Aquatic-plant Protein Combined Restructured Meat and Preparation Method thereof

Abstract

The present disclosure discloses an aquatic-plant protein combined restructured meat and a preparation method thereof, and belongs to the technical field of processing of foods. According to the present disclosure, a protein combined restructuring processing technology can be summarized as including pretreatment of an aquatic-plant protein, combined restructuring, high-temperature qualitative treatment, and integrated forming. The whole process is green, safe, and environmentally friendly. The protein combined restructured meat prepared contains two proteins including an animal protein and a plant protein, and has a protein content of greater than 20%. While the demands for nutritional dietary proteins are met, the chewability is greater than 1,500 g.Math.mm, and the viscoelasticity is excellent. The meat can be processed in various shapes according to needs, directly heated for eating, or processed into a prepared food, a semi-finished product and the like, so that the product has a large application space.

Claims

1. A preparation method of an aquatic-plant protein combined restructured meat, comprising the following steps: (1) preparation of an aquatic protein: defrosting an aquatic animal meat slice, conducting cutting and chopping, conducting soaking and cleaning in baking soda to obtain a meat pulp, and dewatering the meat pulp with a physical field to obtain an aquatic protein pulp; (2) preparation of a plant protein: weighing a plant protein powder accounting for 5%-15% of the mass of the aquatic protein pulp obtained in step (1); (3) uniform mixing and stirring: conducting mixing and stirring on the aquatic protein pulp obtained in step (1) and the plant protein powder obtained in step (2) until a homogeneous state is reached, and then obtaining a protein homogenate; (4) pretreatment of a protein: adding a complex salt to the protein homogenate obtained in step (3) for pickling and rolling, adding a food-grade acid-base regulator for adjusting the pH so as to form a paste protein, and then obtaining the paste protein; (5) combined restructuring: adding protease to the paste protein obtained in step (4), adding a natural small-molecule substance for crosslinking and restructuring of a protein, adding a color improver at the same time, conducting uniform mixing and stirring, and then conducting incubation in a water bath, wherein the natural small-molecule substance is epigallocatechin gallate (EGCG); (6) high-temperature qualitative treatment: subjecting a product obtained in step (5) to inactivation and qualitative treatment in a high-temperature water bath, and then conducting cooling rapidly to room temperature; and (7) integrated forming: conducting press forming on a sample obtained in step (6), or directly kneading the sample in the shape of a desired product to obtain the aquatic-plant protein combined restructured meat.

2. The method according to claim 1, wherein in step (2), the plant protein powder is derived from one of soybeans, peas, black beans, mung beans, kidney beans, and chickpeas.

3. The method according to claim 1, wherein in step (3), the mixing mass ratio of the aquatic protein pulp to the plant protein is 30:1 to 1:1.

4. The method according to claim 1, wherein in step (4), the complex salt is a complex of NaCl and phosphate, the added amount of the NaCl is controlled to be 0.5-1.5 wt % of the weight of the protein homogenate, and the added amount of the phosphate is 0-0.7 wt % of the weight of the protein homogenate.

5. The method according to claim 1, wherein in step (5), the protease is one of glutamine transaminase, papain, bromerain, and flavourzyme.

6. The method according to claim 1, wherein in step (5), the protease accounts for 0.2-4.0 wt % of the weight of the paste protein.

7. The method according to claim 1, wherein in (5), the added amount of the natural small-molecule substance is 0.02-0.20 wt % of the weight of the paste protein.

8. An aquatic-plant protein combined restructured meat prepared by the method according to claim 1.

9. A health food containing the aquatic-plant protein combined restructured meat according to claim 8.

Description

BRIEF DESCRIPTION OF FIGURES

[0042] FIG. 1 is a diagram showing a process flow of an aquatic-plant protein combined restructured meat prepared by the present disclosure.

DETAILED DESCRIPTION

[0043] The following examples are used to illustrate the present disclosure, rather than to limit the scope of the present disclosure. All modifications or substitutions of the method, steps or conditions of the present disclosure made without departing from the spirit and essence of the present disclosure shall fall within the scope of the present disclosure.

