which coloring, unfavorable flavor and its causative substances are reduced.
When this method is adopted, since no time is required for filtration,
The treatment temperature can be appropriately set within a range in which coloring, undesired flavor, and a substance causing the unfavorable flavor can be sufficiently reduced.

Further, as described in Embodiment 3, the activated carbon treatment can be carried out by recovering the non-adsorbed fraction using activated carbon activated with a chemical, as is clear from the test examples described later. It is desirable because a protein hydrolyzate in which coloring and generation of an undesirable flavor are suppressed can be obtained.

Activated carbon is activated by zinc chloride, phosphoric acid, sodium phosphate, calcium chloride,
Potassium sulfide, potassium hydroxide, sodium hydroxide, potassium carbonate, sodium carbonate, potassium thiocyanate,
Using potassium sulfate, sodium sulfate, calcium carbonate, sulfuric acid, boric acid, nitric acid, hydrochloric acid, etc., in a conventional manner [Yuzo Sanada et al., “New Activated Carbon-Fundamentals and Applications-”, Nos. 51 to 5
3, Kodansha Scientific Co., Ltd., August 10, 1998] to obtain fine porous adsorbed carbon. For convenience, commercially available activated carbon activated with chemicals, such as carbofin (manufactured by Takeda Pharmaceutical Co., Ltd .; zinc chloride activated), ZN (manufactured by Ajinomoto Fine Techno Co., zinc chloride activated), and the like can be used.

The ultrafiltration membrane used in the method of the present invention has no problem in food production, and can be used as an organic membrane, an inorganic membrane, or a composite membrane as long as it can separate and fractionate coloring, unfavorable flavor and its causative substances. Any material, such as a membrane,
The shape may be any of a hollow fiber type, a tubular type, a flat membrane type, a spiral type and the like. For example, commercially available products include Microza (manufactured by Asahi Kasei Kogyo), Molsep (manufactured by Daisen Membrane Systems), NTU series (manufactured by Nitto Denko Corporation), Romicon (manufactured by Romicon, USA), AMT-UF
(AMT, USA), DDSS (Dow D, Denmark)
ANMARK A / S).

In the ultrafiltration treatment, the operating pressure and the circulating flow rate are reduced according to the physical properties of the solution to be treated and the shape of the ultrafiltration membrane to be used, such that the permeation flux is reduced due to fouling and contamination is less likely to occur due to bacterial growth. The temperature and the like are set appropriately and the permeate fraction is collected.

As described in Embodiment 2, the ultrafiltration treatment is carried out by using an ultrafiltration membrane having a molecular weight cut-off of 2,000 to 6,000 and collecting the permeated fraction. As is evident from the above, it is desirable to obtain a protein hydrolyzate with a high recovery rate and in which the generation of coloring and an undesirable flavor due to heating are suppressed.

The order of the activated carbon treatment and the ultrafiltration treatment is not particularly limited and can be carried out as appropriate. However, when the activated carbon treatment is performed after the ultrafiltration treatment, the activated carbon is not treated when the activated carbon is used in a batch treatment. Separation operation is required, and when powdered charcoal is used, a precise filtration operation is required to prevent leakage of fine activated carbon particles. In addition, when activated carbon treatment is performed after ultrafiltration processing without being limited to batch processing, column processing, and adsorption filtration processing, it is necessary to pay close attention to contamination such as bacteria. On the other hand, if the ultrafiltration treatment is performed after the activated carbon treatment, even if there is some leakage of fine activated carbon particles, the separation can be performed by the ultrafiltration membrane. Because the liquid is sterile,
The bacterial count of the liquid after filtration can be greatly reduced. Therefore, as described in Embodiment 1, it is desirable to perform an ultrafiltration treatment after the activated carbon treatment.

As described above, according to the production method of the present invention,
A protein hydrolyzate in which coloring due to heating and generation of an unfavorable flavor is suppressed is obtained, and a protein hydrolyzate having good digestibility and absorption and reduced antigenicity is obtained. The hydrolyzate is sterilized, concentrated, and dried in the form of a solution or a conventional method, and is blended and added as a protein source, or as a flavor improver or seasoning in general foods, nutritional foods for infants, nutritional foods for infants, etc. can do.

