High-foamability fish protein glue and preparation method thereof

Abstract

The invention provides high-foamability fish protein glue and a preparation method thereof. The method comprises the following steps: S1, preparing a fish protein glue solution; s2, dissolving Arabic gum in the fish protein glue solution obtained in the step S1; s3, adjusting the pH value of the solution obtained in the step S2, and adding an enzyme for enzymolysis; s4, performing enzyme deactivation on the materials subjected to enzymolysis, and adjusting the pH value again after enzyme deactivation; and S5, freezing the material obtained in the step S4 at low temperature, and freeze-drying to obtain the high-foamability fish protein glue. The preparation process is simple, no pollution is generated in the treatment process, and the fish protein glue has the advantages of being green and environmentally friendly, the foamability of the prepared fish protein glue reaches up to 158.89%, and the foamability stability reaches up to 55.40%.

Description

TECHNICAL FIELD

[0001] The present application relates to the field of functional food technology, in particular to a fish protein gel with high foaming property and a preparation method thereof. BACKGROUND

[0002] The main component of protein gel is high polymer of high molecular polypeptide, contains 20 kinds of essential amino acids for human body, is the product of condensation of various amino acids in a certain proportion, and the main source of protein gel at present is pig, cow and other mammals. However, due to various constraints, the use of mammalian protein gel is limited, so people begin to develop other sources of protein gel to replace mammalian protein gel. At present, the main alternative source is fish protein gel. Foaming property is an important functional property of fish protein gel, which plays a very important role in foods such as ice cream, cake and beer which need foaming property. Foaming property is due to the fact that surfactants can reduce the surface tension of liquid and form a directional molecular adsorption layer at the gas-liquid interface. Protein is an amphiphilic molecule, which can spontaneously migrate to the gas-liquid interface and form a high viscoelastic film on the interface, and the interface system is more stable than the interface formed by low molecular weight surfactants, so it can be used as a good foaming agent. With the increasing demand for food technology function, nutritional function and sensory properties, the application of protein is increasingly unable to meet the needs of modern food development and processing, so the modification technology of food protein becomes an important tool to make protein meet the required quality.

[0003] Therefore, how to improve the foaming capacity of fish protein gel and obtain more stable foaming effect needs to be studied. SUMMARY

[0004] The present application aims to provide a fish protein gel with high foaming property and a preparation method thereof, which obtains fish protein gel with strong foaming capacity and stable foaming effect.

[0005] To achieve the above purpose, the present application provides the following technical solutions: A preparation method of fish protein gel with high foaming property, the method comprising the following steps: S1, preparing a fish protein gel solution; S2, dissolving gum arabic in the fish protein gel solution obtained in step S1; S3, adjusting the pH value of the solution obtained in step S2 and adding enzyme for enzymolysis; S4, inactivating the enzyme of the material after completing the enzymolysis, and adjusting the pH value again after inactivation; S5, freezing the material obtained in step S4 at low temperature, and obtaining the fish protein gel with high foaming property after freeze-drying.

[0006] To achieve the above purpose, the present application also provides the following technical solutions: A high-foaming fish protein glue obtained by the method described above.

[0007] Other suitable fields will become apparent from the description provided in this disclosure.

[0008] The description in the summary and specific examples are only intended to illustrate and are not intended to limit the scope of the present disclosure.

[0009] Compared with the prior art, the technical solution provided by the present application has the following beneficial effects: 1. The present application provides a high-foaming fish protein glue and a preparation method thereof, obtaining a fish protein glue with strong foaming ability and stable foaming effect; 2. The present application improves the foaming property of fish protein glue by combined modification, specifically, fish protein glue is combined with gum arabic, and enzymolysis is carried out by using neutral protease, which changes the structure of fish protein glue, and the foaming property of the obtained fish protein glue is improved to 158.89%, and the foaming stability is improved to 55.40%, which is increased by 62.22% and 11.71% respectively compared with unmodified protein; 3. The present application uses neutral protease to moderately hydrolyze fish protein glue to destroy the spatial conformation of protein, so that the originally dense structure of fish protein glue becomes loose, so that more hydrophobic groups are exposed to the surface of the molecule; in addition, more hydroxyl and amino groups are exposed after enzymolysis, which are further combined with gum arabic glycoprotein branches and free carboxyl groups, so that more hydrogen bonds and stronger electrostatic interaction force are formed between fish protein glue and gum arabic, which are all conducive to improving the foaming property of fish protein glue; 4. The preparation method provided by the present application has simple process and does not produce pollution in the processing process, and has the advantages of green environmental protection. The fish protein glue extracted by the present application is transparent and free of impurities, has good foaming characteristics, and is suitable for industrialized production of fish protein glue-based foaming agent. BRIEF DESCRIPTION OF DRAWINGS