[0044] Unless particularly specified, experimental materials, reagents, instruments and the like used in the examples of the present disclosure are commercially available. Unless specifically specified, technical means used in the examples are conventional means well known to persons skilled in the art.

[0045] Test methods in the following examples:

[0046] Protein content: The protein content is determined by an automatic Kjeldahl apparatus.

[0047] 1) 0.50-1.00 g of a sample was weighed and placed in a digestion flask, two tablets made of copper sulfate and potassium sulfate were added, and 10 ml of concentrated sulfuric acid was added. The digestion flask was placed in a digestion furnace, and then connected and sealed with a connection tube. An air pumping device was started, and a power supply of the digestion furnace was turned on. After a digestion solution was completely clarified and turned into bluish green, digestion was conducted for 30 min until the sample was completely digested.

[0048] 2) The digestion flask was taken out and transferred into an automatic Kjeldahl apparatus, and relevant procedures, such as alkali addition, water addition, and distillation time, were set.

[0049] 3) After a start key was pressed, distillation titration was automatically completed by the apparatus, and the results were displayed.

[0050] 4) A digestion tube was taken out and cleanly rinsed for use in the next time.

[0051] Full-texture test: A P20 cylindrical probe with the cross-sectional area greater than the area of a sample was selected. The running track of the probe was as follows: the probe was started in the form of auto-20 g and compressed to the test sample at a pre-test rate of 2 mm/s from a starting position; after touching the surface of the sample, the probe was compressed to the sample at a test rate of 2 mm/s with a compression ratio of 30%; and after returning to a compression trigger point and waiting for an interval of 5 s, the probe was continuously compressed down for the same distance at a rate of 2 mm/s and then returned to the position before the test at a post-test rate of 5 mm/s.

[0052] Elasticity is expressed by the height at which the sample recovers after first compression.

[0053] Hardness is expressed by the force at which the maximum degree of compression is reached in a first compression process.

[0054] Cohesiveness is expressed by the ratio of the peak area in a second compression process to the peak area in the first compression process.

[0055] Adhesion is expressed by the negative peak area in a first ascending process.

[0056] Recoverability is expressed by the ratio of the peak area in the first ascending process to the peak area in a descending process.

[0057] Chewability is expressed by hardness*cohesiveness*elasticity.

Example 1

[0058] (1) Preparation of an aquatic protein: 500 g of frozen basa fish slices were defrosted at low temperature, cut and chopped into evenly diced meats with a size of about 0.8 cm, and soaked and cleaned in 0.6% baking soda for 8 min to obtain a meat pulp. The meat pulp was treated with a dewatering machine to remove free water, and then a protein pulp was obtained.

[0059] (2) Preparation of a plant protein: Soybeans were crushed and sifted, and n-hexane accounting for 4 times the volume of the soybeans was added for degreasing. A degreased soybean powder was resuspended in deionized water. Next, the pH of an obtained solution was adjusted to 9.0 with sodium hydroxide, stirring was conducted at a constant temperature of 30° C. for 2 h, centrifugation was conducted to obtain a supernatant, and the pH was adjusted to 4.0 with hydrochloric acid. The above steps were repeated for 2 times. Then, centrifugation was conducted at 8,000 rpm for 15 min, and a protein precipitate was collected and washed with deionized water until the pH was neutral. Finally, freeze-drying was conducted to obtain a soybean protein isolate.

[0060] (3) Uniform mixing and stirring: The aquatic protein pulp obtained in step (1) and a soybean protein powder obtained in step (2) were mixed and stirred at a mass ratio of 10:1 at 4° C. for 25 min until a homogeneous state was reached, and then a protein homogenate was obtained.

[0061] (4) Pretreatment of a protein: A complex salt (including NaCl and phosphate) was added to the protein homogenate obtained in step (3) for pickling and rolling for 50 min, where the added amount of the NaCl was controlled to be 0.8 wt % of the weight of the protein homogenate, and the added amount of the phosphate (consisting of sodium pyrophosphate, sodium tripolyphosphate and sodium hexametaphosphate at a mass ratio of 3:5:1) was 0.4 wt % of the weight of the protein homogenate. Then food-grade sodium lactate was added for adjusting the pH to 7.5 so as to form a meat paste, and a paste protein was obtained.