Next, the present invention will be described in detail with reference to test examples. Test Example 1 This test was performed to show that the method for producing a protein hydrolyzate of the present invention is superior to the conventional art. (1) Preparation of Samples The following four types of samples were prepared. Sample 1: Protein hydrolyzate prepared by the same method as in Example 1 of the present invention Sample 2: As shown in Prior Art 1, except that no heating treatment and ultrafiltration treatment were performed, Protein hydrolyzate produced by the same method Sample 3: Protein hydrolyzate produced by the same method as in Example 1 except that the heating treatment and the activated carbon treatment are not performed, as shown in Prior Art 2: Sample 4 : Protein hydrolyzate produced by the same method as in Example 1 except that no heating treatment, activated carbon treatment, and ultrafiltration treatment were performed as a control sample

(2) Test Method Coloring, unpleasant taste, and the causative substance of each sample were measured five times for each sample by the following test method, and the average value was calculated and evaluated.

(A) Method of judging coloring Each sample was dissolved in purified water at a concentration of 10%, heated at 90 ° C. for 30 minutes, cooled to 10 ° C., and then a spectrophotometer (U-3210 manufactured by Hitachi, Ltd.). ) Using a wavelength of 400 nm,
The transmittance (T%) of the sample in a 1 cm glass cell was measured. Since coloring reduces the transmittance, it can be determined that the coloring is weak when the value of the transmittance is high and that the coloring is strong when the value of the transmittance is low.

(B) Test method for undesired flavor The unpleasant flavor was tested as follows using odor as an index. Each sample was dissolved at 10% concentration in purified water,
Heat for 30 minutes, cool to 10 ° C,
The taste was sensually tested by a panel of 20 men and women up to 0 years old, and there were no odor (0 points), slight odor (1 point), odor (2 points), and strong odor (3 points). It was evaluated on a scale, and from the average of the evaluation points, less than 0.5
A score of at least 1.5 and less than 1.5 was determined to be slightly higher, a score of 1.5 to less than 2.5 was determined, and a score of 2.5 to less than 3.0 was determined to be strong.

(C) Method of measuring the causative substance The causative substance of the coloring and the undesirable flavor of each sample was equipped with a reversed-phase column (Octadecyl-4PW column, manufactured by Tosoh Corporation) using acetonitrile and purified water as eluents. HPLC
(Shimadzu Corporation), high-performance liquid chromatography by gradient elution (elution conditions of acetonitrile concentration of 9% to 54% in 50 minutes at a flow rate of 1 ml / min) was performed, and a UV detector (wavelength: 215 nm) was used. )
It is detected as a peak around the elution time of 35 minutes.

The amount of the causative substance is based on the peak area of the causative substance (B) contained in each sample with respect to the peak area (A) of the sample 4 with the peak area of the control sample 4 as 100%. And expressed as a relative percentage shown in the following equation. Relative amount (%) of causative substance = B / A × 100

(3) Test Results Table 1 shows the results of this test. As is clear from Table 1, the transmittance of the production method of the present invention (Sample 1) is higher than that of the conventional method (Sample 2 and Sample 3).
It was excellent because there was no odor and the amount of the causative substance was small. That is, it has been found that the production method of the present invention is superior in all of the coloring, the flavor, and the amount of the causative substance thereof, as compared with the method of the prior art.

In the production method of the present invention, even if the order of the activated carbon treatment step and the ultrafiltration treatment step is changed to prepare a sample, the coloring, flavor and the cause thereof are higher than those of the prior art method. Approximately similar results were obtained, with superior amounts of material.

In the above-mentioned method for producing each sample, the type of the protein material, the type of the protease, the heating temperature, the type of the ultrafiltration membrane, or the type of the activated carbon were appropriately changed. Similar results were obtained.

[0042]

[Table 1]

Test Example 2 This test was performed to examine the temperature range of an appropriate heating treatment. (1) Preparation of Samples The following four types of samples were prepared. Sample 5: Protein hydrolyzate produced by the same method as in Example 1 except that the temperature of the heating treatment was set to 60 ° C. Sample 6: Example except that the temperature of the heating treatment was set to 65 ° C. Sample 7: Protein hydrolyzate produced by the same method as in Example 1 except that the temperature of the heating treatment was set to 90 ° C. Sample 8: Protein hydrolyzate produced by the same method as in Example 1 Except that the temperature was 100 ° C,
Protein hydrolyzate produced by the same method as in Example 1

(2) Test Method The amount of the causative substance in each sample was measured five times for each sample by the test method described in Test Example 1, and the average value was calculated and evaluated.