[0010] In order to more clearly illustrate the technical solutions in the embodiments of the present application, the drawings needed in the embodiment description will be briefly introduced. Obviously, the drawings in the following description are only some embodiments of the present application, and other embodiments can be obtained by those skilled in the art without creative labor on the basis of these drawings.

[0011] Figure 1 Effect of combined modification on foaming property and foaming stability of fish protein glue solution; Figure 2 Effect of combined modification on particle size, PDI and potential of fish protein glue; Figure 3The effect of different neutral protease activities on the foaming properties and foam stability of fish protein gel solutions; Figure 4 The effects of different hydrophilic colloids on the foaming properties and foam stability of fish protein gel solutions; Figure 5 The effect of different gum arabic concentrations on the foaming properties and foam stability of fish protein glue solutions was investigated. Detailed Implementation

[0012] The technical solutions in the embodiments of the present invention will be clearly and completely described below. Obviously, the described embodiments are only some embodiments of the present invention, and not all embodiments. Based on the embodiments of the present invention, all other embodiments obtained by those skilled in the art without creative effort are within the scope of protection of the present invention. It should be understood that the specific embodiments described herein are only for illustration and explanation of the present invention and are not intended to limit the present invention.

[0013] Any specific numerical values ​​disclosed herein (including the endpoints of numerical ranges) are not limited to their exact values, but should be understood to also include values ​​close to the exact value, such as all possible values ​​within ±5% of the exact value. Furthermore, with respect to the disclosed numerical ranges, one or more new numerical ranges can be obtained by arbitrarily combining the endpoint values ​​of the range, the endpoint values ​​with specific point values ​​within the range, and the specific point values ​​themselves; these new numerical ranges should also be considered as specifically disclosed herein.

[0014] The terminology used in this disclosure is for the purpose of describing particular exemplary embodiments only and is not intended to be limiting. Unless the context clearly indicates otherwise, the singular forms “a,” “an,” and “the” as used in this disclosure are intended to include the plural forms as well. The terms “comprising,” “including,” “containing,” and “having” are inclusive and thus describe the presence of said features, elements, compositions, steps, integers, operations, and / or components, but do not exclude the presence or inclusion of one or more other features, integers, steps, operations, elements, components, and / or sets thereof. Although the open-ended term “comprising” should be understood as a non-limiting term used to describe and claim the various embodiments described in this disclosure, in some aspects it may instead be understood as a more restrictive and limiting term, such as “consisting of” or “substantially consisting of.” Thus, for any given embodiment describing a composition, material, component, element, feature, integer, operation, and / or process step, this disclosure also particularly includes embodiments consisting of or substantially consisting of such compositions, materials, components, elements, features, integers, operations, and / or process steps. In the case of “consisting of…”, the alternative embodiments exclude any additional compositions, materials, components, elements, features, integers, operations and / or process steps. In the case of “essentially composed of…”, any additional compositions, materials, components, elements, features, integers, operations and / or process steps that substantially affect the essential and novel characteristics are excluded from such embodiments. However, any compositions, materials, components, elements, features, integers, operations and / or process steps that do not substantially affect the essential and novel characteristics may be included in the embodiments.

[0015] Any method steps, processes, and operations described in this disclosure should not be construed as necessarily requiring them to be performed in a particular order as discussed or shown, unless explicitly specified. It should also be understood that additional or alternative steps may be used unless otherwise stated.

