Protein composition with foaming performance as well as preparation method and application thereof

Abstract

The invention relates to the field of foaming, and discloses a protein composition with foaming performance and a preparation method and application thereof. The method comprises the following steps: hydrolyzing gelatin, and mixing the hydrolyzed product with collagen peptide. The prepared protein composition solution has good emulsibility, emulsion stability, foamability and foam stability, the viscosity of the foam surface is properly increased, a firm framework can be given to a whipped foam system, the foam is not prone to breakage, and the stability of the foam is improved. Bubbles filled into the system are easily broken into smaller bubbles under the whipping action and can be stably kept, and the whipped foam is white and fine at the moment and forms cream-shaped foam, and the foam cannot be solidified.

Description

Technical Field

[0001] The invention relates to the field of foaming, and in particular to a protein composition with foaming performance and a preparation method and application thereof. Background Art

[0002] Generally speaking, natural macromolecular protein substances contain specific hydrophilic and lipophilic groups (such as amino, carboxyl, R groups), and have certain functional properties, such as emulsification and foaming properties, but their functional properties (foaming properties and foam stability) are poor and cannot meet the requirements of many food processes. This is mainly because the molecular weight of natural proteins is too large, often more than 200,000, and the molecular chain is long and complex. Therefore, it is necessary to degrade macromolecular proteins into hydrolyzed collagen with small molecular weight through hydrolysis treatment, and improve the foaming properties and foaming stability of proteins by reducing the molecular weight. The traditional degradation method is acid or alkaline hydrolysis. The advantages of this method are fast hydrolysis speed and low cost, but the process is not easy to control, and the neutralization product has high salt content and general product quality. In recent years, there have been many studies and applications on the method of degrading macromolecular proteins into small molecular polypeptides using enzymatic hydrolysis, all of which are to completely hydrolyze macromolecular proteins into collagen peptides with low molecular weight (usually less than 10,000 Da) to achieve their application in the fields of medicine and food. Protein peptides have a low molecular weight, which is beneficial for human absorption and utilization. However, if the large molecular protein is completely hydrolyzed into collagen peptides, the interaction between the hydrophobic group and the solution surface is small, and the molecules are not easy to form an adsorption film on the surface of the aqueous solution, which is not conducive to the formation of foam. In addition, the surface tension of the completely hydrolyzed gelatin solution is high, and the force on the foam surface is large. The pressure difference between the inside and outside of the formed foam is large, which makes the foam easy to break, which is not conducive to the stable existence of the foam, resulting in poor foaming and foaming stability of the product. This limits its application in foods that utilize the foaming properties of protein, such as cakes, marshmallows, soufflés, beer foam, bread, etc.

[0003] CN114907470A discloses that the animal skin is first subjected to dehairing and degreasing pretreatment, and then ultrasonically enzymatically hydrolyzed for 2-3 hours using a composite enzyme (pepsin and subtilisin) under acidic conditions, centrifuged, and the supernatant is taken and freeze-dried to obtain collagen. The raw material used in this patent is animal skin, and the skin material needs to be treated first. The enzymatic hydrolysis uses a composite enzyme and needs to be coordinated with ultrasonic treatment, which is a complex process. The molecular weight of the obtained product is 3300Da. The functional properties of collagen products with this molecular weight, such as emulsification and foaming properties, are poor, which limits its application in the fields of food and medicine. Summary of the invention

[0004] The purpose of the present invention is to overcome the problems existing in the prior art and provide a protein composition with foaming performance and a preparation method and application thereof.

[0005] In order to achieve the above object, the first aspect of the present invention provides a method for preparing a protein composition with foaming properties, the method comprising: hydrolyzing gelatin and mixing the hydrolyzate with collagen peptides.

[0006] The second aspect of the present invention provides a protein composition with foaming properties prepared by the above method.

[0007] The third aspect of the present invention provides the use of the above protein composition in the preparation of foamed food.

[0008] The present invention has the following beneficial effects:

[0009] (1) When the concentration of the protein composition solution prepared by the present invention reaches 20%, the solution of the composition is in a semi-fluid state, and can be applied to foamed food to not only play a thickening role, but also have good emulsification properties and foam stability. Conventional gelatin solutions are in a solidified state when the concentration reaches 20%, and collagen solutions are in a liquid state when the concentration reaches 20%, both of which are not conducive to application.