[0062] (5) Combined restructuring: 1.0 wt % of glutamine transaminase and 0.10 wt % of epigallocatechin gallate (EGCG) were added to the paste protein obtained in step (4) for uniform mixing. Next, 0.35 wt ‰ of monascus red (which was purchased from a local supermarket in Wuxi, and has a CAS Number of 874807-57-5) was added for uniform stirring. Then, incubation was conducted in a water bath at 50° C. for 120 min to obtain a protein combined restructured meat, where the glutamine transaminase had an enzyme activity of 10 units/mg.

[0063] (6) High-temperature qualitative treatment: The protein combined restructured meat obtained in step (5) was subjected to inactivation and qualitative treatment in a high-temperature water bath at 90° C. for 10 min, and then cooling was conducted rapidly to room temperature to obtain an aquatic-plant protein combined restructured meat sample.

[0064] (7) Integrated forming: The aquatic-plant protein combined restructured meat sample obtained in step (6) was directly kneaded in the shape of a meat pie.

[0065] The aquatic-plant protein combined restructured meat prepared in Example 1 has high protein content, good color and lustre, moderately soft and hard taste, good elasticity, good chewability, obvious fleshy taste, good flavor and no obvious fishy taste.

Example 2

[0066] With reference to Example 1, the difference was only that the soybeans in step (2) were separately substituted with mung beans, peas, black beans, kidney beans, and chickpeas. Results of properties of obtained aquatic-plant protein combined restructured meats were as shown in Table 1.

TABLE-US-00001 TABLE 1 Comparison table of properties of aquatic-plant protein combined restructured meats prepared with different plant proteins Protein Plant content Elasticity Hardness Adhesion Chewability protein (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) Soybeans 22 0.754 3150.487 0.76 0.348 −18.329 1805.355 Mung beans 21 0.745 3268.147 0.68 0.315 −20.249 1655.643 Peas 19 0.716 3045.896 0.65 0.327 −19.863 1417.560 Black beans 17 0.734 2968.721 0.71 0.298 −17.548 1547.119 Kidney beans 18 0.689 3054.762 0.59 0.259 −16.982 1241.791 Chickpeas 20 0.74 3348.146 0.61 0.264 −16.254 1511.353

[0067] From the data in Table 1, it can be seen that the type of the plant protein has little influence on the protein content of a product, but has certain influence on the texture and taste of the product, and the soybean protein has the best effect.

Example 3

[0068] With reference to Example 1, the difference was only that the glutamine transaminase (TG enzyme) in step (5) was separately substituted with papain, bromerain, and flavourzyme. Results of properties of obtained aquatic-plant protein combined restructured meats were as shown in Table 2.

TABLE-US-00002 TABLE 2 Comparison table of properties of aquatic-plant protein combined restructured meats prepared after treatment with different enzymes Protein content Elasticity Hardness Adhesion Chewability Protease (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) TG enzyme 22 0.754 3150.487 0.76 0.348 −18.329 1805.355 Papain 16 0.647 3215.468 0.68 0.315 −15.146 1414.677 Bromerain 14 0.568 3048.853 0.72 0.287 −12.864 1246.859 Flavourzyme 18 0.698 2959.487 0.61 0.296 −14.437 1260.090

[0069] From the data in Table 2, it can be seen that the type of the protease has certain influence on the protein content, texture and taste of a product, and the glutamine transaminase (TG enzyme) has the best effect.

Example 4

[0070] With reference to Example 1, the difference was only that the epigallocatechin gallate (EGCG) in step (5) was separately substituted with genipine, resveratrol, curcumin, and rosmarinic acid. Results of properties of obtained aquatic-plant protein combined restructured meats were as shown in Table 3.

TABLE-US-00003 TABLE 3 Comparison table of properties of aquatic-plant protein combined restructured meats prepared with different natural small molecules Protein content Elasticity Hardness Adhesion Chewability Protease (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) EGCG 22 0.754 3150.487 0.76 0.348 −18.329 1805.355 Genipine 20 0.742 3058.465 0.65 0.315 −19.543 1475.098 Resveratrol 19 0.716 3287.914 0.71 0.321 −17.425 1671.444 Curcumin 18 0.782 3398.147 0.59 0.285 −16.527 1567.837 Rosmarinic 17 0.705 3008.698 0.68 0.294 −19.613 1442.370 acid

[0071] From the data in Table 3, it can be seen that the type of the natural small molecule has little influence on the protein content of a product, but has certain influence on the texture and taste of the product, and the EGCG has the best effect.