[0016] In this application, except where expressly stated, any matters or issues not mentioned are directly applicable to those known in the art without any modification. Furthermore, any implementation described in this disclosure may be freely combined with one or more other implementations described in this disclosure, and the resulting technical solutions or concepts shall be considered part of the original disclosure or original record of this application, and should not be regarded as new content not disclosed or anticipated in this disclosure, unless those skilled in the art consider the combination to be clearly unreasonable.

[0017] Unless otherwise stated, the terms used herein have the same meaning as commonly understood by those skilled in the art, and if a term is defined herein and its definition differs from the common understanding in the art, the definition herein shall prevail.

[0018] Unless otherwise stated, when % is mentioned in this document, it refers to wt%.

[0019] First aspect This invention provides a method for preparing high-foaming fish protein gel, the method comprising the following steps: S1, preparing a fish protein gel solution; S2, dissolving gum arabic in the fish protein gel solution obtained in step S1; S3, adjusting the pH value of the solution obtained in step S2, and adding an enzyme for enzymatic hydrolysis; S4, inactivating the enzyme in the material after enzymatic hydrolysis, and adjusting the pH value again after enzyme inactivation; S5, freezing the material obtained in step S4 at low temperature, and freeze-drying it to obtain the high-foaming fish protein gel.

[0020] This invention employs a combined modification approach to improve the foaming properties of fish gelatin. Specifically, enzymatically hydrolyzed fish gelatin is first combined with gum arabic. Gum arabic enhances the hydrogen bonding and electrostatic forces of the composite modified fish gelatin, thereby improving its foaming performance. Then, a neutral protease is used to enzymatically hydrolyze the fish gelatin, altering its structure, enhancing surface hydrophobicity, and disrupting its microstructure. Based on this, the final fish gelatin exhibits improved foaming properties to 158.89% and improved foaming stability to 55.40%, representing increases of 62.22% and 11.71%, respectively, compared to the unmodified protein.

[0021] Specifically, this invention utilizes neutral protease to moderately hydrolyze fish protein gelatin, thereby disrupting the spatial conformation of the protein and making the originally dense structure of fish protein gelatin more porous, thus exposing more hydrophobic groups to the molecular surface. In addition, enzymatic hydrolysis exposes more hydroxyl and amino groups, which further bind to the branched chains of gum arabic glycoprotein and free carboxyl groups, respectively. This results in more hydrogen bonds and stronger electrostatic interactions between fish protein gelatin and gum arabic, all of which contribute to improving the foaming properties of fish protein gelatin.

[0022] The preparation method provided by this invention is simple in process and does not generate pollution during the process, thus having the advantages of being green and environmentally friendly. The fish protein gel extracted by this invention is transparent and free of impurities and has good foaming properties, making it suitable for the industrial production of fish protein gel-based foaming agents.

[0023] The high foaming fish protein glue provided by this invention can be used as a foaming agent, specifically a foaming agent based on fish protein glue, and has wide applications in industry.

[0024] In some embodiments of the present invention, in step S1, the protein concentration of the fish protein gel solution is 5 wt%.

[0025] In some embodiments of the present invention, in step S1, the fish protein gel in the fish protein gel solution is sourced from tilapia. Tilapia protein gel is widely available and cost-effective, making it suitable as an experimental material.

[0026] In some embodiments of the present invention, in step S2, the mass ratio of gum arabic to the fish protein glue solution is 1:(30~70), preferably 1:50. It should be noted that too little gum arabic will result in insufficient force to form with the fish protein glue to maintain stability, while too much gum arabic will cause the fish protein glue to combine with excessive gum arabic, leading to its own aggregation and the masking of hydrophobic groups.

[0027] In some embodiments of the present invention, in step S2, after dissolving gum arabic in the fish protein gum solution obtained in step S1, it is necessary to let it stand for 10 minutes to allow the fish protein gum to combine with gum arabic and stabilize the solution system.

[0028] In some embodiments of the present invention, in step S3, the pH value of the solution obtained in step S2 is adjusted to the optimal pH range of neutral protease: 6.8~7.2, preferably 7.0.

