Method for flexibly regulating and controlling gel strength through food protein molecules

Through thermal processing collaborative physical tandem modification technology, the flexibility of food protein molecules is regulated, and the problem of insufficient gel strength in the existing technology is solved, and the ease of swallowing performance and resource utilization are improved.

CN119498438APending Publication Date: 2025-02-25XIHUA UNIV
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Patent Information

Application Number
CN202411408200.0
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2024-10-10
Publication Date
2025-02-25

AI Technical Summary

Technical Problem

The prior art is difficult to effectively improve the flexibility of food protein molecules, thereby increasing the strength of the gel, especially under low temperature conditions.

Method used

Through thermal processing collaborative physical tandem modification technology, the three-dimensional spatial structure of animal and plant double proteins is regulated, the proportion of flexible intervals of protein molecules is enhanced, and the self-assembly and aggregation of flexible molecules is promoted at low temperatures to achieve an increase in gel strength.

Benefits of technology

The easy swallowing performance of protein gels is achieved, the gel strength is increased by more than 20%, the utilization rate of marine and grain and oil resources is improved, and the utilization rate of low-value processing by-products is improved.

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Abstract

The invention discloses a method for flexibly regulating and controlling the gel strength of food protein molecules, which comprises the steps of curing, fish meat prefabrication, protein compounding, protein molecule flexible regulation and control, low-temperature induction and the like, and particularly comprises the following steps: mixing heated and cured fish meat with a salt solution, rinsing, filtering, mixing with vegetable protein, adding water to obtain a protein mixture, and performing physical modification, so as to obtain the food protein molecule flexible regulation and control gel strength. And finally, the protein gel is placed in a low-temperature environment and stored for a period of time, and the protein gel with the gel strength / hardness improved is obtained. According to the invention, thermal processing is cooperated with a physical series modification technology, so that the flexibility of animal and plant protein molecules is improved, the self-assembly crosslinking of the molecules is promoted, a compact and uniform network structure is formed inside, and the protein gel with easy swallowing performance is obtained; in addition, by-products such as minced meat, broken rice, oil meal and the like left after processing can be used as raw materials to prepare the easy-to-swallow gel, and the utilization rate of low-value processing by-products can be increased.
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Description

Technical Field

[0001] The invention belongs to the technical field of food processing and relates to a method for improving gel strength by flexible regulation of food protein molecules. Background Art

[0002] The three-dimensional structure of protein is the basis of its biochemical function. The flexible region of protein can be generally understood as the part that is easy to change in the spatial structure of protein molecules, while the part with stable and solid structure that is not easy to change is called rigid region. By changing the natural rigid structure of protein and making it flexible, the comprehensive application value of protein such as functional properties, nutritional properties and biological functions can be greatly improved.

[0003] As a new type of nutritious and healthy food, dual-protein food combines the dual advantages of plant protein and animal protein. It has great potential in promoting human health, preventing nutritional deficiencies and assisting disease management. It is one of the important directions for the development of the food industry to increase efforts to innovate basic research and processing technology and carry out basic research on dual-protein engineering. Mixing plant protein with animal protein can improve anabolic function by balancing amino acid distribution, maintaining amino acid release and utilizing synergistic effects. This is a strategy to solve the problem of a single protein source in the diet. Summary of the invention

[0004] The purpose of the present invention is to provide a method for flexibly regulating gel strength of food protein molecules in response to the deficiencies in the prior art. Through thermal processing and physical tandem modification technology, the three-dimensional spatial structure of plant and animal diproteins is regulated, the proportion of molecular flexible intervals is increased, and self-assembly aggregation of flexible molecules is promoted at low temperatures, thereby achieving improved gel strength.

