JP3738614B2 - Emulsifier composition and acidic oil-in-water emulsion using the same - Google Patents

Description

表１に示すように、ポリペプチドとＳＳＰＳ、或いはＣペクチンを混合することで、相乗的にｐH ４の乳化活性が顕著に上昇することが判る。また、低分子のペプチドでは効果はないことが判る。
【００２８】
実施例１
前記製造例１にて作成したポリペプチド（Ｔ−１）５０重量部とＳＳＰＳ５０重量部を均一に混合し、乳化剤組成物を調製した（以下Ｍ−１とする）。配合表の成分のうち、サラダ油以外をケンウッドミキサー（愛工舎製作所社製「プロKM- ２３０」）にて攪拌混合後、サラダ油を添加しながら乳化した。そして、乳化物をコロイドミル（Ｆｒｙｍａ社製）にて均質化し、マヨネーズ様乳化物を調製した。

Ｍ−１と、比較としてポリペプチド（Ｔ−１）のみにて作成したマヨネーズ様乳化物（pH４．２）の平均乳化粒子径及び−３０℃で１日凍結し、その後解凍した状態を観察した結果を以下に示す。

Ｍ−１はＴ−１に比べ、良好な乳化物が得られ、また凍結に対しても安定なマヨネーズ様乳化物が調製可能であった。
【００２９】
実施例２
前記製造例２にて作成したポリペプチド（Ｔ−２）５０重量部とＰペクチンを５０重量部を均一に混合し、乳化剤組成物を調製した（以下Ｍ−２とする）。尚、Ｐペクチンは乾燥馬鈴薯粕を５％濃度となるように水に分散させ、ｐH を塩酸で４．５に調整し、１２０℃、３０分加熱し、抽出液を得、これを凍結乾燥して製造した。以下の配合の成分を混合し、６０℃にて超音波乳化器を用い、コーヒークリーム用乳化物を調製した。尚、比較として、ポリペプチド（Ｔ−２）のみを用いたコーヒークリーム用乳化物も調製した。

市販インスタントコーヒー（ネスレ社製）３０ｇ、砂糖５０ｇを１L の熱湯で溶解させ、８０−８５℃に保温した。このコーヒー液１００ｍｌ（pH５）に、上記コーヒークリーム用乳化物を１０ｍｌずつ添加し、状態を観察した。

