JP2001095538A - Oil separation-preventing agent for sources, sources and method for producing the same - Google Patents

Abstract

PROBLEM TO BE SOLVED: To obtain an oil separation-preventing agent for sources, capable of preventing the separation of the oil in the step for producing the sources, and further capable of preventing the separation of the oil generated in a final product shape after a heating treatment for sterilization, and further to provide a method for producing the sources. SOLUTION: This method for producing sources comprises formulating 0.05-3 pts.wt. oil separation-preventing agent for the sources containing polypeptides obtained by separately hydrolyzing 7S and 11S components in soybean proteins, with 100 pts.wt. sources.

Description

DETAILED DESCRIPTION OF THE INVENTION

[0001]

[0001] The present invention relates to the manufacture of sauces. In detail, pasta sauce such as tomato sauce, meat sauce, carbonara sauce, cream sauce,
For source foods such as Demigrass sauce, white sauce, stew, curry, etc., prevent the separation of oil contained in the sauce at the time of sauce production, and also prevent the separation of oil in the sauce during sterilization and heat treatment, to reduce the quality of the sauce. The present invention relates to an oil reserving agent for sauces for the purpose of improvement, and to sauces and a method for producing the same.

[0002]

2. Description of the Related Art Sauces in the present invention refer to pasta sauces such as tomato sauce, meat sauce, carbonara sauce and cream sauce, and source foods such as demiglace sauce, white sauce, stew and curry. These sauces, in the manufacturing process, vegetable oils such as olive oil, tallow, lard, chicken fat, cheese, milk,
In many cases, butter and the like are added for the purpose of flavoring, and beef, pork, pork, chicken, etc. containing beef tallow, lard, and chicken fat are added as ingredients. In addition, most sauces include vegetables and fruits such as tomatoes and onions, and the pH of the product is weakly acidic, about 4 to 6, except for white sauce. Other ingredients in the sauce include wheat flour, starch, thickening polysaccharides, etc.
Includes spices, salt and seasonings. These sources are
Spaghetti, beef stew,
It is used as a raw material for secondary processing such as cream stew, curry and rice, and is manufactured and sold in the form of pack packaging or canning by sterilizing boiled sauce by retort heat sterilization or the like.

As described above, these sauces often contain vegetable oils such as olive oil, and fats such as beef tallow, lard, chicken fat and butter, but the components themselves contained in the sauces themselves retain oils and fats. Since there are few components having the effect of reducing the amount of oil, fats and oils may be separated in the step of boiling down the sauce. Especially in the case of mass production, oil separation makes the product uneven, cleaning work takes a lot of trouble, and oils and fats emerge on the surface at the stage of final product form after sterilization heat treatment. There has been a problem that the appearance of the sauce itself is deteriorated, such as an oil pool or the solidified solidified state, leading to a reduction in product quality. However, despite these problems, no effective method for solving this problem has been reported in the past. The reason for this is that the sauce preparation is limited to a gentle stirring method that does not apply a shear, that is, it cannot emulsify oils and fats contained in a strong shear such as a high-pressure homogenizer. Inability to bring out the oil-retaining power of the protein. It is also considered that one of the reasons is that the product pH is weakly acidic and the solubility is lowered even when trying to use the protein, so that the environment is unable to exert sufficient oil-retaining ability. As described above, at present, there is no effective method in the technology for preventing the separation of fats and oils from sauces described in the present invention.

[0004]

SUMMARY OF THE INVENTION As described above, the present invention relates to the preservation of sauces for preventing oil separation during the production process of sauces and for preventing oil separation occurring in the final product form after sterilization and heat treatment. By proposing an oil agent and a method for producing the same, the aim is to improve manufacturing workability and prevent deterioration in product quality.