(3) Test Results The results of this test are shown in Table 2. As is clear from Table 2, at least 65%
It was found that it was necessary to perform a heating treatment at a temperature of ° C. In addition, there is a problem that a pressure-resistant and heat-resistant device such as a retort device is required in order to maintain the temperature at 100 ° C. or more for several minutes or more. Therefore, in consideration of the production efficiency, the temperature range of the heating treatment is appropriately in the range of 65 to 90 ° C.

Further, in the above-mentioned methods for producing each sample, the type of the protein raw material, the type of the proteolytic enzyme, the type of the ultrafiltration membrane, or the type of the activated carbon were appropriately changed and tested. Was done.

[0047]

[Table 2]

Test Example 3 This test was performed to determine a desirable order of the activated carbon treatment step and the ultrafiltration treatment step. (1) Preparation of Samples The following two types of samples were prepared. Sample 9: Protein hydrolyzate produced by the same method as in Example 1 of the present invention Sample 10: Produced by the same method as in Example 1 except that the order of the activated carbon treatment step and the ultrafiltration treatment step was changed. Protein hydrolyzate

(2) Test Method The transparency of each sample was measured five times for each sample by the following test method, and the average value was calculated and evaluated. Each sample was dissolved in purified water at a concentration of 10%, and a wavelength of 800 nm and a wavelength of 1 nm were measured using a spectrophotometer (U-3210, manufactured by Hitachi, Ltd.).
The transmittance (T%) of the sample in the cm glass cell was measured. If the value of the transmittance is high, it can be determined that the transparency is high.

(3) Test Results The results of this test are shown in Table 3. As is clear from Table 3, the method of performing the ultrafiltration treatment after the activated carbon treatment (sample 9) has a smaller leakage of activated carbon than the method of performing the activated carbon treatment after the ultrafiltration treatment (sample 10). It was excellent because there was no decrease in transmittance based on the above. That is, in order to prevent the leakage of activated carbon particles and to produce a protein hydrolyzate having high transparency, it has been found that a method of performing ultrafiltration treatment after activated carbon treatment is desirable.

Further, in the above-mentioned method for producing each sample, the type of the protein raw material, the type of the protease, the heating temperature, the type of the ultrafiltration membrane, or the type of the activated carbon were appropriately changed. Similar results were obtained.

[0052]

[Table 3]

Test Example 4 This test was conducted to examine the molecular weight cutoff range of an appropriate ultrafiltration membrane. (1) Preparation of Samples The following four types of samples were prepared. Sample 11: Molecular weight cut off in the ultrafiltration treatment step: 1000
Protein 12 hydrolyzate prepared by the same method as in Example 1 except that the ultrafiltration membrane of Example 12 was used.
Protein 13 prepared by the same method as in Example 1 except that the ultrafiltration membrane of Example 13 was used.
Protein hydrolyzate prepared by the same method as in Example 1 of the present invention using the ultrafiltration membrane of Example 14: Molecular weight cut off of 1,000 in the ultrafiltration step
Protein hydrolyzate produced by the same method as in Example 1 except that an ultrafiltration membrane of 0 was used.

(2) Test Method The amount of the causative substance in each sample was measured five times for each sample by the test method described in Test Example 1, and the average value was calculated and evaluated. The recovery rate of each sample was measured five times for each sample by the following test method, and the average value was calculated and evaluated.

The dry weight (D) of the protein hydrolyzate produced from the raw material relative to the dry weight (C) of the protein raw material
And the recovery rate was calculated by the following equation. Recovery rate (%) = D / C × 100

(3) Test Results The results of this test are shown in Table 4. As is evident from Table 4, it was revealed that the ultrafiltration membrane having a molecular weight cut off of 10,000 was not enough to reduce the causative substances, and the ultrafiltration membrane having a molecular weight cut off of 1,000 had a poor recovery. That is, it was found that the molecular weight cut-off range of the ultrafiltration membrane, which sufficiently reduces the causative substance and has an excellent recovery rate, is desirably 2,000 to 6,000.