Example 5

[0072] With reference to Example 1, the difference was only that the mixing ratio of the aquatic protein pulp to the soybean protein powder in step (3) was separately changed into 30:1, 20:1, 5:1, and 1:1 Results of properties of obtained aquatic-plant protein combined restructured meats were as shown in Table 4.

TABLE-US-00004 TABLE 4 Comparison table of properties of aquatic-plant protein combined restructured meats prepared at different protein mixing ratios Protein Mixing content Elasticity Hardness Adhesion Chewability ratio (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) 30:1 17 0.564 3285.198 0.58 0.283 −14.285 1074.654 20:1 19 0.688 3195.487 0.69 0.301 −16.358 1516.962 10:1 22 0.754 3150.487 0.76 0.348 −18.329 1805.355  5:1 28 0.675 2898.583 0.61 0.215 −14.527 1193.492  1:1 53 0.614 2248.942 0.46 0.186 −10.591 635.1912

[0073] From the data in Table 4, it can be seen that when the mixing ratio of the aquatic protein pulp to the soybean protein powder is lower, a product has higher protein content, and when the ratio is 10:1, the product has the best texture and taste.

Example 6

[0074] With reference to Example 1, the difference was only that the use amount of the glutamine transaminase in step (5) was separately changed into 0.2%, 0.5%, 1.0%, 2.0%, and 4.0%. Results of properties of aquatic-plant protein combined restructured meats obtained were as shown in Table 5.

TABLE-US-00005 TABLE 5 Comparison table of properties of aquatic-plant protein combined restructured meats prepared with different use mounts of TG enzyme Protein Use content Elasticity Hardness Adhesion Chewability amount/% (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) 0.2 24 0.705 3021.046 0.68 0.288 −14.587 1448.289 0.5 23 0.728 3047.345 0.73 0.312 −16.458 1619.481 1.0 22 0.754 3150.487 0.76 0.348 −18.329 1805.355 2.0 20 0.748 2987.465 0.67 0.334 −19.618 1497.198 4.0 19 0.719 2876.423 0.61 0.316 −20.247 1261.570

[0075] From the data in Table 5, it can be seen that the use amount of the glutamine transaminase has little influence on the protein content of a product, and when the use amount of the glutamine transaminase is 1.0%, the product has the best texture and taste.

Example 7

[0076] With reference to Example 1, the difference was only that the use amount of the epigallocatechin gallate (EGCG) in step (5) was separately changed into 0.02%, 0.05%, 0.10%, 0.15%, and 0.20%. Results of properties of aquatic-plant protein combined restructured meats obtained were as shown in Table 6.

TABLE-US-00006 TABLE 6 Comparison table of properties of aquatic-plant protein combined restructured meats prepared with different use mounts of EGCG Protein Use content Elasticity Hardness Adhesion Chewability amount/% (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) 0.02 20 0.684 2674.656 0.61 0.308 −15.421 1115.973 0.05 21 0.724 2924.688 0.68 0.317 −17.873 1439.882 0.10 22 0.754 3150.487 0.76 0.348 −18.329 1805.355 0.15 23 0.741 3038.216 0.72 0.329 −19.145 1620.949 0.20 22 0.694 2817.492 0.65 0.289 −19.692 1270.971

[0077] From the data in Table 6, it can be seen that the use amount of the epigallocatechin gallate (EGCG) has little influence on the protein content of a product, but has certain influence on the texture and taste of the product, and when the use amount of the epigallocatechin gallate is 0.1%, the product has the best texture and taste.

Comparative Example 1

[0078] With reference to the method in Example 1, raw materials were prepared. 500 g of frozen basa fish slices were defrosted at low temperature, and the defrosted meat slices were directly chopped in the shape of a meat pie.