[0010] (2) The emulsification, emulsion stability, foaming and foam stability of the protein composition solution prepared by the present invention are much better than those of ordinary bone gelatin, cod skin gelatin and collagen peptide, and can be applied to foaming foods such as cream, cake and ice cream. While improving the product quality, it can also give the product a mellow taste and the product system is less likely to be stratified (better emulsification and emulsion stability), with a larger foam whipping volume and less likely to dissipate (foaming and foam stability), and meet people's nutritional needs for high protein.

[0011] (3) The viscosity of the protein composition solution prepared by the present invention is higher than that of collagen peptide, but lower than that of bone gelatin and cod skin gelatin. Properly increasing the viscosity of the foam surface can give the foam system a strong skeleton after whipping, making the foam not easy to break. The bubbles filled into the system are easily broken into smaller bubbles under the action of whipping and can be stably maintained. At this time, the whipped foam is whiter and more delicate, forming a creamy foam. More preferably, within the weight average molecular weight range of the present invention, the foam will not solidify. DETAILED DESCRIPTION

[0012] The endpoints and any values ​​of the ranges disclosed in this article are not limited to the precise ranges or values, and these ranges or values ​​should be understood to include values ​​close to these ranges or values. For numerical ranges, the endpoint values ​​of each range, the endpoint values ​​of each range and the individual point values, and the individual point values ​​can be combined with each other to obtain one or more new numerical ranges, which should be considered as specifically disclosed in this article.

[0013] The first aspect of the present invention provides a method for preparing a protein composition with foaming properties, the method comprising: hydrolyzing gelatin, and mixing the hydrolyzed product with collagen peptides.

[0014] In the present invention, in order to make the composition have better emulsification, emulsification stability, foaming, foam stability and viscosity, the weight ratio of gelatin to collagen peptide is 1:1.5-3, which can be 1:1.5, 1:1.6, 1:1.7, 1:1.8, 1:1.9, 1:2, 1:2.1, 1:2.2, 1:2.3, 1:2.4, 1:2.5, 1:2.6, 1:2.7, 1:2.8, 1:2.9, 1:3 or the range formed by the above two values ​​and the value within the range.

[0015] In the present invention, in order to make the composition have better emulsification, emulsification stability, foaming, foam stability and viscosity, the gel strength of the gelatin is 100-150g. Preferably, the weight average molecular weight of the gelatin is 110-180kDa, which can be 110kDa, 120kDa, 130kDa, 140kDa, 150kDa, 160kDa, 170kDa, 180kDa or the range formed by the above two values ​​and the value within the range.

[0016] In the present invention, in order to make the composition have better emulsification, emulsification stability, foaming, foam stability and viscosity, the weight average molecular weight of the collagen peptide is 3000-7000Da, which can be 3000Da, 4000Da, 5000Da, 6000Da, 7000Da or the range formed by two of the above values ​​and the value within the range. Preferably, the collagen peptide is derived from at least one of animal skin, tendons, tendons and bones, preferably bones.

[0017] In the present invention, in order to make the composition have better emulsification, emulsification stability, foaming, foam stability and viscosity, the mixing temperature is 30-60°C, and can be 30°C, 40°C, 50°C, 60°C or a range formed by two of the above values ​​and a value within the range. There is no limit to the mixing time, as long as the mixing is uniform.

[0018] In the present invention, the source of the gelatin is not limited, as long as it can be successfully hydrolyzed to a certain weight average molecular weight. Preferably, the gelatin is derived from at least one of animal skin, tendons, tendons and bones, more preferably bones. Further preferably, the hydrolysis conditions make the weight average molecular weight of the hydrolyzed product 25000-45000Da, which can be 25000Da, 30000Da, 35000Da, 40000Da, 45000Da or the range formed by the above two values ​​and the value within the range.

[0019] In the present invention, there is no limitation on the hydrolysis method of gelatin, and it can be hydrolyzed into a certain weight average molecular weight. Preferably, the hydrolysis method includes: contacting gelatin with protease in the presence of water.

[0020] In the present invention, in order to make the composition have better emulsification, emulsification stability, foaming, foam stability and viscosity, the weight ratio of water to gelatin is 100:20-35, which can be 100:20, 100:23, 100:25, 100:27, 100:30, 100:32, 100:35 or the range formed by the above two values ​​and the value within the range.

[0021] In the present invention, in order to make the composition have better emulsification, emulsification stability, foaming, foam stability and viscosity, relative to 100g of the gelatin, the enzymatic activity of the protease is 55-180U, which can be 55U, 60U, 70U, 80U, 90U, 100U, 110U, 120U, 130U, 140U, 150U, 160U, 170U, 180U or the range formed by two of the above values ​​and the value within the range.