[0005] To achieve the above object, the technical solution of the present invention is to provide a method for flexibly regulating gel strength of food protein molecules, comprising the following steps:

[0006] S1. Cooking: heating and cooking the fish meat of the raw material fish to obtain cooked fish meat;

[0007] S2, fish meat pre-preparation: the cooked fish meat obtained in step S1 is mixed with 1-20 g / L NaCl solution at a solid-liquid ratio of 1:10 to 1:1000 g / mL, rinsed, and filtered to obtain pre-prepared fish meat;

[0008] S3, protein compounding: the pre-prepared fish meat obtained in step S2 is mixed with a plant protein having a concentration of 10 to 20 mg / mL, with a mixing mass: volume ratio of 10:0 to 10:6 (g:mL), and finally water is added to make the total mass 5 times the mass of the pre-prepared fish meat to obtain a protein mixture;

[0009] S4, protein molecule flexibility regulation technology: the protein mixture obtained in step S3 is physically modified to increase the flexibility of the protein molecules to above 0.1, thereby obtaining a flexible protein solution;

[0010] S5, low temperature induction: the flexible protein solution obtained in step S4 is placed in an environment of 2 to 10°C for 12 to 48 hours to obtain a protein gel.

[0011] In one embodiment, the raw fish in step S1 is cod, sturgeon or grass carp; the heating and maturation is performed by heating at 60-100° C. in a water bath or under steam conditions for 5-30 min.

[0012] In one embodiment, the raw fish described in step S1 includes frozen raw fish and fish meat of fresh fish, and the fish body is skinned, boned and visceral to obtain the fish meat.

[0013] In one embodiment, the rinsing temperature in step S2 is 40-70° C., and the rinse is performed 3-10 times, each time for 1-5 minutes.

[0014] In one embodiment, the filtration in step S2 is performed using a 60-100 mesh filter cloth.

[0015] In one embodiment, the water in step S3 is purified water or mineral water.

[0016] In one embodiment, the plant protein in step S3 is rice protein or rapeseed protein.

[0017] In one embodiment, the rice protein in step S3 can come from broken rice produced by processing indica rice or japonica rice, and the rapeseed protein can be extracted from rapeseed, a raw material for rapeseed oil processing, or rapeseed meal, a byproduct, or microalgae protein recovered from sewage treatment.

[0018] In one embodiment, the physical modification method in step S4 includes ultrasound, high-pressure microfluidization, and homogenization.

[0019] The present invention also provides a protein gel with easy-to-swallow properties obtained by the above method. The strength / hardness of the obtained gel is increased by more than 20% compared with that before the flexibility of the protein molecules is increased.

[0020] The beneficial effects of the present invention are:

[0021] 1. The present invention creatively proposes a method for regulating molecular flexibility, that is, through thermal processing and physical series modification technology, the flexibility of animal and plant protein molecules is improved, which helps to promote molecular self-assembly and cross-linking, form a dense and uniform network structure inside, and obtain a protein gel with easy-to-swallow performance.

[0022] 2. The three-dimensional structure of protein is the basis of its biochemical function. The present invention improves the flexibility of protein molecules through physical modification and dual protein coupling.

[0023] 3. The present invention fully improves the utilization rate of marine, grain and oil resources, and can use some by-products such as minced meat, broken rice, and oil cakes left over from processing as raw materials to prepare easy-to-swallow gel, which helps to improve the utilization rate of low-value processing by-products. BRIEF DESCRIPTION OF THE DRAWINGS

[0024] Figure 1 is a macroscopic image of a gel prepared from a single protein in Example 1 of the present invention;

[0025] Figure 2 This is a macroscopic image of the gel prepared from the double protein in Example 2 of the present invention;

[0026] Figure 3 This is a macroscopic image of the sample prepared in comparative example 1 of the present invention, where I, II, and III are state images before, during, and after the TPA probe presses the sample, respectively. DETAILED DESCRIPTION

[0027] Test method:

[0028] Determination of molecular flexibility: 250 μL of trypsin solution (trypsin powder was dissolved in Tris-HCL buffer at pH 8.0, 1 mg / mL) was mixed with 4 mL (sample) protein solution (1 mg / mL), placed in a 38°C water bath for 5 min, and 4 mL of trichloroacetic acid (5%) was used to terminate the enzymatic reaction. The enzymatic supernatant was centrifuged at 25°C and 10,000 rpm for 30 min, and its absorbance at 280 nm was characterized as molecular flexibility.