Further, in the above-mentioned method for producing each sample, the type of the protein raw material, the type of the protease, the temperature of the heating treatment, the type of the ultrafiltration membrane, or the type of the activated carbon were appropriately changed. Similar results were obtained.

[0058]

[Table 4]

Test Example 5 This test was conducted to determine the type of activated carbon. (1) Preparation of Samples The following four types of samples were prepared. Sample 15: Protein hydrolyzate produced by the same method as in Example 1 of the present invention using activated carbon (Activated carbon (manufactured by Takeda Pharmaceutical Co., Ltd., Carborafin, activated by zinc chloride)) activated for activated carbon treatment Sample 16: Active carbon treatment Protein 17 hydrolyzate produced by the same method as in Example 1 except that a chemical activated activated carbon (manufactured by Ajinomoto Fine Techno Co., Ltd., ZN; zinc chloride activated) was used. Sample 17: Activated carbon not activated by activated carbon treatment Protein hydrolyzate produced by the same method as in Example 1, except that (Shirasagi M, manufactured by Takeda Pharmaceutical Co., Ltd.) Sample 18: Activated carbon (Ajinomoto Fine-Techno, manufactured by Ajinomoto Fine Techno Co., Inc.) that was not chemically activated in the activated carbon treatment. SD), except
Protein hydrolyzate produced by the same method as in Example 1

(2) Test Method The coloration of each sample and the amount of the causative substance were measured five times for each sample by the test method described in Test Example 1, and the average value was calculated and evaluated.

(3) Test Results The results of this test are shown in Table 5. As is evident from Table 5, it was found that the use of the activated carbon, which was not activated by the chemical, was superior to the use of the activated carbon, which was not activated by the chemical, in the coloring and the reduction of the causative substances. That is, it has been found that it is desirable that the activated carbon excellent in the coloring and the reduction of the causative substance is a chemically activated activated carbon.

In the above-mentioned method for producing each sample, the test was carried out by appropriately changing the type of the protein raw material, the type of the protease, the heating temperature, or the type of the ultrafiltration membrane.
Almost the same results were obtained.

[0063]

[Table 5]

Next, the present invention will be described in more detail by way of Examples, but the present invention is not limited to the following Examples.

[0065]

Example 1 130 g of commercially available casein lactate (manufactured by New Zealand Daily Board; protein content: 85%) was dispersed in 870 g of purified water, and sodium hydroxide was added to adjust the pH of the solution to 7.0.
It was adjusted to 0 and heated at 85 ° C. for 10 minutes to completely dissolve casein. Thereafter, the temperature of the solution was cooled to 50 ° C., and sterilized pancreatin (manufactured by Amano Pharmaceutical Co., Ltd., 112000 activity units /
g) and 2.6 g of protease A Amano (manufactured by Amano Pharmaceutical Co., Ltd., 10,000 active units / g),
The mixture was kept at 50 ° C. for 18 hours, heated at 90 ° C. for 10 minutes to inactivate the enzyme and sterilize the solution, cooled to 10 ° C., and filtered using diatomaceous earth silica # 600H (manufactured by Chuo Silica Co., Ltd.). The permeated fraction was collected, heated at 80 ° C. for 10 minutes, cooled to 10 ° C., and added with 3% of activated carbon per solid (manufactured by Takeda Pharmaceutical Co., Ltd .; carboraffin; zinc chloride activation). After holding for 5 hours, filtration was performed using diatomaceous earth silica # 600H to collect a permeated fraction, and the permeated fraction was filtered using an ultrafiltration membrane SIP-1013 (manufactured by Asahi Kasei Corporation; molecular weight cut off 600;
The permeated fraction was collected by ultrafiltration according to 0), then concentrated to a concentration of 15% using a rotary evaporator, and lyophilized by a conventional method to obtain about 117 g of a powdery protein hydrolyzate.