[0022] In the present invention, the enzyme activity of the neutral protease is defined as the amount of enzyme required to release 1 ug of tyrosine within 1 minute at a temperature of 40° C. and a pH of 7.

[0023] In the present invention, in order to allow gelatin to be hydrolyzed smoothly, the contact conditions include: a temperature of 50-55°C, which can be 50°C, 51°C, 52°C, 53°C, 54°C, 55°C or a range formed by two of the above values ​​and a value within the range; a time of 1-3h, which can be 1h, 1.5h, 2h, 2.5h, 3h or a range formed by two of the above values ​​and a value within the range.

[0024] In the present invention, in order to make the mixed composition of hydrolyzed gelatin and collagen peptide have better emulsification, emulsification stability, foaming property, foam stability and viscosity, the protease is a neutral protease.

[0025] In the present invention, in order to prevent the gelatin from being over-hydrolyzed, the hydrolysis method further comprises: inactivating the enzyme in the contact product.

[0026] In the present invention, the method of inactivating the enzyme is not limited, and the protease can be successfully inactivated, preferably by high-temperature inactivation. Preferably, the conditions for inactivating the enzyme include: a temperature of more than 90° C. and a time of 15-20 min.

[0027] Preferably, the method further comprises: drying the mixed product; preferably, the drying method is spray drying; preferably, the drying conditions include: a temperature of 100-230°C, when spray drying is actually used, an inlet air temperature of 150-200°C, and an outlet air temperature of 80-100°C.

[0028] The second aspect of the present invention provides a protein composition with foaming properties prepared by the above method.

[0029] Preferably, the weight average molecular weight of the composition is 15000-20000 Da, and may be 15000 Da, 16000 Da, 17000 Da, 18000 Da, 19000 Da, 20000 Da or a range formed by two of the above values, or a value within the range.

[0030] The third aspect of the present invention provides the use of the above protein composition in preparing a foaming food. The foaming food comprises at least one of cream, cake, ice cream, marshmallow, soufflé, beer and bread.

[0031] The present invention will be described in detail by way of examples. In the following examples, the bone gelatin is from Baotou Dongbao Biotechnology Co., Ltd., with a gel strength of 120 g and a weight average molecular weight of 157 kDa.

[0032] Source of cod skin gelatin: The material ratio of cod skin to water is 1:10, add 0.4% sodium hydroxide to a concentration of 0.4% by weight, soak for two hours, pour out the alkali solution, wash with tap water until the pH is less than 10, drain the water, add pure water, the material-liquid ratio is 1:4, and then add phosphoric acid to a concentration of 0.075% by weight. Stir evenly and let it stand for two hours, extract the gelatin at 52±2℃, filter out the gelatin when the concentration of the gelatin remains unchanged, cool and form, squeeze the gelatin, dry and crush it to obtain cod skin gelatin.

[0033] Source of collagen peptide: Baotou Dongbao Biotechnology Co., Ltd.

[0034] Source of neutral protease: Nanning Dongheng Huadao Biotechnology Co., Ltd., enzyme activity 130,000 U / g.

[0035] Weight average molecular weight determination:

[0036] Instrument name: Shimadzu GPC gel permeation chromatograph

[0037] Column model: Tskgel G4000SWXL

[0038] Mobile phase: 80.7775 g of sodium dihydrogen phosphate, 35.2 g of potassium dihydrogen phosphate, and 4 g of sodium azide, dissolved in 500 ml of ultrapure water, take 50 ml and dilute to 2000 ml as the mobile phase.

[0039] Experimental conditions: column temperature 30°C, detector temperature 30°C, flow rate 0.5ml / min, wavelength 210nm, injection volume 10ul.

[0040] Sample preparation: Take 0.125g of sample into a 25ml volumetric flask, make up to volume with ultrapure water, filter with a 0.2-0.5um filter membrane, and use the filtrate for determination.

[0041] Preparation of standard solution: A series of monodisperse sodium polystyrene sulfonate salts were used as molecular weight standards, with molecular weights of 1400Da, 4300Da, 6800Da, 17000Da, 32000Da, and 77000Da, respectively. A series of standard solutions with a concentration of 1g / L were prepared with mobile phase, and passed through a filter membrane with a pore size of 0.2-0.5um. After filtration, the samples were injected respectively to obtain a series of standard chromatograms. The logarithm of the relative molecular mass was plotted against the retention time to obtain the relative molecular mass calibration curve and its equation.