[0005]

Means for Solving the Problems The inventors of the present invention have conducted intensive studies to achieve the above object, and have found that a low-denatured soybean protein containing both 7S and 11S components, which are main constituents of soybean protein, is used as a substrate. The two-step enzymatic decomposition reaction, ie, the 7S component by the first decomposition reaction, the 11S component by the second decomposition reaction, or conversely, the 11S component by the first decomposition reaction, and the 7S component by the second decomposition reaction, respectively It has been found that polypeptides obtained by hydrolysis are excellent in the effect of preventing oil separation of sauces described in the present invention and exhibit an effective effect as an oil retaining agent for sauces, which has led to the present invention. That is, the present invention relates to 7S and 1
1S component is separately hydrolyzed and a polypeptide containing both hydrolysates, more specifically, a two-stage process using a low-denatured soybean protein containing both 7S and 11S components, which are main constituents of soybean protein, as a substrate The 7S component is decomposed by the first decomposition reaction, and the 11S is decomposed by the second decomposition reaction.
S component or vice versa by the first decomposition reaction
An oil sorbent of a source containing a polypeptide obtained by hydrolyzing each of the 7S components by a second decomposition reaction as an active ingredient, and 0.05 to 3 parts by weight of the polypeptide based on 100 parts by weight of the source Then, a method for producing sauces produced by heat sterilization and producing
It relates to sauces containing 0.05 to 3 parts by weight based on parts by weight.

[0006]

BEST MODE FOR CARRYING OUT THE INVENTION The soybean protein used in the present invention is a low-denatured, low-denatured defatted soybean defatted with a solvent such as whole soybean or hexane, or a soymilk or defatted soybean milk obtained by extracting these with water. An isolated soybean protein, which is subjected to isoelectric focusing using an acid to recover the precipitated fraction, can be exemplified as the substrate. In particular, when the isolated soybean protein is used as a substrate, the finally obtained polypeptide has excellent flavor and quality as an oil retaining agent for sauces, and is preferably a low-denatured defatted soybean (NSI 60 or more, preferably NSI 80 or more) having a pH of 6 to 9, Preferably pH6.
7 to 15 times water in the range of 5 to 8.0, 60 ° C or less,
Preferably, the extract is extracted at 50 ° C. or lower, and the defatted soymilk from which the okara component has been removed is subjected to isoelectric point precipitation to collect a precipitate fraction. These defatted soybeans, defatted soymilk, and isolated soybean proteins obtained by decomposing or removing phytic acid during the preparation process are also effective in improving the quality of the oil retaining agent for sauces. As an example of separately hydrolyzing, first,
The case where the 11S component is selectively hydrolyzed by the first decomposition reaction is as follows. Using the above-mentioned soybean protein as a substrate, a protein hydrolase is used in an amount of 0.001 to 1%, preferably 0.01 to 0.5%, based on a solid content of a substrate, in a solution having a protein concentration of 1% to 30%. At a temperature of 45 ° C. or lower, preferably at 30 to 40 ° C., at a pH of 3.0 or lower, preferably at a pH of 1.8 to 2.5, for a short time within 4 hours of the reaction time, preferably within 10 minutes to 2 hours. 0.22M TCA
(Trichloroacetic acid) It is preferable to react until the solubility becomes 10 to 50%. If the reaction temperature exceeds 45 ° C., the 7S component in addition to the 11S component is also easily decomposed at the same time, and it becomes difficult to selectively decompose the 11S component. And the quality as an oil retainer for sauces decreases. Also, if the reaction time is too long, the decomposition product of the 11S component is further reduced in molecular weight, so that the quality is deteriorated as described above, which is not preferable.