[0029] In some embodiments of the present invention, in step S3, a neutral protease obtained from Bacillus subtilis is used for enzymatic hydrolysis. The cleavage site of this neutral protease is a hydrophobic amino acid, which helps to improve the foaming properties of fish protein gel.

[0030] In some embodiments of the present invention, in step S3, the amount of enzymatic hydrolysis added is 8-15 U / g, preferably 10 U / g. If the activity of the neutral protease is too low, it cannot fully open the structure of the fish protein gel; if the activity of the neutral protease is too high, it will excessively damage the structure of the fish protein gel.

[0031] In some embodiments of the present invention, the enzymatic hydrolysis time in step S3 is 20-40 minutes, preferably 30 minutes. A hydrolysis time that is too short is not suitable for practical applications, while a hydrolysis time that is too long will lead to over-hydrolysis.

[0032] In some embodiments of the present invention, in step S3, the temperature during enzymatic hydrolysis is 35~42℃, preferably 40℃. 40℃ is the optimal reaction temperature for neutral proteases; if the hydrolysis temperature is different, the enzymatic hydrolysis reaction may be incomplete.

[0033] In some embodiments of the present invention, in step S4, the enzyme is inactivated by a boiling water bath for 10 minutes.

[0034] In some embodiments of the present invention, in step S4, after enzyme inactivation, the pH value is adjusted to 6.8-7.2, preferably 7.0. This ensures that the modified fish protein gel solution system does not have its foaming performance affected by pH changes caused by the enzymatic hydrolysis process.

[0035] In some embodiments of the present invention, in step S5, the freeze-drying temperature is -70~-80℃, preferably -80℃, the freeze-drying time is 24~48h, preferably 48h, and the freeze-drying pressure is 5~7MPa, preferably 5MPa. Fish protein gel is composed of protein, which is easily denatured at high temperatures. To ensure that the obtained sample has a sufficiently high degree of dryness without damaging its original structure, a sufficiently low freeze-drying temperature and pressure, and a sufficiently long freeze-drying time should be selected.

[0036] Second aspect This invention provides a highly foaming fish protein gel, obtained by the method described above.

[0037] Example 1. Materials and Methods Tilapia scales (260-270 Bloom) gelatin were purchased from Suzhou Jiliding Marine Biotechnology Co., Ltd., China; neutral protease (50 U / mg) was supplied by Aladdin Industries, Ltd. (Shanghai, China); sodium carboxymethyl cellulose, sodium alginate, pectin, and gum arabic were supplied by Food Chemicals International Ltd. (Shanghai, China).

[0038] 2. Instruments and Equipment Digital display constant temperature magnetic stirring water bath, Changzhou Huabang Instrument Manufacturing Co., Ltd.; KA-T25 homogenizer, IKA GmbH, Germany.

[0039] 3. Experimental Methods Example 1 Fish protein gel dissolution pretreatment: Dissolve 5.0 g of fish protein gel in 100 mL of ultrapure water and stir for 60 min in a constant temperature magnetic stirring water bath at 40℃ to ensure complete dissolution.

[0040] Example 2 Effects of combined modification with neutral protease and gum arabic on the foaming properties and characteristics of fish protein gelatin solution: The pH of the obtained fish protein gelatin solution was adjusted to 6.8-7.2. 20 mL of the fish protein gelatin solution was taken and neutral protease solution (neutral protease added at a concentration of 10 U / g fish protein gelatin) was added for enzymatic hydrolysis for 30 min. Then, 0.1% gum arabic powder was added and completely dissolved in a 40℃ water bath for 10 min. After the hydrolysis, the enzyme was inactivated for 10 min. After enzyme inactivation, the pH of the hydrolysate was adjusted to 6.8-7.2, and the sample was stored at 4℃. The fish protein gelatin solution was diluted to 1% by adding 4 times the volume of distilled water, and then the foaming properties and foaming stability were determined.