Ｍ−２はＴ−２に比べ、より良好なコーヒークリーム用乳化物が調製可能であった。
【００３０】
【発明の効果】
食品をはじめ化粧品、トイレタリー製品、医薬品更には工業用途などの様々な分野において利用できる乳化剤組成物、特に酸性水中油型乳化物の製造に適した乳化剤組成物を提供することが可能となった。[0001]
BACKGROUND OF THE INVENTION
The present invention relates to an emulsifier composition comprising a polypeptide and a water-soluble polysaccharide, and an oil-in-water emulsion obtained using the same.
[0002]
[Prior art]
In recent years, with the avoidance of consumers' use of synthetic additives, development of natural materials to replace synthetic emulsifiers has been demanded. Soy protein as a natural material has been developed and studied as an emulsifier, and a method for enzymatically degrading soy protein under specific conditions (Japanese Patent Laid-Open No. 56-26171, Japanese Patent Laid-Open No. 57-16674, Japanese Patent Laid-Open No. Hei. 6-197788), a method using a glycinin acidic subunit focused on soybean protein components (Japanese Patent Laid-Open No. 63-36748), a method using a glycinin basic subunit, and the like are known. The method still does not have sufficient emulsifying power.
[0003]
A method for improving the emulsifying power by adding a protein degradation product to water-soluble hemicellulose for an emulsified preparation has been proposed (JP-A-7-97339). However, the proteolysate used here is a low molecular weight peptide having about 2 to 10 amino acids and is applied to a preparation having a relatively low oil content in the neutral range. Not applicable to oil-in-water emulsions. In addition, a method of using water-soluble soybean polysaccharide or the like in an acidic beverage with a relatively low oil content (Japanese Patent Laid-Open No. 5-7458) is disclosed, but protein particles in the acidic beverage cause aggregation, precipitation, and phase separation. The purpose is to prevent this. Furthermore, an attempt to use cyclodextrin in combination in the production of an oil-in-water emulsion has also been proposed (Japanese Patent Application Laid-Open No. 10-262560).
[0004]
[Problems to be solved by the invention]
In view of the above circumstances, the present invention provides an emulsifier composition that can be used in various fields such as foods, cosmetics, toiletries, pharmaceuticals, and industrial applications, particularly an emulsifier composition suitable for the production of acidic oil-in-water emulsions. It is to provide.
[0005]
[Means for solving the problems]
As a result of intensive studies on solving the above problems, the present inventors have found that an emulsifier composition containing a soybean protein obtained by a specific decomposition method and a water-soluble polysaccharide in a specific ratio has a wide pH range. It showed excellent emulsifying power, and was found to be particularly suitable for the preparation of emulsions in the acidic range, thereby completing the present invention.
That is, the present invention provides an emulsifier composition containing a water-soluble polysaccharide and a polypeptide having the following properties.
1) Mainly a polypeptide having a molecular weight in the range of 5,000 to 35,000 as analyzed by SDS polyacrylamide gel electrophoresis containing mercaptoethanol.
2) The main peak molecular weight by gel filtration is about 8,000, the molecular weight range 5,000 to 30,000 is 70% or more of the total peak area, and the molecular weight less than 5,000 is 20% of the total peak area. It is as follows.
3) It is 30-90% by 0.22M TCA solubility rate.
This polypeptide is a polypeptide obtained by separately hydrolyzing 7S component and 11S component in soybean protein, and is an emulsifier composition containing this polypeptide and water-soluble polysaccharide. The present invention provides an emulsifier composition characterized in that the weight ratio of the water-soluble polysaccharide to the total weight of saccharides is 0.1 to 0.9, and an acidic oil-in-water emulsion using the same. The water-soluble polysaccharide in the emulsifier composition is preferably derived from soybean, citrus fruit or potato. Furthermore, it becomes possible to produce a good oil-in-water emulsion using 0.01 to 10% by weight of the emulsifier composition of the present invention. In particular, an acidic oil-in-water emulsion having a pH of 3 to 6 and an acidic oil-in-water emulsion having a relatively high oil content of 5 to 80% can be produced.
[0006]
DETAILED DESCRIPTION OF THE INVENTION
As the polypeptide used in the emulsifier composition of the present invention, it is desirable to use a polypeptide obtained by a specific decomposition method described below.
That is, a low-modified soybean protein containing both 7S component and 11S component, which are main components in soybean protein, is used as a substrate in a two-stage enzymatic degradation reaction, that is, 7S component by the first degradation reaction, and 11S by the second degradation reaction. The polypeptide obtained by hydrolyzing the component, or conversely, the 11S component by the first decomposition reaction and the 7S component by the second decomposition reaction, is an effective polypeptide for solving the above problems, and is not decomposed. It is difficult to solve the above problems with isolated soybean protein, non-selectively hydrolyzed degradation products, low molecular weight peptides, and amino acids.
Analysis of the main components of the polypeptide of the present invention can be performed by a known analytical method called SDS-PAGE. The molecular weight of each polypeptide is determined from the mobility of a standard molecular weight marker, and the content of each polypeptide is determined by quantification using a densitometer. Can be evaluated. The main components of the polypeptide of the present invention to be evaluated in this way include components having a molecular weight of about 10,000, about 20,000, about 25,000, about 29,000, about 32,000, etc. From the quantification by the tometer, the area area of the polypeptide having a molecular weight in the range of 5,000 to 35,000 is about 50% or more with respect to the total area area of the polypeptide of the present invention. Compared with the case where all the fractions obtained by selectively hydrolyzing the 7S component and the 11 component separately are used, for example, when a large amount of the fraction obtained by selectively hydrolyzing the 11S component is used, the molecular weight of about 10 Although the composition of the polypeptide having a molecular weight in the range of 5,000 to 35,000 varies to some extent depending on the blending ratio of both fractions, such as an increase in the components of 1,000 and a decrease in other components, it is 5 for the total area area. The area area of the polypeptide in the range of 3,000 to 35,000 is not less than about 50%.
[0007]