[0007] The protease used here is pH
Suitable are all proteases having an activity of 3.0 or less, such as animal-derived pepsin, cassepsin and a series of microbial-derived aspartic proteases such as Newase F and Protease M (manufactured by Amano Pharmaceutical Co., Ltd.). And a commercially available enzyme preparation such as Sumiteam LP (manufactured by Shin Nippon Chemical Co., Ltd.). Among them, pepsin is preferred. 7
In order to selectively hydrolyze the S component by the first decomposition reaction, the above-mentioned soybean protein is used as a substrate, and a protein hydrolase is added to a solution having a protein concentration of 0.5% to 20% with respect to the solid content of the substrate. 0.001 to 0.5%, preferably 0.01 to 0.5%
At a reaction temperature of 50 ° C. or higher, preferably 55 ° C.
PH above pH 3.0 at ~ 85 ° C, preferably pH
The reaction can be carried out at a rate of 3.5 to 8.0 and a short time within 2 hours of the reaction time, preferably about 10 minutes to 30 minutes, until the solubility of 0.22M TCA becomes 10 to 50%. The protease used here has a temperature of more than 50 ° C and 90 ° C.
It is necessary that the enzyme agent has a proteolytic activity at a temperature lower than 0 ° C, preferably 55 to 85 ° C. These are not particularly limited in their origin such as commercially available enzyme preparations derived from plant or animal organs or microorganisms.

When the selective hydrolysis is recovered from the reaction solution after the completion of the first decomposition reaction, pH fractionation is simple and suitable, and when the selective hydrolysis of the 11S component is recovered, the pH is 3
-5, preferably in the range of pH 3.5-4.5,
When recovering the selective hydrolyzate of the S component, the pH is adjusted to pH 3 to 6, preferably pH 3.5 to 5.5, and the supernatant fraction mainly composed of the selective hydrolyzate is obtained. The sediment fraction mainly composed of the fractions is collected by centrifugation or filter press separation.

Next, the second decomposition reaction will be described. The precipitate fraction obtained by separation after the first decomposition reaction (7)
S component or a fraction rich in 11S component)
The second decomposition reaction is performed under different conditions from the first decomposition reaction.
For example, after the first decomposition reaction of the 11S component, 45
The fraction enriched in the 7S component is subjected to a second decomposition reaction at a reaction temperature higher than 0 ° C. In this case, it is particularly preferable to carry out at pH 3.0 or lower and at 50 ° C. or higher. After the first decomposition of the 7S component, the fraction rich in the 11S component undergoes a second decomposition reaction. In this case, it is particularly preferable to carry out the reaction at a pH of 3.0 or less and a reaction temperature of 45 ° C. or less. The 7S component undergoes a first decomposition reaction, and 11S
When a fraction rich in components is subjected to the second decomposition reaction, a separation operation after the first decomposition reaction is not necessarily required, and the first decomposition reaction solution can be directly transferred to the second decomposition reaction. The proteolytic enzyme used in the second decomposition reaction may have any activity at the reaction pH, and examples thereof include the aforementioned enzymes. The reaction time is a short time within 2 hours, preferably about 10 minutes to 30 minutes, and it decomposes to about 10 to 50% at a solubility of 0.22 M TCA.

[0010] The decomposition product obtained in the first decomposition reaction and the decomposition product obtained in the second decomposition reaction are used in their entirety, or one or both decomposition products are purified to an arbitrary ratio such as 9%. : 1 to 1: 9 to prepare a polypeptide derived from the soybean protein of the present invention. In addition, a polypeptide having good properties can be obtained in high yield by containing both hydrolysates.

[0011] The polypeptide of the present invention can also be expressed as having the following physicochemical properties. 1) Polypeptides are mainly composed of polypeptides having a molecular weight in the range of 5,000 to 35,000 as analyzed by SDS polyacrylamide gel electrophoresis containing mercaptoethanol. 2) The polypeptide has a main peak molecular weight of about 8,000 by gel filtration, and a molecular weight range of 5,000 to 30,000.
Is 70% or more of the total peak area, and has a molecular weight of 5,
Less than 000 is 20% or less of the total peak area area. 3) The solubility of 0.22M TCA is 30 to 90%.