[0042] Viscosity determination: refer to QB 2354-2005 "Pharmaceutical Gelatin" 5.4 Boehm viscosity for determination. If the viscosity value is low, the foam system skeleton is not firm, making the foam easy to break. If the viscosity is high, there is a sticky feeling and the taste is poor. Better results will be achieved within the range of 0.5-0.8mPa.S.

[0043] Determination of foaming performance and foaming stability:

[0044] (1) The semi-hydrolyzed gelatin-collagen composition was prepared into a 200 mL solution with a concentration of 1%, and the initial height h0 of the liquid level was recorded.

[0045] (2) Immerse the dissolved solution under the emulsification head of the high shear emulsifier, set the speed to 10000 rpm, and time for 2 minutes. Immediately after the end, record the bubble height h1. After the bubble measurement is completed, time for 10 minutes and record the height h1 after 10 minutes. 10 .

[0046] (3) Foamability FC (%) = (foam height h1-initial height h0) / initial height h0×100% Foam stability FS (%) = (height h1 after 10 minutes) 10 -initial height h0) / (bubble height h1-initial height h0).

[0047] Determination of emulsification and emulsion stability:

[0048] Prepare a 0.1% (g / L) solution of the composition, take 300 ml of the dispersed sample and mix it with 75 ml of salad oil, then disperse it with an emulsifying disperser at 10000 rpm for 2 min, take out 50 ul from the bottom and dilute it with 10 ml of 0.1 wt% SDS, measure the absorbance A0 at 500 nm with a spectrophotometer (with 0.1 wt% SDS as a blank), let it stand for 30 min, and then perform a colorimetric A1 again, record the data twice, and all experiments were carried out at room temperature.

[0049] Emulsification EAI = 2 × 2.303 × A0 × N / (0.2 × C × 10000)

[0050] N is the dilution factor

[0051] C is the concentration of semi-hydrolyzed gelatin-collagen complex solution (g / ml)

[0052] Emulsion stability ESI = A0 × △t / △A

[0053] △A=A0-A1△t=30min.

[0054] The higher the emulsification property, the better the product uniformity and the better the taste; the higher the emulsification stability, the less likely the product system is to stratify; the better the foaming property, the larger the volume of the foam; the higher the foaming stability, the less likely the foam will dissipate after whipping.

[0055] Example 1

[0056] (1) Take 100 g of bone gelatin particles, add 75°C hot pure water, and stir to prepare gelatin into a gelatin solution with a concentration of 21% by weight.

[0057] (2) 82.5 U of neutral protease was added to 100 g of bone gelatin, and the mixture was stirred at 53° C. for 1 h.

[0058] (3) Inactivate the enzyme at above 90°C for 15 min to obtain semi-hydrolyzed gelatin solution (weight average molecular weight: 43,000 Da).

[0059] (4) When the semi-hydrolyzed gelatin solution is cooled to 45°C, 280 g of bone collagen peptide with a weight average molecular weight of 6000 Da is added and the mixture is fully dissolved and mixed.

[0060] (5) The composite solution was spray dried at an air inlet temperature of 180°C and an air outlet temperature of 85°C to obtain a semi-hydrolyzed gelatin-collagen composite. The emulsification, foaming and viscosity of the product were tested, and the results are shown in Table 1.

[0061] Example 2

[0062] (1) Take 100 g of bone gelatin particles, add 70°C hot pure water, and stir to prepare gelatin into a gelatin solution with a concentration of 28%.

[0063] (2) 137 U of neutral protease was added to 100 g of bone gelatin, and the mixture was stirred at 53° C. for 2 h.

[0064] (3) Inactivate the enzyme at above 90°C for 15 min to obtain semi-hydrolyzed gelatin solution (weight average molecular weight: 37,000 Da).

[0065] (4) When the semi-hydrolyzed gelatin solution is cooled to 45°C, 180 g of bone collagen peptide powder with a weight average molecular weight of 6000 Da is added and the mixture is fully dissolved and mixed.

[0066] (5) The composite solution was spray-dried at an air inlet temperature of 170°C and an air outlet temperature of 90°C to obtain a semi-hydrolyzed gelatin-collagen composite. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0067] Example 3

[0068] (1) Take 100 g of bone gelatin particles, add 73°C hot pure water, and stir to prepare gelatin into a gelatin solution with a concentration of 30%.

[0069] (2) Add 165 U of neutral protease to 100 g of bone gelatin and stir at 53°C for 1.5 h.

[0070] (3) Inactivate the enzyme at above 90°C for 15 min to obtain semi-hydrolyzed gelatin solution (weight average molecular weight: 33,000 Da).