Comparative Example 2

[0079] With reference to Example 1, the difference was only that the soybeans were not additionally added. Specific operation steps were as follows.

[0080] (1) Preparation of an aquatic protein: 500 g of frozen basa fish slices were defrosted at low temperature, cut and chopped into evenly diced meats with a size of about 0.8 cm, and soaked and cleaned in 0.6% baking soda for 8 min to obtain a meat pulp. The meat pulp was treated with a centrifuge to remove free water, and then a protein pulp was obtained.

[0081] (4) Pretreatment of a protein: A complex salt was added to the obtained protein pulp for pickling and rolling for 50 min, where the added amount of NaCl was controlled to be 0.8% of the weight of a protein homogenate, and the added amount of phosphate was 0.4% of the weight of a protein homogenate. Then food-grade sodium lactate was added for adjusting the pH to 7.5 so as to form a meat paste.

[0082] (5) Forming and coloring: 1.3% of glutamine transaminase and 0.10% of epigallocatechin gallate (EGCG) were added to a paste protein obtained in the above step for uniform mixing. Next, 0.35‰ of monascus red was added for uniform stirring. Then, incubation was conducted in a water bath at 50° C. for 120 min.

[0083] (6) High-temperature qualitative treatment: A protein combined restructured meat obtained was subjected to inactivation and qualitative treatment in a high-temperature water bath at 90° C. for 10 min, and then cooling was conducted rapidly to room temperature in an ice bath.

[0084] (7) Integrated forming: A protein combined restructured meat sample obtained was directly kneaded in the shape of a meat pie.

Comparative Example 3

[0085] With reference to Example 1, the differences were only that the EGCG was omitted in step (5), and only the glutamine transaminase was added. Specific steps were as follows.

[0086] (1) Preparation of an aquatic protein: 500 g of frozen basa fish slices were defrosted at low temperature, cut and chopped into evenly diced meats with a size of about 0.8 cm, and soaked and cleaned in 0.6% baking soda for 8 min to obtain a meat pulp. The meat pulp was treated with a centrifuge to remove free water, and then a protein pulp was obtained.

[0087] (2) Preparation of a plant protein: Soybeans were crushed and sifted, and n-hexane accounting for 4 times the volume of the soybeans was added for degreasing. A degreased soybean powder was resuspended in deionized water. Next, the pH of an obtained solution was adjusted to 9.0 with sodium hydroxide, stirring was conducted at a constant temperature of 30° C. for 2 h, centrifugation was conducted to obtain a supernatant, and the pH was adjusted to 4.0 with hydrochloric acid. The above steps were repeated for 2 times. Then, centrifugation was conducted at 8,000 rpm for 15 min, and a protein precipitate was collected and washed with deionized water until the pH was neutral. Finally, freeze-drying was conducted to obtain a soybean protein isolate.

[0088] (3) Uniform mixing and stirring: The aquatic protein pulp obtained in step (1) and a soybean protein powder obtained in step (2) were mixed and stirred at a ratio of 10:1 at 4° C. for 25 min until a homogeneous state was reached.

[0089] (4) Pretreatment of a protein: A complex salt was added to a protein homogenate obtained in step (3) for pickling and rolling for 50 min, where the added amount of NaCl was controlled to be 0.8% of the weight of the protein homogenate, and the added amount of phosphate was 0.4% of the weight of the protein homogenate. Then food-grade sodium lactate was added for adjusting the pH to 7.5 so as to form a meat paste.

[0090] (5) Combined restructuring: 1.3% of glutamine transaminase and 0.35% of monascus red were added to a paste protein obtained in step (4) for uniform stirring. Then, incubation was conducted in a water bath at 50° C. for 120 min.

[0091] (6) High-temperature qualitative treatment: A protein combined restructured meat obtained in step (5) was subjected to inactivation and qualitative treatment in a high-temperature water bath at 90° C. for 10 min, and then cooling was conducted rapidly to room temperature in an ice bath.

[0092] (7) Integrated forming: A protein combined restructured meat sample obtained in step (6) was directly kneaded in the shape of a meat pie.

Comparative Example 4

[0093] With reference to Example 1, the differences were only that the protease in step (5) was omitted, and only the EGCG was added. Specific steps were as follows.