Analysis of the main components of the polypeptide of the present invention can be performed by a known analysis method using SDS-polyacrylamide gel electrophoresis containing mercaptoethanol (hereinafter referred to as SDS-PAGE). The molecular weight of each polypeptide can be evaluated, and quantification using a densitometer is also possible. The major components of the polypeptides of the invention typically have a molecular weight of about 10,000, about 20,000, about 25,000, about 29,000, about 3
2,000. When, for example, a fraction obtained by selectively hydrolyzing 11S is used in a larger amount than in a case where both fractions are used in total, the component having a molecular weight of 10,000 among the above is increased, and For example, there are components that do not easily appear depending on the mixing ratio of both hydrolysates, such as a decrease. The molecular weight of the polypeptide of the present invention was evaluated by the gel filtration method under the following conditions. Conditions) Column: SW3000XL, manufactured by Tosoh Corporation
(7.6 mm × 30 cm) Eluate: Elution was performed at a flow rate of 0.8 ml / min using a 25 mM phosphate buffer (pH 7) containing 1% SDS and 0.2 M NaCl. Detection; absorbance at 220 nm. The sample to be analyzed is added to the above eluate at a concentration of 0.5% (0.1%).
% Mercaptoethanol), boiled for 2 minutes to completely dissolve, and used for analysis. The molecular weight was evaluated based on the elution time of a standard protein having a known molecular weight.
The polypeptide of the present invention has a molecular weight of 5,000 to 30,000 at 70% or more of the total peak area and a molecular weight of 5,0.
Less than 00 is 20% or less of the total peak area area. Although the degree of hydrolysis can be determined to some extent by the above SDS-PAGE, it can also be evaluated using the 0.22 M TCA solubility, which is generally used as a protein degradation rate, as an index. The solubility of the polypeptide of the present invention in the range of 0.22M TCA is 30 to 9%.
0%, preferably 40-90%, is appropriate.

[0013] When referring to the oil retention in the present invention, the evaluation was made by measuring the oil separation rate. The oil separation rate was 25% soybean oil, 0.2% sample concentration, and the balance of water, using an emulsifier (POLYTRON KINEMATICA AG).
At 10,000 RPM for 1 minute to prepare an emulsified solution.
Next, a certain amount of this emulsified solution was put into a centrifuge tube with a memory, and centrifuged at 2,000 RPM for 20 minutes. After centrifugation, the height (B) of the separated oil layer (supernatant) was measured, and the ratio of the oil layer (supernatant) to the blank (A) with no sample added was shown as% oil separation. Oil separation rate (%) = B / A × 100 In the evaluation, the smaller the oil separation rate, the higher the oil retention power. The oil retaining power of the polypeptide of the present invention is 40 or less at pH 5,
Preferably, it satisfies 30 or less, more preferably 20 or less. The above is the preparation of the polypeptide of the present invention and its properties.

The source oil reserving agent of the present invention may be in the form of an aqueous solution, a paste, or a powder as long as it contains the above-mentioned polypeptide. The amount of the polypeptide of the present invention used is 10
0.05 to 3 parts by weight, preferably 0.2 to 1 part by weight, of the polypeptide solid is added to 0 parts by weight. 0.
If the addition is less than 05 parts by weight, the effect of retaining oils and fats in the sauce is poor, and oil separation is likely to occur. If the addition exceeds 3 parts by weight, the obtained oil retention power is not so much higher than the ratio of the increment of addition. Therefore, the merit of addition is small, and the change in color tone and the unique flavor and bitterness of soybean protein can be felt, which is not preferable. The addition time of the polypeptide of the present invention is not particularly limited, but at the time of blending of the source raw material, the subsequent heating and stewing step, or at any stage before the final sterilization heating, leave it as a powder or preferably as an aqueous solution. Add and mix uniformly. In addition, heat sterilization of sauce is UH
Methods such as T and retort heat sterilization can be used. The effect of the lubricating agent of the present invention is further enhanced when used in combination with a thickening polysaccharide such as xanthan gum, and the combined use with a thickening polysaccharide is also effective.

[0015]

EXAMPLES Hereinafter, the embodiments of the present invention will be described in detail with reference to examples, but the technical scope of the present invention is not limited by these.