[0041] Determination of foaming ability and foaming stability: 30 mL (V0) of 1% sample was poured into a 100 mL conical flask and homogenized at 13600 rpm for 2 min; then the solution was immediately transferred to a 100 mL graduated cylinder, and the foam volume (V1) was recorded; after standing for 30 min, the foam volume (V2) was recorded; finally, the foaming capacity (FA) and foaming stability (FS) were calculated using the following formula: FA(%)=(V1-V0) / V0×100%(Eq.1); FS(%)=(V2-V0) / (V1-V0)×100%(Eq.2); Where V0 is the initial volume of the protein solution; V1: The total volume of solution and foam after homogenization for 2 minutes; V2: The total volume of solution and foam after standing for 30 minutes.

[0042] Depend on Figure 1 As shown, compared to other samples, the foaming performance of fish protein gel modified with neutral protease and gum arabic was significantly improved, with FA and FS increasing to approximately 158.89% and 55.4%, respectively. The order of addition of neutral protease and gum arabic had no significant effect on the foaming performance of fish protein gel. Compared to pure fish protein gel, more hydroxyl and amino groups were exposed after enzymatic hydrolysis, further binding with the glycoprotein branches and free carboxyl groups of gum arabic, respectively. More hydrogen bonds and electrostatic interactions were formed between fish protein gel and gum arabic, making it easier to form a stable elastic film at the air-water interface, resulting in a more stable foam structure. Therefore, as the stability of the foam structure increased, the foam strength also increased. In summary, the foaming performance of the composite modified fish protein gel was significantly improved; among them, different lowercase letters indicate significant differences in foaming properties and foaming stability (p<0.05).

[0043] Determination of average particle size, polymer dispersibility index (PDI), and zeta potential: The particle size, PDI value, and zeta potential of fish protein gel solutions obtained under different modification conditions were determined using a ZS180 nanoparticle size and zeta potential analyzer. The modified fish protein gel solution was diluted with distilled water to 1 mg / mL and directly injected into a zeta potential culture dish, removing air bubbles. Instrument settings: temperature 25°C, refractive index 1.590, absorption parameter 0.01. Results are as follows: Figure 2 As shown, the particle size of the gum arabic modified fish protein glue is reduced to about 200 nm. The particle size of the composite modified fish protein glue is greatly reduced, the charge is the highest, and the stability and uniformity are better. Figure 2 Different letters in the text indicate significant differences (p<0.05).

[0044] The effects of different proportions of neutral protease activity and gum arabic concentration on the foaming properties and foam stability of fish protein gel solutions.

[0045] Comparative Example 1 Effects of different neutral protease activities on the foaming properties and foam stability of fish protein gel solution: Fish protein gel solution was prepared according to the method in Example 1. The pH of the obtained fish protein gel solution was adjusted to 6.8-7.2. 20 mL of the fish protein gel solution was taken and neutral protease solutions with different activities were added (0, 5, 10, 15, and 20 U / g fish protein gel). Enzymatic hydrolysis was performed for 30 min, followed by enzyme inactivation for 10 min. After enzyme inactivation, the pH of the hydrolysate was adjusted to 6.8-7.2, and the sample was stored at 4℃. Four times the volume of distilled water was added to dilute the fish protein gel solution to 1%. Similarly, 30 mL (V0) of the 1% sample was poured into a 100 mL Erlenmeyer flask and homogenized at 13600 rpm for 2 min. The solution was then immediately transferred to a 100 mL graduated cylinder, and the foam volume (V1) was recorded. After standing for 30 min, the foam volume (V2) was recorded.

[0046] from Figure 3 As can be seen, foaming ability increases and then decreases with increasing enzyme dosage, with the 10 U / g sample exhibiting the highest foaming ability. However, the foaming stability of all enzymatically hydrolyzed samples decreased. After enzymatic hydrolysis, compared with the pure fish protein gel group, FA increased by up to 140%, while FS decreased by up to 11.11%. Moderate hydrolysis of fish protein gel by neutral proteases disrupts the spatial conformation of the protein, making the dense structure looser and exposing more hydrophobic groups to the molecular surface, resulting in higher density and more fish protein gel foam, thus improving foaming ability. The interaction between protein peptide chains weakens, and its network structure is destroyed, reducing foaming stability. However, excessive hydrolysis may lead to too much destruction of the protein structure, preventing small molecules from forming an adhesive film at the interface, resulting in reduced foaming ability and foam stability. Among these, different lowercase letters represent significant differences in foaming ability and foaming stability (p < 0.05).