The molecular weight of the polypeptide of the present invention by gel filtration was evaluated under the following conditions.
(Condition) Column: manufactured by Tosoh Corporation, SW3000XL (7.6 mm × 30 cm), eluent: eluted with 25 mM phosphate buffer (pH 7) containing 1% SDS and 0.2 M NaCl, at a flow rate of 0.8 ml / min. . Detection; absorbance at 220 nm.
The sample to be analyzed was dissolved in the eluate at a concentration of 0.5% (including 0.1% mercaptoethanol), and then dissolved by boiling for 2 minutes for analysis. The molecular weight was evaluated based on the elution time of a standard protein with a known molecular weight.
[0008]
The degree of hydrolysis is suitably 30 to 90%, preferably 40 to 90%, based on the solubility of 0.22M TCA (trichloroacetic acid) generally used as the protein degradation rate.
[0009]
By having the above properties, the polypeptide of the present invention is excellent in emulsifying properties and foaming properties. In the present invention, the emulsifying power is evaluated by measuring the emulsifying activity. The emulsification activity was adjusted to pH 4, pH 5.5 and pH 7 by adding 1 ml soybean oil to 3 ml sample solution (1 wt%), preparing an emulsion with an ultrasonic disperser, and diluting 1000 times with a 0.1% SDS solution. Then, the solution turbidity (absorbance at 500 nm) was measured. Evaluation judges that emulsification power is so high that the turbidity value is high. The emulsifying power of the polypeptide of the present invention is 0.15 or more at pH 4, preferably 0.2 or more, more preferably 0.25 or more, 0.4 or more at pH 5.5, preferably 0.5 or more, more preferably It can satisfy 0.6 or more, 0.8 or more at pH 7, preferably 1.0 or more, more preferably 1.2 or more.
[0010]
In the present invention, the foaming power is evaluated based on the foaming capacity and stability in aqueous and oil systems. Here, the evaluation was based on the bubble capacity and its stability in a more severe oil system. That is, 4 ml of soybean oil was added to 100 ml of a 5% by weight aqueous solution, and this was treated with a homogenizer (manufactured by Nippon Seiki Co., Ltd.) at 10,000 rpm for 1 minute. It was measured. The stability evaluation was judged from the change in foam volume (ml) immediately after foaming and after standing for 1 hour. The foaming power of the polypeptide of the present invention is 250 or more, preferably 300 or more, more preferably 350 or more.
[0011]
As a mode of separately hydrolyzing the 7S component and the 11S component in the soybean protein, it is possible to hydrolyze the soybean protein after separating it into 7S and 11 components by a known method. In general, it is poor in separability for severe pH and salinity control for industrial implementation, and in order to obtain a predetermined hydrolyzate, the yield of undecomposed components is large and the yield is poor. . In this regard, as a method of separately hydrolyzing the 7S component and the 11S component, either the 7S component or the 11S component in the soybean protein is first selectively hydrolyzed, and then the hydrolyzed fraction and the undegraded fraction. A method of further hydrolyzing the undecomposed fraction without separating or separating the fraction is excellent.
[0012]
That is, the polypeptide of the present invention is preferably subjected to a two-stage enzymatic degradation reaction using soybean protein containing both 7S component and 11S component, which are main components of soybean protein, as a substrate. Alternatively, the 11S component may be selectively hydrolyzed by the second decomposition reaction, or the 11S component by the first decomposition reaction, and the 7S component by the second decomposition reaction. A novel polypeptide of the nature can be easily obtained.
[0013]
The soy protein used for selective hydrolysis is preferably unmodified or low-denatured. Low-denatured defatted soybeans defatted with a solvent such as whole soybeans or hexane, or soy milk or defatted soy milk obtained by water extraction of these, and low-denatures that collect an isoelectric point precipitation using acid. An example is isolated soybean protein. Whether or not these proteins are denatured by heating or the like can be determined by DSC (Differential Scanning Calorimetry) analysis of the proteins (Nagano et al., J. Agric. Food Chem., 40, 941-944). (1992)). According to this analysis method, for example, in the case of undenatured isolated soybean protein, endothermic peaks derived from the 7S component and 11S component, which are the main constituent components, are observed, but excessively denatured. In the case of isolated soy protein, the endothermic peak of the constituent component is not recognized, and therefore the presence or absence of modification can be easily determined.
Among the soy proteins, the case where isolated soy protein is used as a substrate is particularly preferable in terms of functions of flavor, emulsifiability and foamability of the finally obtained polypeptide. That is, low-denatured defatted soybeans (NSI 60 or more, preferably NSI 80 or more) are added 7 to 15 times in the range of pH 6 to 9, preferably pH 6.5 to 8.0, and 60 ° C. or less, preferably 50 ° C. or less. It is preferable that the defatted soymilk extracted with the above method and subjected to removal of the okara component is subjected to isoelectric point precipitation to recover the precipitate fraction. In addition, these defatted soybeans, defatted soymilk, and separated soybean protein are preferably those obtained by decomposing or removing phytic acid, which is undesirable for emulsifiability and foamability, during the preparation process.
[0014]
In the case where the 11S component is selectively hydrolyzed by the first decomposition reaction, the above-mentioned soybean protein is used as a substrate, and the protein hydrolase is added to the substrate solid content in a solution of 1 to 30% protein concentration to 0.001. -1%, preferably 0.01-0.5%, and added at 45 ° C or lower, preferably 30-40 ° C, pH 3.0 or lower, preferably pH 1.8-2.5, reaction time 4 The reaction should be carried out within a short period of time, preferably 10 minutes to 2 hours, until the 0.22 M TCA solubility is 10 to 50%. When the reaction temperature exceeds 45 ° C., the 7S component is easily decomposed in addition to the 11S component, making it difficult to selectively decompose the 11S component, and the decomposed product of the 11S component itself also has a lower molecular weight. Foam properties are reduced. In addition, even if the reaction time is too long, the decomposition product of the 11S component has a lower molecular weight, which is not preferable because the physical properties and flavor are lowered as described above.
[0015]