[0071] (4) When the semi-hydrolyzed gelatin solution is cooled to 45°C, 160 g of bone collagen peptide powder with a weight average molecular weight of 6000 Da is added and the mixture is fully dissolved and mixed.

[0072] (5) The composite solution was spray dried at an air inlet temperature of 185°C and an air outlet temperature of 85°C to obtain a semi-hydrolyzed gelatin-collagen composite. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0073] Example 4

[0074] The method of Example 1 was followed, except that the amount of neutral protease used was 200 U, and the weight average molecular weight of the semi-hydrolyzed gelatin solution was 20,000 Da. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0075] Example 5

[0076] The method of Example 1 was followed, except that the amount of neutral protease used was 45 U, and the weight average molecular weight of the semi-hydrolyzed gelatin solution was 57,000 Da. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0077] Example 6

[0078] The method of Example 1 was followed, except that the amount of collagen peptide used was 130 g. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0079] Example 7

[0080] The method of Example 1 was followed, except that the amount of collagen peptide used was 350 g. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0081] Example 8

[0082] The method of Example 1 was followed, except that the weight average molecular weight of the collagen peptide was 8000 Da. The results are shown in Table 1. The results of the emulsification, foaming and viscosity tests are shown in Table 1.

[0083] Example 9

[0084] The method of Example 1 was followed, except that the weight average molecular weight of the collagen peptide was 2000 Da. The results of the emulsification, foaming and viscosity tests are shown in Table 1. The results are shown in Table 1.

[0085] Comparative Example 1

[0086] The method of Example 1 was followed, except that step 4 was not performed, and drying was performed directly after the enzyme was inactivated. The results are shown in Table 1.

[0087] Comparative Example 2

[0088] According to the method of comparative example 1, except that the amount of neutral protease used was 250U, the weight average molecular weight of the obtained hydrolyzate was similar to that of the product obtained in Example 1. The results are shown in Table 1.

[0089] Table 1

[0090]

[0091] It can be seen from the above results that the composition prepared by the method of the present invention has significantly better effects in emulsification, emulsification stability, foaming, foam stability and viscosity.

[0092] The preferred embodiments of the present invention are described in detail above, but the present invention is not limited thereto. Within the technical concept of the present invention, the technical solution of the present invention can be subjected to a variety of simple modifications, including the combination of various technical features in any other suitable manner, and these simple modifications and combinations should also be regarded as the contents disclosed by the present invention and belong to the protection scope of the present invention.

Claims

1. A method for preparing a protein composition having foaming properties, characterized in that: The method comprises: hydrolyzing gelatin and mixing the hydrolyzed product with collagen peptide.

2. The method according to claim 1, wherein: The weight ratio of gelatin to collagen peptide is 1:1.5-3; And / or, according to the standard "GB6783-2013", the gel strength of the gelatin is 100-150g; and / or, the gelatin has a weight average molecular weight of 110-180 kDa; and / or, the weight average molecular weight of the collagen peptide is 3000-7000Da; and / or, the collagen peptide is derived from at least one of animal skin, tendons, tendons and bones, preferably bones; And / or, the mixing temperature is 30-60°C; and / or, the gelatin is derived from at least one of animal skin, tendons, tendons and bones, preferably bones; And / or, the hydrolysis conditions are such that the weight average molecular weight of the hydrolyzed product is 25000-45000 Da.

3. The method according to claim 1 or 2, wherein: The hydrolysis method comprises: contacting gelatin with protease in the presence of water.

4. The method according to claim 3, wherein: The weight ratio of water to gelatin is 100:20-35; and / or, relative to 100 g of the gelatin, the enzyme activity of the protease is 55-180 U; And / or, the contacting conditions include: temperature of 50-55°C and time of 1-3h; And / or, the protease is a neutral protease.

5. The method according to claim 3, wherein: The hydrolysis method also includes: inactivating enzymes in the contact product; Preferably, the enzyme inactivation conditions include: temperature above 90°C and time of 15-20 min.

6. The method according to claim 1 or 2, wherein: The method further comprises: drying the mixed product; Preferably, the drying method is spray drying; Preferably, the drying temperature is 100-230°C.

7. A protein composition with foaming properties prepared by the method according to any one of claims 1 to 6.

8. The protein composition according to claim 7, wherein The weight average molecular weight of the protein composition is 15000-20000 Da.

9. Use of the protein composition according to claim 8 in preparing foamed food.

10. The use according to claim 9, wherein: The foaming food comprises at least one of cream, cake, ice cream, marshmallow, soufflé, beer and bread.

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