Example 2 200 g of commercially available casein lactate (manufactured by New Zealand Daily Board; protein content: 85%) was dispersed in 1400 g of purified water, and sodium hydroxide was added to adjust the pH of the solution to 7.0. C. for 10 minutes to completely dissolve casein. Then, the temperature of the solution is cooled to 55 ° C.
1 g of TN6.0S (manufactured by Novo Nordisk; 1250 activity units / mg), 2 g of protease N Amano (manufactured by Amano Pharmaceutical Co .; 150,000 activity units / g), and protease A Amano (manufactured by Amano Pharmaceutical Co .; 10,000 activity units) /
g), and kept at 55 ° C. for 10 hours, heated at 90 ° C. for 15 minutes for both inactivation of the enzyme and sterilization of the solution.
After cooling to 0 ° C., filtration was performed using a diatomaceous earth Celite High Flow Super Cell (manufactured by Manville, USA; hereinafter, abbreviated as HSC) to collect a permeated fraction, followed by heating at 70 ° C. for 30 minutes. After cooling to 10 ° C. and adding 3% of activated carbon per solid content (manufactured by Takeda Pharmaceutical Co., Ltd .; carbofin; zinc chloride activated) for 5 hours, the mixture was filtered using diatomaceous earth HSC and permeated fraction And the permeated fraction was subjected to ultrafiltration membrane SIP-1013 (manufactured by Asahi Kasei Kogyo Co., Ltd .; molecular weight cut off 60).
The resulting fraction was collected by ultrafiltration according to (00), concentrated to 15% using a rotary evaporator, and lyophilized by a conventional method to obtain about 180 g of a powdery protein hydrolyzate.

Example 3 200 g of commercially available casein lactate (manufactured by New Zealand Daily Board; protein content: 85%) was dispersed in 1800 g of purified water, and the pH of the solution was adjusted to 6.5 by adding tripotassium phosphate. The casein was completely dissolved by heating at 80 ° C. for 10 minutes. Thereafter, the temperature of the solution was cooled to 50 ° C., and 2 g of sterilized pancreatin (manufactured by Amano Pharmaceutical Co., Ltd., 112000 activity units / g), 4 g of Protease A Amano (manufactured by Amano Pharmaceutical Co., 10,000 activity units / g), and FC- H
(2 g of Morinaga Milk Industry Co., Ltd., concentrated frozen solution of crushed cells of Lactobacillus helveticus) was added, and the mixture was kept at 50 ° C. for 18 hours.
Heat for 0 minutes, cool to 10 ° C., diatomaceous earth silica # 600
S (manufactured by Chuo Silica Co., Ltd.), and the permeated fraction was collected, heated at 75 ° C. for 10 minutes, concentrated to 15% concentration using a rotary evaporator, and concentrated at 10 ° C.
Then, 2% of activated carbon per solid content (manufactured by Ajinomoto Fine Techno Co., Inc., ZN; zinc chloride activated) was added, the mixture was maintained for 8 hours, and filtered using diatomaceous earth silica # 600S to collect a permeate fraction. , The permeated fraction was subjected to ultrafiltration membrane SEP-1013.
Ultrafiltration was performed using (Asahi Kasei Kogyo Co., Ltd., molecular weight cut-off 3000) to collect the permeated fraction, which was then freeze-dried by a conventional method to obtain about 165 g of a powdery protein hydrolyzate.

Example 4 200 g of commercially available casein lactate (manufactured by New Zealand Daily Board; protein content: 85%) was dispersed in 1300 g of purified water, and magnesium carbonate was added to adjust the pH of the solution to 7.5. For 10 minutes to completely dissolve casein. Thereafter, the temperature of the solution was cooled to 50 ° C., and Papain W-40 (manufactured by Amano Pharmaceutical Co., Ltd., 400 activity units / m)
g) and equine enzyme (manufactured by Amano Pharmaceutical Co., Ltd., 20000)
2 g of Sumiteam LP (manufactured by Shin Nippon Chemical Co., Ltd .; 50,000 activity units / g) was added, and the mixture was kept at 50 ° C. for 8 hours to combine deactivation of the enzyme and sterilization of the solution. Heat at 85 ° C. for 6 minutes, 130 ° C. for 2 seconds,
C., and filtered through a microfiltration membrane (trade name “Scepter”, manufactured by Gray Barr Co., USA) to collect a permeated fraction.
After heating at 10 ° C. for 10 minutes and concentrating to a concentration of 15% using a rotary evaporator, the mixture was cooled to 10 ° C., and activated carbon / cellulose fiber composite of 5% per solid content (Ecosorb, manufactured by US Graver Co., USA). , And filtered through a Buchner funnel according to a conventional method to collect a permeated fraction. The permeated fraction is subjected to ultrafiltration using an ultrafiltration membrane AIP-1013 (manufactured by Asahi Kasei Corporation; molecular weight cut off 6000). The permeated fraction was collected by filtration and then freeze-dried by a conventional method to obtain about 170 g of a powdery protein hydrolyzate.