The protein hydrolase used here is generally any protein hydrolase that exhibits an activity at pH of 3.0 or lower, such as animal-derived pepsin, cathepsin, and a series of microorganism-derived aspartic proteases such as “Neurase F”. Commercially available enzyme agents such as “Protease M” (manufactured by Amano Pharmaceutical Co., Ltd.) and “Sumiteam LP” (manufactured by Shin Nippon Chemical Co., Ltd.) can be used. Of these, pepsin is preferred.
[0016]
In order to selectively hydrolyze the 7S component by the first decomposition reaction, the above-mentioned soybean protein is used as a substrate, and a protein hydrolase is applied to a substrate solid content in a solution having a protein concentration of 0.5% to 20%. It is added in the range of 0.001 to 0.5%, preferably 0.01 to 0.5%, and has a pH higher than pH 3.0 at a reaction temperature of 50 ° C. or higher, preferably 55 to 85 ° C., preferably pH 3.5. It can be carried out by reacting at a reaction time of ˜8.0 for a short time within 2 hours, preferably about 10 to 30 minutes, until the 0.22 M TCA solubility is 10 to 50%. Although the reaction is possible in the vicinity of the isoelectric point of soybean protein at pH 4 to 5, since the dispersibility of the substrate is remarkably lowered and the enzyme reaction rate is deteriorated, it is not a good idea to react in this pH range.
[0017]
The proteolytic enzyme used here needs to be an enzyme agent having a proteolytic activity at more than 50 ° C. and less than 90 ° C., particularly 55 to 85 ° C. The origin of these is not particularly limited, such as commercially available enzyme preparations of plant or animal organs or microorganisms.
[0018]
When the hydrolyzed fraction and the undegraded fraction are separated after the first decomposition reaction, the pH fractionation is convenient and suitable, and when recovering the selective hydrolyzate of the 11S component, the pH is 3-5. In the case of recovering the selective hydrolyzate of the 7S component, preferably in the range of pH 3.5 to 4.5, the pH is adjusted to 3 to 6, preferably in the range of pH 3.5 to 5.5. The supernatant fraction mainly composed of the decomposed product is collected, and the precipitate fraction mainly composed of the undegraded fraction is collected by centrifugation, filter press separation or the like.
[0019]
The undecomposed fraction of the first decomposition reaction is subjected to the second decomposition reaction. When the undecomposed fraction is a precipitate fraction as described above, it is hydrated and the second decomposition reaction is performed under conditions different from the first decomposition reaction. For example, after the first decomposition reaction of the 11S component, the fraction rich in the 7S component is subjected to the second decomposition reaction at a reaction temperature higher than 45 ° C. or a pH higher than pH 3. In particular, the second decomposition reaction is preferred at a pH of 3 or less and a temperature of 50 ° C. or more. After the first decomposition reaction of the 7S component, the fraction rich in the 11S component is subjected to the second decomposition reaction. In this case, it is particularly preferable to carry out at a pH of 3.0 or less and a reaction temperature of 45 ° C. or less. When the 7S component is subjected to the first decomposition reaction and the fraction rich in the 11S component is subjected to the second decomposition reaction, the reaction performed at the pH of 3.0 or less and the reaction temperature of 45 ° C. or less can be selectively performed. The separation operation after the first decomposition reaction is not always necessary, and the first decomposition reaction liquid can be transferred to the second decomposition reaction as it is. The proteolytic enzyme used in the second degradation reaction may be any enzyme that has activity at the reaction pH, and examples include the enzymes described above. The reaction time is a short time within 2 hours, preferably about 10 to 30 minutes, and decomposes to about 10 to 50% with a 0.22 M TCA solubility.
[0020]
In this way, 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 of the decomposition products are purified to an arbitrary ratio, for example, 9: 1 to Mixing 1: 9 to prepare a polypeptide derived from the soy protein of the present invention. Moreover, a polypeptide having good properties can be obtained in a high yield by including both degradation products. This polypeptide should be adjusted to any pH, and if necessary, fats and oils, emulsifiers, saccharides and other proteins should be mixed before or after sterilization and left as it is or concentrated to be in liquid form or dried into a powdered product. Can do. In addition, low-solubility protein contained in the mixture and phytic acid, which is a trace component derived from soybean, tend to adversely affect emulsifying power (especially in the acidic range) and foaming power (particularly foaming stability). By removing these components, emulsifying power and foaming power can be further improved. Furthermore, even if these trace components are removed, a solid recovery rate of 70% or more can be secured.
For removal of these components, the polypeptide solution is used as it is, preferably an alkaline earth metal hydroxide or salt such as Ca hydroxide, Ca chloride, Ca carbonate, Ca lactate, Ca sulfate, Ca glycerophosphate, Ca citrate. In addition, 1 or 6% of Ca salt of gluconate Ca or Ca phosphate or 2 or more kinds of Ca salt is added to the solid content of the mixed solution, and the pH is 2 to 4 or 5 to 9, preferably pH 5. It can adjust to 5-7.5 and can remove the insoluble matter which arises. Furthermore, the mixed solution is subjected to an enzymatic reaction with phytase (an enzyme having phytic acid decomposing activity in a broad sense) to obtain a mixed solution obtained by hydrolyzing phytic acid. Further, the pH of the mixed solution after decomposition by phytase is adjusted to 2 to 4 or 5 to 9, preferably pH 5.5 to 7.5, and a phytase-treated mixed supernatant fraction from which the insoluble matter produced is removed is obtained. These methods can further increase the emulsifying power and foaming power of the polypeptide.
The above shows the characteristic properties of the polypeptide used in the emulsifier composition of the present invention.
[0021]
Examples of the water-soluble polysaccharide used in the emulsifier composition of the present invention include water-soluble soybean polysaccharide and pectin. Water-soluble soybean polysaccharide (hereinafter abbreviated as SSPS) is a water-soluble polysaccharide composed of rhamnose, fucose, arabinose, xylose, galactose, glucose and uronic acid, and standard pullulan (manufactured by Showa Denko KK) as a standard substance. The average molecular weight determined by the intrinsic viscosity method is 1,000,000 or less. This is produced from an extract koji from soybean protein extracted from soybeans. Pectin can be extracted from citrus fruit peel (hereinafter abbreviated as C pectin), and potato-derived pectin can be produced from an extract from starch extracted from potato (hereinafter abbreviated as P pectin). .