[0047] Comparative Example 2 Effects of different hydrophilic colloids on the foaming properties and foam stability of fish protein gel solution: Fish protein gel solution was prepared according to the method in Example 1. The pH of the obtained fish protein gel solution was adjusted to 6.8-7.2. 20 mL of fish protein gel solution was taken and neutral protease solution was added (neutral protease activity was set at 10 U / g fish protein gel). It was enzymatically hydrolyzed for 30 min, and then the enzyme was inactivated for 10 min. After cooling, sodium carboxymethyl cellulose, sodium alginate, pectin, and gum arabic were added to the fish protein gel solution and completely dissolved and stabilized in a 40℃ water bath for 10 min. After that, the pH was adjusted to 6.8-7.2, and then the sample was stored at 4℃. 4 times the volume of distilled water was added to dilute the fish protein gel solution to 1%, and then the foaming properties and foam stability were measured. 30 mL (V0) 1% sample was poured into a 100 mL conical flask and homogenized at 13600 rpm for 2 min. Then immediately transfer the solution quickly to a 100mL graduated cylinder and record the foam volume (V1); let it stand for 30 min and record the foam volume (V2).

[0048] To compensate for the reduced foaming stability caused by the damage to the fish protein gel structure by neutral proteases, several hydrophilic colloids were screened; from Figure 4 As can be seen, all hydrophilic colloids improved the foaming stability of enzymatically modified fish protein gel, but the gum arabic group showed the best overall performance, with FS increasing to 55.4% and FA increasing to 158%, which not only improved foaming stability but also further enhanced foaming properties. Different lowercase letters indicate significant differences in foaming properties and foaming stability (p<0.05).

[0049] Comparative Example 3 Effects of different gum arabic concentrations on the foaming properties and foam stability of fish protein gelatin solution: Fish protein gelatin solution was prepared according to the method in Example 1. The pH of the obtained 5% fish protein gelatin solution was adjusted to 6.8-7.2. 20 mL of the fish protein gelatin solution was taken and neutral protease solution (neutral protease addition amount was 10 U / g fish protein gelatin) was added. Enzymatic hydrolysis was performed for 30 min, followed by enzyme inactivation for 10 min. After cooling, 0, 0.05%, 0.1%, 0.15%, and 0.2% gum arabic were added to the fish protein gelatin solution, respectively. The solution was completely dissolved and stabilized in a 40℃ water bath for 10 min. The pH was then adjusted to 6.8-7.2, and the sample was stored at 4℃. Four times the volume of distilled water was added to dilute the fish protein gelatin solution to 1%, and then the foaming properties and foam stability were determined. 30 mL (V0) of the 1% sample was poured into a 100 mL Erlenmeyer flask and homogenized at 13600 rpm for 2 min. Then immediately transfer the solution quickly to a 100mL graduated cylinder and record the foam volume (V1); let it stand for 30 min and record the foam volume (V2).

[0050] fromFigure 5 It was found that with the increase of gum arabic concentration, both foaming properties and foam stability showed a trend of first increasing and then decreasing. Fish protein glue with 0.1% gum arabic added exhibited the best foaming properties and foam stability. Gum arabic is composed of arabinogalactan peptide (AG), arabinogalactan protein (AGP), and glycoprotein (GP). Among them, the β-(1,6)-galactopyranose side chain of AGP is linked to the hydroxyl groups of polar amino acids in fish protein glue, forming a hydrogen bond network. This facilitates the rapid adsorption of protein molecules at the air-water interface and subsequently reduces the interfacial tension to a low level, enhancing foaming properties and foam stability. Different lowercase letters indicate significant differences in foaming properties and foam stability (p<0.05).