Production Example 1 (T-1) Low-denatured defatted soybean flakes (NSI 9) manufactured by Fuji Oil Co., Ltd.
To 0), 10 times the amount of warm water at 40 ° C. was added, and the pH was adjusted to 7.0 by adding a NaOH solution. Mix this gently and add 1
The extract was extracted for a time, and separated into okara of the insoluble fraction and skim milk of the soluble fraction by a centrifuge. Hydrochloric acid was added to the obtained defatted soy milk to adjust the pH to 4.5, and the resulting protein precipitate was collected by a centrifuge to obtain a separated soy protein curd. Then
Water was added to the isolated soybean protein curd, and hydrochloric acid was added to adjust the pH to 2.0 and the isolated soybean protein to 10% by weight. To 1 L of this solution, 200 mg of pepsin (manufactured by Nippon Biocon) was added.
For 30 minutes (first reaction). As a result of analyzing the reaction solution by electrophoresis, the 11S component in the soybean protein was selectively hydrolyzed, the band having the mobility corresponding to 11S disappeared, the low molecular weight peptide component derived from the 11S component, and A band having a mobility corresponding to the 7S component that had not undergone decomposition was observed. The reaction solution is pH adjusted using NaOH.
Adjust the precipitate to 4.5, and precipitate the resulting precipitate with a centrifuge.
It was separated into a supernatant fraction containing the decomposition product of the component and a precipitation fraction (undegraded fraction) rich in the 7S component. The final 0.22M TCA solubility of the reaction solution of the pepsin degradation product was 25%,
The final 0.22 M TCA solubility of the supernatant fraction after pH fractionation was 7
The volume recovery of the supernatant fraction after the pH fractionation was 2%, and the solid recovery of the supernatant fraction after the pH fractionation was 24%. 7S
The precipitated fraction (undegraded fraction) rich in components was adjusted to pH 2.0 and a solid content of 7% by weight by adding water and hydrochloric acid, and 100 mg of pepsin (manufactured by Nippon Biocon) was added to 1 liter of this solution. The hydrolysis was carried out again at 60 ° C. for 20 minutes (second reaction). In addition, the final 0.22M of the reaction solution after pepsin decomposition
The TCA solubility was 46%.

The reaction solution of the precipitate fraction was mixed with the supernatant fraction containing the 11S component in a total amount, and the mixture was adjusted to pH 6.5 using a NaOH solution. Peptide (T-1) was prepared. The composition of the resulting polypeptide was determined by SDS electrophoresis analysis to have a molecular weight of 5,000.
90% or more in the range of ~ 35,000. The gel filtration analysis revealed that the main peak molecular weight was about 8,000.
The peak area in the molecular weight range of 5,000 to 30,000 was about 85%. The general analysis values were as follows: crude protein 84%, ash 11%, moisture 5%
And the solubility of 0.22M TCA was 52%.

Production Example 2 (T-2) A mixture of the supernatant fraction of the first reaction and the reaction solution of the second reaction in Production Example 1 was used, and 3% by weight of the solid content thereof was hydroxylated. Ca was added, and the pH was further adjusted to 6.5 using a NaOH solution. This was heated at 140 ° C. for 7 seconds at a high temperature for a short time, then cooled to room temperature, and the insoluble components were centrifuged at 5000 G for 10 minutes. Then, a mixed supernatant fraction was obtained, and this was spray-dried to prepare a polypeptide (T-2). As a result of SDS electrophoresis analysis, the composition of the obtained polypeptide was found to be 80% or more in the molecular weight range of 5,000 to 35,000. As a result of gel filtration analysis, the main peak molecular weight was about 8,000, and the molecular weight range was 5,000 to 30,000.
The peak area in the range of 000 was about 80%, and the molecular weight of less than 5,000 was 15%. And the general analysis values are as follows: crude protein 76%, ash content 15%, moisture 5%,
The solubility of 0.22M TCA was 70%.