[0022]
The emulsifier composition of the present invention contains the polypeptide and the water-soluble polysaccharide, and the weight ratio of the water-soluble polysaccharide to the total weight of the polypeptide and the water-soluble polysaccharide is 0.1 to 0.9, preferably 0.8. It is desirable that it is 2-0.8. When this weight ratio is less than 0.1, the emulsifying power in acidity is insufficient, and when the weight ratio exceeds 0.9, the emulsifying power of not only the acidic range but also weakly acidic to neutral range is extremely high. It becomes worse and the emulsion stability is also poor. In particular, when emulsifying power in the vicinity of pH 3 to 6 is required, it is more preferable that the weight ratio is 0.3 to 0.7 because it exhibits good emulsifying power. The emulsifier composition of the present invention optionally contains other proteins, carbohydrates, fats and oils in addition to the main components of the polypeptide and the water-soluble polysaccharide.
[0023]
Using the emulsifier composition of the present invention, 0.05 wt% to 10 wt%, preferably 0.1 wt% to 5 wt% per oil-in-water emulsion is preferable. An oil-in-water emulsion can be produced. If it is less than 0.05% by weight per emulsion, the emulsification becomes unstable, which is not preferable, and it is not economically preferable to use more than 10% by weight. Specific examples of the acidic oil-in-water emulsion of the present invention include mayonnaise, sour cream, cream with fruit juice, etc., and the product has a pH of 3 to 6, particularly 3.5 to 5.5. It is effective, and the effect is exhibited even when the oil content is 5 to 80%, particularly 20 to 80%. When manufacturing such acidic oil-in-water emulsions, oils, proteins, carbohydrates, flavors, pH adjusters to be blended in addition to the machine used for preparing the emulsion, manufacturing conditions, and the emulsifier composition of the present invention Etc. are not particularly limited, and known substances can be used.
[0024]
【Example】
Hereinafter, the embodiments of the present invention will be specifically described by way of examples. However, the technical scope of the present invention is not limited by these examples.
Production Example 1 (T-1)
Ten times the amount of hot water at 40 ° C. was added to low-denatured defatted soybean flakes (NSI 90) manufactured by Fuji Oil Co., Ltd., and a NaOH solution was added thereto to adjust the pH to 7.0. This was gently stirred and extracted for 1 hour, and then separated into okara of an insoluble fraction and defatted soy milk of a soluble fraction by a centrifuge.
Hydrochloric acid was added to the obtained defatted soymilk to adjust the pH to 4.5, and the resulting protein precipitate was collected by a centrifuge to obtain a separated soybean protein curd. Next, water is added to the separated soy protein curd and hydrochloric acid is added to adjust the pH to 2.0 and the separated soy protein is 10% by weight. 200 mg of pepsin (manufactured by Nippon Biocon) is added to 1 L of this solution and hydrolyzed at 37 ° C. 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 mobility band corresponding to 11S disappeared, and the degradation product component derived from the 11S component and the decomposition were received. A mobility band corresponding to no 7S component was observed. The reaction solution was adjusted to pH 4.5 using NaOH solution, and the resulting precipitate was centrifuged with a supernatant fraction containing 11S component degradation product and a precipitate fraction rich in 7S component (undecomposed fraction). Fractions). In addition, the 0.22 M TCA solubility of the reaction solution of the first reaction is 25%, and the final 0.22 M TCA solubility of the supernatant fraction after pH fractionation is 72%, that after the pH fractionation. The volume recovery of the clear fraction was 80%, and the solid recovery of the supernatant fraction after pH fractionation was 24%. Precipitate fraction rich in 7S component (undegraded fraction) is prepared by adding hydrochloric acid and adding hydrochloric acid to adjust the pH to 2.0 and solid content of 7% by weight. To 1 L of this solution, 100 mg of pepsin (manufactured by Nippon Biocon) is added. In addition, hydrolysis was performed again at 60 ° C. for 20 minutes (second reaction). The final 0.22 M TCA solubility of the reaction solution after pepsin decomposition was 46%. The reaction solution of the second reaction was mixed with the supernatant fraction of the first reaction, adjusted to pH 6.5 using NaOH solution, and spray-dried to prepare polypeptide (T-1). As a result of SDS electrophoretic analysis, 90% or more of the composition of the obtained polypeptide was included 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, the peak area in the molecular weight range of 5,000 to 30,000 was 94%, and the molecular weight less than 5,000 was 1%. . The general analysis values were 84% crude protein, 11% ash, and 5% moisture, and the 0.22M TCA solubility was 52%.
[0025]
Production Example 2 (T-2)
Using the mixed solution of the supernatant fraction of the first reaction and the reaction mixture of the second reaction in Production Example 1, 3% by weight of Ca hydroxide was added to the solid content, and pH was adjusted to 6 using NaOH solution. 5 was heated at 140 ° C. for 7 seconds and then cooled to room temperature, and insoluble components were removed by centrifugation at 5000 G for 10 minutes to obtain a mixed supernatant fraction. This was spray-dried to prepare a polypeptide (T-2). 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 SDS electrophoresis analysis. As a result of gel filtration analysis, the main peak molecular weight is about 8,000, the peak area in the molecular weight range of 5,000 to 30,000 is 89%, and the molecular weight less than 5,000 is 10% or less. It was. The general analysis values were 76% crude protein, 15% ash, and 5% moisture, and the 0.22M TCA solubility was 70%.
[0026]
Test Example Polypeptides (T-1 and T-2) prepared above, soybean peptide (trade name High Nut D3, average peptide chain length 5, 0.22 M TCA solubility 98%, manufactured by Fuji Oil Co., Ltd. ), Water-soluble soybean polysaccharide (SSPS; trade name Soya Five DA-100, manufactured by Fuji Oil Co., Ltd.), C pectin (trade name; SM-478, manufactured by Saneigen FFI Co., Ltd.). Table 1 shows the results of measuring the emulsification activity (by the method in the text) at various pHs using various mixing ratios (water-soluble polysaccharide / (polypeptide + water-soluble polysaccharide)) of 1 wt% solution. .
[0027]