[0051] Table 1. Numerical Results of Each Embodiment and Comparative Example

[0052] As shown in Table 1, treatment with larger neutral protease activities resulted in smaller fish protein gel particle sizes. The PDI (Potential Density Intake) did not change significantly, but the potential initially decreased and then increased, and the foaming property initially increased and then decreased. This indicates that excessive enzymatic hydrolysis reduces foaming property, and the resulting peptides re-aggregate, increasing foaming stability. Figure 3 As can be seen, with the increase of enzyme dosage, the foaming property showed a trend of increasing and then decreasing, but the foaming stability of all enzymatically hydrolyzed samples decreased. Neutral protease significantly helped increase the foaming property of fish protein gel. Figure 4 As can be seen, all hydrophilic colloids improved the foaming stability of the enzymatically modified fish protein gel, but the gum arabic group showed the best overall performance; from Figure 5 It can be seen that with the increase of gum arabic concentration, both foaming properties and foaming stability show a trend of first increasing and then decreasing. Fish protein glue with 0.1% gum arabic added has the best foaming properties and foaming stability. Therefore, the optimal enzyme activity for neutral protease is 10 U / g fish protein glue. After enzymatic hydrolysis, the particle size of the composite modified fish protein glue first decreases and then increases with the increase of gum arabic concentration, while the potential gradually increases, indicating that fish protein glue molecules bind with more gum arabic. The optimal content of gum arabic is 0.1 wt%.

[0053] The above description is merely a specific embodiment of the present invention, but the scope of protection of the present invention is not limited thereto. Any variations or substitutions that can be easily conceived by those skilled in the art within the technical scope disclosed in the present invention should be included within the scope of protection of the present invention. Therefore, the scope of protection of the present invention should be determined by the scope of the claims. Furthermore, specific examples have been used in the specification to illustrate the principles and implementation methods of the present invention. The above description of the embodiments is only for the purpose of helping to understand the method and core ideas of the present invention, and the content of this specification should not be construed as a limitation of the present invention.

Claims

1. A method for preparing a highly foaming fish protein gel, characterized in that, The method includes the following steps: S1, Prepare fish protein gel solution; S2, dissolve gum arabic in the fish protein gum solution obtained in step S1; S3, Adjust the pH of the solution obtained in step S2, and add enzymes for enzymatic hydrolysis; S4, inactivate the enzyme in the material after enzymatic hydrolysis, and then adjust the pH value again after enzyme inactivation; S5, the material obtained from the low-temperature freezing step S4 is freeze-dried to obtain the high foaming fish protein gel.

2. The method according to claim 1, characterized in that, In step S1, the protein concentration of the fish protein gel solution is 5 wt%. The fish protein gel in the fish protein gel solution is derived from tilapia.

3. The method according to claim 1, characterized in that, In step S2, the mass ratio of gum arabic to fish protein gelatin solution is 1:(30~70), preferably 1:50; And / or, in step S2, after dissolving gum arabic in the fish protein glue solution obtained in step S1, it needs to be allowed to stand for 10 minutes to stabilize the solution system.

4. The method according to claim 1, characterized in that, In step S3, the pH value of the solution obtained in step S2 is adjusted to 6.8~7.2, preferably 7.0; And / or, in step S3, a neutral protease is used for enzymatic hydrolysis.

5. The method according to claim 1, characterized in that, In step S3, the amount of enzymatic hydrolysis added is 8~15 U / g, preferably 10 U / g.

6. The method according to claim 1, characterized in that, In step S3, the enzymatic hydrolysis time is 20-40 min, preferably 30 min; And / or, in step S3, the temperature during enzymatic hydrolysis is 35~42℃, preferably 40℃.

7. The method according to claim 1, characterized in that, In step S4, the enzyme is inactivated by boiling water bath for 10 minutes.

8. The method according to claim 1, characterized in that, In step S4, after enzyme inactivation, the pH value is adjusted to 6.8~7.2, preferably 7.

0.

9. The method according to claim 1, characterized in that, In step S5, the freeze-drying temperature is -70~-80℃, preferably -80℃, the freeze-drying time is 24~48h, preferably 48h, and the freeze-drying pressure is 5~7MPa, preferably 5MPa.

10. A highly foaming fish protein gel, characterized in that, Obtained by the method of any one of claims 1 to 9.

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