Production Example 3 (T-3) The isolated soybean protein curd prepared in the same manner as in Production Example 1 was adjusted to pH 3.5 and 10% by weight of isolated soybean protein by adding hydrochloric acid and adding hydrochloric acid. On the other hand, 200 mg of pepsin (Nippon Biocon) was added and hydrolyzed at 70 ° C. for 30 minutes (first reaction). As a result of analyzing the reaction solution by electrophoresis, the 7S component in the soybean protein was selectively hydrolyzed, the band having the mobility corresponding to the 7S component disappeared, and the polypeptide component derived from the 7S component and the degradation were observed. Not 11S
A band having a mobility corresponding to the component was observed. The reaction solution was cooled to 37 ° C., adjusted to pH 2.0 by adding hydrochloric acid, added with 200 mg of pepsin, and hydrolyzed at 37 ° C. for 30 minutes (second reaction). The pH of the reaction solution was adjusted to 6.5 using a NaOH solution, and then the solution was spray-dried to obtain a polypeptide (T-
3) was prepared. The composition of the resulting polypeptide is SDS
As a result of the electrophoresis analysis, the molecular weight was 5,000 to 35,000.
Or more in the range of 90%. As a result of gel filtration analysis, the main peak molecular weight was about 8,000, and the peak area in the molecular weight range of 5,000 to 30,000 was about 85%. The general analysis values were as follows: crude protein 85%, ash content 10%, moisture 5%, 0.22
The M TCA solubility was 56%.

Comparative Production Example 1 (t-1) Hydrolyze the isolated soybean protein curd of Production Example 1 and add hydrochloric acid to add p.
H2.0, 10% by weight of isolated soybean protein, 200 mg of pepsin was added to 1 L of this solution, and the mixture was hydrolyzed at 60 ° C. for 2 hours. When the reaction solution was analyzed by electrophoresis, not only 11S but also 7S was decomposed. This reaction solution
The pH was adjusted to 6.5 using a NaOH solution, and the supernatant fraction was separated by a centrifugal separator. This was sterilized, heated, and spray-dried to prepare a polypeptide (t-1).

Comparative Production Example 2 (t-2) In the preparation of Comparative Production Example 1, a pepsin decomposition reaction solution was used.
The resulting precipitate was adjusted to pH 4.5 using a NaOH solution, and the resulting precipitate was separated into a supernatant fraction and a precipitate fraction by a centrifugal separator. The precipitate fraction was hydrolyzed, and hydrochloric acid was added to adjust the pH to 2.0 and 7. Weight percent, and add 100 mg of pepsin to 1 liter of this solution,
After hydrolyzing again at 60 ° C. for 20 minutes, the mixture was mixed with the supernatant fraction to form a mixture, adjusted to pH 6.5 with a NaOH solution, sterilized, heated and spray-dried to obtain the polypeptide ( t-2) was prepared.

Comparative Production Example 3 (t-3) The isolated soybean protein curd of Production Example 1 was hydrated, adjusted to pH 7.0 using a NaOH solution, sterilized, heated and spray-dried to obtain isolated soybean protein (t-3). -3) was prepared.

Example 1 (Evaluation of Oil Retaining Power) Production Examples (T-1 to 3) and Comparative Production Examples (t-1 to 3)
Was evaluated for oil retention. The solution pH at the time of emulsification was 5, and it was prepared using citric acid and phosphate buffers. Table 1 shows the measurement results of the oil retention of each sample.

[0024]

[Table 1]

As shown in Table 1, T-1 to T-3 of the product of the present invention
Shows that the oil separation rate is about 20% level, the oil retention under pH 5 condition is significantly higher than that of other comparative production examples, and it is understood that it has an excellent oil retention. On the other hand, Comparative Production Example t-
In all of the samples 1 to 3, the oil separation rate was about 50%, and the oil retention was inferior.

Example 2 (Source) Hereinafter, Examples and Comparative Examples will be described using specific sources.
The effect of the present invention is further clarified. In addition, the part illustrated below means a weight basis. The evaluation was made using commercially available tomato sauce (oil content: 7.3%) and meat sauce (oil content: 3.2).
%), Demiglace sauce (oil content: 6.8%), white sauce (oil content: 5.0%), curry (oil content: 8.7%), total 5
Product was used.