As shown in Table 1, it can be seen that the emulsifying activity of pH 4 is significantly increased synergistically by mixing the polypeptide and SSPS or C-pectin. Moreover, it turns out that there is no effect in a low molecular weight peptide.
[0028]
Example 1
50 parts by weight of the polypeptide (T-1) prepared in Production Example 1 and 50 parts by weight of SSPS were uniformly mixed to prepare an emulsifier composition (hereinafter referred to as M-1). Of the ingredients in the recipe, other than salad oil was stirred and mixed with a Kenwood mixer (“Pro KM-230” manufactured by Aikosha Seisakusho Co., Ltd.), and then emulsified while adding salad oil. Then, the emulsion was homogenized with a colloid mill (manufactured by Flyma) to prepare a mayonnaise-like emulsion.

An average emulsion particle size of a mayonnaise-like emulsion (pH 4.2) prepared only with polypeptide (T-1) as a comparison with M-1 and a frozen state at −30 ° C. for one day, and then a thawed state was observed. The results are shown below.

M-1 had a better emulsion than T-1, and could prepare a mayonnaise-like emulsion that was stable against freezing.
[0029]
Example 2
50 parts by weight of the polypeptide (T-2) prepared in Production Example 2 and 50 parts by weight of P-pectin were uniformly mixed to prepare an emulsifier composition (hereinafter referred to as M-2). For P-pectin, dry potato is dispersed in water to a concentration of 5%, pH is adjusted to 4.5 with hydrochloric acid, heated at 120 ° C. for 30 minutes to obtain an extract, which is freeze-dried. Manufactured. Components of the following composition were mixed, and an emulsion for coffee cream was prepared using an ultrasonic emulsifier at 60 ° C. For comparison, an emulsion for coffee cream using only the polypeptide (T-2) was also prepared.