[0029] Gel hardness determination: The sample was measured using a texture analyzer, and the TPA mode was selected. The probe was P36R, the parameter strain was adjusted to 20%, the trigger force was 5g, and the speed before / during / after the measurement was 1.0mm / s.

[0030] Example 1

[0031] S1. Cooking: heating and cooking fresh grass carp meat to obtain cooked fish meat;

[0032] S2, fish meat pre-preparation: the cooked fish meat obtained in step S1 is mixed with 0.1% NaCl salt solution, rinsed 5 times at 60° C., and filtered through 80-mesh filter cloth to obtain pre-prepared fish meat;

[0033] S3, protein compounding: the pre-prepared fish meat obtained in step S2 is mixed with the vegetable protein, the mixing mass: volume ratio is 10:0 (g:mL), and finally water is added to make the total mass 5 times the mass of the fish meat to obtain a protein mixture;

[0034] S4, protein molecule flexibility regulation technology: the protein mixture obtained in step S3 is subjected to ultrasonic treatment (480W, 10min) to increase the flexibility of the protein molecules to 0.175, thereby obtaining a flexible protein solution;

[0035] S5, low temperature induction: the flexible protein solution obtained in step S4 was placed in an environment of 2-10°C for 12 hours to obtain a protein gel. The gel hardness was 23.35 g. Before the flexibility of the protein molecules was improved, the sample was in a non-gel state, and its gel hardness could not be measured.

[0036] Example 2

[0037] S1. Cooking: heating and cooking the thawed cod fish meat to obtain cooked fish meat;

[0038] S2, fish meat pre-preparation: the cooked fish meat obtained in step S1 is mixed with 0.1% NaCl salt solution, rinsed 5 times at 60° C., and filtered through 80-mesh filter cloth to obtain pre-prepared fish meat;

[0039] S3, protein compounding: the pre-prepared fish meat obtained in step S2 is mixed with the vegetable protein, the mixing mass: volume ratio is 10:0 (g:mL), and finally water is added to make the total mass 5 times the mass of the fish meat to obtain a protein mixture;

[0040] S4, protein molecule flexibility regulation technology: the protein mixture obtained in step S3 is subjected to ultrasonic treatment (400W, 8min) to increase the flexibility of the protein molecules to 0.33, thereby obtaining a flexible protein solution;

[0041] S5, low temperature induction: the flexible protein solution obtained in step S4 is placed in an environment of 2-10°C for 12 hours to obtain cod protein gel, and the gel hardness reaches 23.46g. Before the flexibility of the protein molecules is improved, the sample is in a non-gel state, and its gel hardness cannot be measured. The obtained protein gel has the characteristic of being easy to swallow, and can be used as a meal for special groups such as the elderly and patients with postoperative dysphagia.

[0042] Example 3

[0043] S1. Cooking: heating and cooking Atlantic cod meat to obtain cooked fish meat;

[0044] S2, fish meat pre-preparation: the cooked fish meat obtained in step S1 is mixed with 0.1% NaCl salt solution, rinsed 7 times at 60° C., and filtered through 80-mesh filter cloth to obtain pre-prepared fish meat;

[0045] S3, protein compounding: the prefabricated fish obtained in step S2 is mixed with rice protein (15 mg / mL), the mixed mass: volume ratio is 10:4 (g:mL), and water is finally added to make the total mass 5 times of the fish mass to obtain a protein mixture;

[0046] S4, protein molecule flexibility regulation technology: The protein mixture obtained in step S3 is subjected to ultrasonic treatment (400W, 8min) to increase the flexibility of the protein molecules to 0.38, which is higher than the flexibility of the protein molecules in Example 2, to obtain a flexible protein solution;

[0047] S5. Low temperature induction: The flexible protein solution obtained in step S4 was placed in a 3°C environment for 24 hours to obtain a mixed protein gel. The gel hardness was increased to 40.81 g, which was 73.96% higher than the gel strength of the sample in Example 2.