Example 5 A commercially available whey protein isolate (produced by Mirai Co., protein content 90
%) Was dispersed in 1800 g of purified water, and potassium hydroxide was added to adjust the pH of the solution to 8.0.
After heating for 15 seconds, the temperature of the solution was cooled to 50 ° C., and sterilized pancreatin (manufactured by Amano Pharmaceutical Co., Ltd., 112000).
2 g of active unit / g), 4 g of protease A Amano (manufactured by Amano Pharmaceutical Co., Ltd., 10,000 active units / g), and Sumiteam FP (manufactured by Shin Nippon Chemical Co., Ltd., 50,000 active units / g)
And 1 g of FC-H (manufactured by Morinaga Milk Industry Co., Ltd .; concentrated frozen liquid of crushed cells of Lactobacillus helveticus), and kept at 50 ° C. for 8 hours to inactivate the enzyme and sterilize the solution. The mixture was heated at 90 ° C. for 10 minutes, cooled to 10 ° C., and filtered using diatomaceous earth HSC to collect a permeated fraction.
After heating at 30 ° C. for 30 minutes, cooling to 10 ° C., adding 3% of activated carbon per solid content (manufactured by Takeda Pharmaceutical Co., Ltd., strong Shirasagi) and holding for 5 hours, then using diatomaceous earth HSC The permeated fraction is collected by filtration, and the permeated fraction is separated by ultrafiltration membrane SE.
P-1013 (manufactured by Asahi Kasei Kogyo Co., Ltd., molecular weight cut off 3000)
To collect the permeate fraction, and then concentrated using a rotary evaporator to a concentration of 15%,
Lyophilized protein hydrolyzate of about 1
70 g were obtained.

[0070]

Industrial Applicability As described above in detail, the present invention relates to a method for producing a protein hydrolyzate from which coloring, an unfavorable flavor and the like and a causative substance thereof have been removed. The effects of the present invention are as follows. . 1) The method for producing a protein hydrolyzate of the present invention can remove coloring, unfavorable flavor, and the like, and its causative substances. 2) According to the method for producing a protein hydrolyzate of the present invention, it is possible to produce a protein hydrolyzate in which coloring by heating and generation of an undesirable flavor are suppressed.

 ──────────────────────────────────────────────────続 き Continuing from the front page (72) Inventor Zenta Takatsu 5-1-183 Higashihara, Zama-shi, Kanagawa Prefecture Morinaga Dairy Products Co., Ltd. No. Morinaga Dairy Co., Ltd., Nutrition Science Laboratory (72) Inventor Hirofumi Miyauchi 5-83, Higashihara, Zama-shi, Kanagawa Prefecture Morinaga Dairy Co., Ltd. No. 1-83 Morinaga Dairy Industry Co., Ltd. Nutrition Science Laboratory F-term (reference) 4B064 AG01 CA21 CB06 CD20 CD21 CE06 CE09 DA10

Claims (4)

[Claims] Claims 1. A protein material is degraded with a protease.
A method for producing a protein hydrolyzate, which comprises deactivating an enzyme by heating, filtering, heating at 65 to 90 ° C., and then performing activated carbon treatment and ultrafiltration. 2. The method for producing a protein hydrolyzate according to claim 1, wherein an ultrafiltration treatment is performed after the activated carbon treatment. 3. The production of the protein hydrolyzate according to claim 1 or 2, wherein the ultrafiltration treatment is performed by using an ultrafiltration membrane having a molecular weight cut-off of 2,000 to 6,000 and collecting a permeated fraction. Method. 4. The method for producing a protein hydrolyzate according to claim 1, wherein the activated carbon treatment is carried out by using activated carbon activated by a chemical and recovering a non-adsorbed fraction.