30 g of commercial instant coffee (manufactured by Nestlé) and 50 g of sugar were dissolved in 1 L of hot water and kept at 80-85 ° C. To 100 ml of this coffee liquid (pH 5), 10 ml of the above emulsion for coffee cream was added and the state was observed.

M-2 could prepare a better emulsion for coffee cream than T-2.
[0030]
【The invention's effect】
It has become possible to provide an emulsifier composition that can be used in various fields such as foods, cosmetics, toiletries, pharmaceuticals, and industrial applications, and particularly suitable for the production of acidic oil-in-water emulsions.

Claims (7)

An emulsifier composition containing a water-soluble polysaccharide and a polypeptide having the following properties.
1) Mainly a polypeptide having a molecular weight in the range of 5,000 to 35,000 as analyzed by SDS polyacrylamide gel electrophoresis containing mercaptoethanol.
2) The main peak molecular weight by gel filtration is about 8,000, the molecular weight range 5,000 to 30,000 is 70% or more of the total peak area, and the molecular weight less than 5,000 is 20% of the total peak area. It is as follows.
3) It is 30-90% by 0.22M TCA solubility rate. The emulsifier composition according to claim 1, wherein the polypeptide is a polypeptide obtained by separately hydrolyzing the 7S component and the 11S component in soybean protein. The emulsifier composition according to claim 1, wherein the weight ratio of the water-soluble polysaccharide to the total weight of the polypeptide and the water-soluble polysaccharide is 0.1 to 0.9. The emulsifier composition according to claim 1, wherein the water-soluble polysaccharide in the emulsifier composition is derived from soybean, citrus fruit or potato. An oil-in-water emulsion obtained by using 0.01 to 10% by weight of the emulsifier composition according to claim 1. The acidic oil-in-water emulsion according to claim 5, which has a pH of 3 to 6. The acidic oil-in-water emulsion according to claim 6, having an oil content of 5 to 80%.