For tomato sauce, meat sauce and curry, 100 parts of sauce are prepared, and production examples T-1, T-2 and T-
3 and Comparative Production Examples t-1, t-2, and t-3 were adjusted to a total of 110 parts by adding 0.5 parts and water (the polypeptide in the final preparation source was 0.45% compounded). ). For the Demiglass sauce and the white sauce, 0.5 part of Production Examples T-1, T-2, and T-3 and Comparative Production Examples t-1, t-2, and t-3 and water were added to 100 parts of the sauce. To prepare a total of 180 parts (the polypeptide in the final preparation source was blended at 0.28%).

(Preparation Method and Evaluation of Each Source) A test sample (polypeptide) was dissolved in water to be added, and then added to a commercial source. 400 g of this sauce was placed in a heating vessel equipped with a propeller stirrer, heated to 95 ° C., mixed by heating for 15 minutes, packed in a retort bag, and subjected to a retort heat sterilization treatment at 120 ° C. for 10 minutes. The sauce after the heat sterilization treatment was allowed to stand at 50 ° C. overnight, and the amount of oil separated from the sauce was sensory evaluated to confirm the effect. Table 2 summarizes the evaluation results when used for each source.

[0029]

[Table 2]

[0030] 0.5 parts of the product of the present invention T-1, T-2, T-3 is added to each source (0.45% and 0.2% parts of the polypeptide in the final preparation source are blended). By doing so, the oil separation was clearly reduced as compared to the control additive-free product, and the color tone of the sauce itself was not affected. Also,
Addition of the products T-1, T-2, and T-3 of the present invention hardly affected the flavor. Comparative Production Example t-1,
0.5 parts of t-2 and t-3 were added to each source (the polypeptide in the final prepared source was 0.45% and 0.1 part).
Each of the sauces (containing 28%) had an effect of slightly reducing oil separation compared to the case where no control was added, but it was hardly recognized as a sufficiently effective effect, and the source color also changed. As can be seen, there was a clear difference in effect from the product of the present invention. The difference in oil retention and color change is that the product of the present invention
It is considered to be due to the fact that the emulsifying power and the solubility in the acidic region are superior to the soybean protein in the comparative production example.

[0031]

According to the present invention, it is possible to prepare sauces in which oil separation during the production process of sauces and oil separation generated in the final product form after the sterilization heat treatment are prevented. To improve workability and prevent deterioration of product quality.

 ──────────────────────────────────────────────────続 き Continuing on the front page (72) Kazunobu Tsumura 4-3 Kinudai, Taniwahara-mura, Tsukuba-gun, Ibaraki Prefecture Inside Tsukuba Research and Development Center, Fuji Oil Co., Ltd. 4-3, Fuji Oil Co., Ltd. Tsukuba R & D Center F-term (reference) 4B036 LC05 LE02 LF03 LF04 LF05 LH16 LH26 LK06 LP18

Claims (4)

[Claims] 1. A source oil reserving agent containing a polypeptide obtained by separately hydrolyzing the 7S and 11S components in soybean protein. 2. A source oil reserving agent containing a polypeptide derived from soy protein and having the following properties. 1) Polypeptides are mainly composed of polypeptides having a molecular weight in the range of 5,000 to 35,000 as analyzed by SDS polyacrylamide gel electrophoresis containing mercaptoethanol. 2) The polypeptide has a main peak molecular weight of about 8,000 by gel filtration, and a molecular weight range of 5,000 to 30,000.
Is 70% or more of the total peak area, and has a molecular weight of 5,
Less than 000 is 20% or less of the total peak area area. 3) The solubility of 0.22M TCA is 30 to 90%. 3. Sources comprising the polypeptide according to claim 1 or 2 in an amount of 0.05 to 3 parts by weight based on 100 parts by weight of the source. 4. A method for producing sauces, comprising mixing 0.05 to 3 parts by weight of the polypeptide according to claim 1 or 2 with respect to 100 parts by weight of the sauce, and sterilizing by heating.