[0048] Example 4

[0049] S1. Cooking: heating and cooking Atlantic cod meat to obtain cooked fish meat;

[0050] S2, fish meat pre-preparation: the cooked fish meat obtained in step S1 is mixed with 0.1% NaCl salt solution, rinsed 7 times at 60° C., and filtered through 80-mesh filter cloth to obtain pre-prepared fish meat;

[0051] S3, protein compounding: the pre-prepared fish meat obtained in step S2 was mixed with rapeseed protein (15 mg / mL) at a mixing mass: volume ratio of 10:2 (g:mL), and finally water was added to make the total mass 5 times the mass of the fish meat to obtain a protein mixture;

[0052] S4, protein molecule flexibility regulation technology: the protein mixture obtained in step S3 is subjected to ultrasonic treatment (450W, 8min) to increase the flexibility of the protein molecules to 0.49, thereby obtaining a flexible protein solution;

[0053] S5. Low temperature induction: The flexible protein solution obtained in step S4 was placed in a 3°C environment for 24 hours to obtain a mixed protein gel, and the gel hardness was increased to 60.40 g.

[0054] Comparative Example 1

[0055] S1. Cooking: heating and cooking the thawed cod meat to obtain cooked fish meat;

[0056] S2, fish meat pre-preparation: the cooked fish meat obtained in step S1 is mixed with 0.1% NaCl salt solution, rinsed 5 times at 60° C., and filtered through 80-mesh filter cloth to obtain pre-prepared fish meat;

[0057] S3, protein compounding: the pre-prepared fish meat obtained in step S2 is mixed with the vegetable protein, the mixing mass: volume ratio is 10:0 (g:mL), and finally water is added to make the total mass 5 times the mass of the fish meat to obtain a protein mixture;

[0058] S4, low temperature induction: the protein mixture obtained in step S3 is placed in an environment of 2-10°C and stored for 12 hours to obtain a cod protein complex. The complex has a solid-like appearance, but after being pressed by a TPA test probe, the sample cannot return to its original shape and is not a protein gel.

[0059] It should be noted that the above is only a preferred embodiment of the present invention and is not intended to limit the present invention. For those skilled in the art, the present invention may have various modifications and variations. Without making creative work, any modification, equivalent replacement, improvement, etc., shall be included in the protection scope of the present invention.

Claims

1. A method for flexibly regulating gel strength of food protein molecules, characterized in that: The steps include: The cooked fish meat is mixed with 1-20 g / L NaCl solution at a solid-liquid ratio of 1:10 to 1:1000 g / mL, rinsed, and filtered to obtain the pre-prepared fish meat; The prepared fish meat is mixed with a plant protein having a concentration of 10 to 20 mg / mL at a mass-to-volume ratio of 10:0 to 10:6 g / mL, and water is added to a total mass that is 5 times the mass of the prepared fish meat to obtain a protein mixture; Physically modifying the protein mixture so that the flexibility of the protein molecules is increased to above 0.1, thereby obtaining a flexible protein solution; The flexible protein solution is placed at 2-10° C. for 12-48 hours to obtain a protein gel.

2. The method according to claim 1, characterized in that The cooked fish meat is prepared by heating and cooking the fish meat of raw fish.

3. The method according to claim 2, characterized in that The raw fish is cod, sturgeon or grass carp; the heating and maturation is heating for 5 to 30 minutes under 60 to 100° C. water bath or steam conditions.

4. The method according to claim 1, characterized in that: The rinsing temperature is 40-70° C., and the rinsing is performed 3-10 times, each time for 1-5 minutes. The filtration is performed using a 60-100 mesh filter cloth.

5. The method according to claim 1, characterized in that The plant protein is rice protein or rapeseed protein.

6. The method according to claim 5, characterized in that The rice protein comes from broken rice produced by processing indica rice and japonica rice, and the rapeseed protein is extracted from rapeseed, rapeseed meal or microalgae protein recovered from sewage treatment.

7. The method according to claim 1, characterized in that The water is purified water or mineral water.

8. The method according to claim 1, characterized in that The physical modification methods include ultrasound, high-pressure microfluidization and homogenization.

9. A protein gel with easy-to-swallow properties obtained by the method according to any one of claims 1 to 8.