[0094] (1) Preparation of an aquatic protein: 500 g of frozen basa fish slices were defrosted at low temperature, cut and chopped into evenly diced meats with a size of about 0.8 cm, and soaked and cleaned in 0.6% baking soda for 8 min to obtain a meat pulp. The meat pulp was treated with a centrifuge to remove free water, and then a protein pulp was obtained.

[0095] (2) Preparation of a plant protein: Soybeans were crushed and sifted, and n-hexane accounting for 4 times the volume of the soybeans was added for degreasing. A degreased soybean powder was resuspended in deionized water. Next, the pH of an obtained solution was adjusted to 9.0 with sodium hydroxide, stirring was conducted at a constant temperature of 30° C. for 2 h, centrifugation was conducted to obtain a supernatant, and the pH was adjusted to 4.0 with hydrochloric acid. The above steps were repeated for 2 times. Then, centrifugation was conducted at 8,000 rpm for 15 min, and a protein precipitate was collected and washed with deionized water until the pH was neutral. Finally, freeze-drying was conducted to obtain a soybean protein isolate.

[0096] (3) Uniform mixing and stirring: The aquatic protein pulp obtained in step (1) and a soybean protein powder obtained in step (2) were mixed and stirred at a ratio of 10:1 at 4° C. for 25 min until a homogeneous state was reached.

[0097] (4) Pretreatment of a protein: A complex salt was added to a protein homogenate obtained in step (3) for pickling and rolling for 50 min, where the added amount of NaCl was controlled to be 0.8% of the weight of the protein homogenate, and the added amount of phosphate was 0.4% of the weight of the protein homogenate. Then food-grade sodium lactate was added for adjusting the pH to 7.5 so as to form a meat paste.

[0098] (5) Combined restructuring: 0.10% of epigallocatechin gallate (EGCG) and 0.35% of monascus red were added to a paste protein obtained in step (4) for uniform stirring. Then, incubation was conducted in a water bath at 50° C. for 120 min.

[0099] (6) Integrated forming: A protein combined restructured meat sample obtained in step (5) was directly kneaded in the shape of a meat pie.

[0100] Properties of products obtained in Comparative Examples 1-4 were determined. Results were as shown in Table 7.

TABLE-US-00007 TABLE 7 Comparison table of properties of samples in various comparative examples Samples with physical property data in Protein comparative content Elasticity Hardness Adhesion Chewability examples (%) (mm) (g) Cohesiveness Recoverability (J) (g .Math. mm) Example 1 22 0.754 3150.487 0.76 0.348 −18.329 1805.355 Comparative 12 0.571 2059.133 0.39 0.125 −32.837 458.548 Example 1 Comparative 15 0.613 2249.867 0.44 0.187 −29.782 606.834 Example 2 Comparative 20 0.718 2956.852 0.68 0.284 −22.846 1443.653 Example 3 Comparative 23 0.688 2657.423 0.53 0.208 −25.465 940.834 Example 4

[0101] From the results in Table 7, it is seen that the untreated aquatic protein meat (in Comparative Example 1) has low texture properties such as protein content, elasticity, hardness and cohesiveness, and poor chewability. The restructured meat (in Comparative Example 2) obtained after treatment by a protein processing technology has increased protein content, and the texture properties are also improved to a certain extent. However, the protein combined restructured meat (in Example 1) obtained after a plant protein is added has higher protein content, the texture properties are significantly improved, and the chewability is good.

[0102] Through comparison between Comparative Example 3 and Comparative Example 4, it is seen that both the EGCG and the glutamine transaminase are beneficial to the improvement of protein structures. When only the EGCG is added, the effect is poor (in Comparative Example 4). When only the glutamine transaminase is used, a certain effect is achieved (in Comparative Example 3). When the two substances are used for combination (in Example 1), properties of the restructured meat are greatly improved.

[0103] Although the present disclosure has been disclosed as preferred examples above, the preferred examples are not intended to limit the present disclosure. Various changes and modifications can be made by any person familiar with the technology without departing from the spirit and scope of the present disclosure. Therefore, the protection scope of the present disclosure shall be as defined in the claims.