Method for improving quality characteristics of salt-reduced minced fillet gel by using protamine

Abstract

The invention discloses a method for improving quality characteristics of light salt surimi gel by adding protamine, which comprises the following preparation steps: S1, air blending of surimi: blending the surimi to obtain surimi A; s2, adding salt and blending the minced fillet: mixing and blending the minced fillet A and salt to obtain minced fillet B; s3, adding protamine into the surimi, and blending: mixing the surimi B with the protamine, putting the mixture into a blending machine, and adjusting the water content of a system to obtain surimi C; s4, water bath of the minced fillet gel: heating the minced fillet C to obtain minced fillet gel D; and S5, cooling the minced fillet gel: cooling the minced fillet gel D, and standing to obtain a minced fillet gel final product. According to the minced fillet gel prepared by the invention, the protamine added under the condition of reduced salt can serve as a natural preservative of the minced fillet gel, the gel strength of the minced fillet gel is also remarkably improved, and a brand-new technical method is provided for quality characteristic regulation and control of a salt-reduced minced fillet gel product and development of a new salt-reduced minced fillet gel product.

Description

Technical Field

[0001] The invention belongs to the field of surimi processing, and in particular relates to a method for improving the quality characteristics of reduced-salt surimi gel by utilizing protamine. Technical Background

[0002] Surimi gel is concentrated myofibrillar protein extracted from chopped and cleaned fish meat. In actual production, salt and other necessary auxiliary materials must first be added to the frozen surimi, and then it must be fully mixed and initially formed by chopping or pounding. Subsequently, heating and other process methods are used to cause the surimi to gel, thereby converting it into an elastic gel-like food. Surimi gel is an important processed aquatic product with the characteristics of high protein, low fat, and smooth taste. It meets people's consumption needs for healthy nutrition and is deeply loved by consumers.

[0003] In recent years, as living standards have gradually improved, consumers have paid more and more attention to healthy eating and have gradually realized the chronic harmful effects of eating unhealthy foods. Table salt is a sodium salt. Although it is an indispensable condiment in life, excessive intake will increase the risk of cardiovascular disease and then burden organs such as the kidneys and stomach. Therefore, a low-salt diet will become a trend in the future for healthy eating among residents, and the surimi production industry must also adapt to this change. The preparation of reduced-salt surimi gel is of great significance to the future development of surimi products.

[0004] Although the sodium content of surimi products is lower than that of other myofibril processed foods, the popular surimi products are in great demand and consumed in large quantities. Researchers still need to explore salt reduction methods and strategies during the gelation process to improve the nutritional value of surimi products and make them healthier. However, improving the health of surimi should not be at the expense of quality, and the reduction in salt concentration usually damages the gel properties of surimi products. In order to solve this problem, researchers have found that the use of some exogenous additives as gel enhancers can effectively compensate for the quality deterioration of surimi caused by the reduction of salt content. At present, under the condition of salt reduction, the quality characteristics of surimi gel can be maintained by adding exogenous additives such as sugars, proteins, antioxidants, sodium salt substitutes, and protease inhibitors. On the one hand, some existing exogenous additives will affect the texture, flavor and taste of surimi. For example, sodium salt substitutes can easily induce bad flavor of surimi, and at the same time have a negative impact on the texture and microbial safety of surimi; on the other hand, the introduction of some exogenous additives will threaten human health, such as long-term and large-scale intake of sugars will increase the risk of diabetes in consumers, etc. Therefore, it is of great significance to find a green and safe new exogenous additive as a gel enhancer for the preparation of reduced-salt surimi gel. Summary of the invention

[0005] In view of the above-mentioned problems, the purpose of the present invention is to provide a method for improving the quality characteristics of reduced-salt fish paste gel. By adding a natural preservative, protamine, during the preparation of the fish paste gel, the strength of the reduced-salt fish paste gel can be improved, so as to solve the problems existing in the existing fish paste gel preparation method, that is, the use of exogenous additives to improve the quality characteristics of the fish paste gel while causing the fish paste to have bad flavor, color change, and loss of taste. This provides a new technical method for improving the edible quality of reduced-salt fish paste gel products and developing new fish paste gel products.

[0006] To achieve the above object, the present invention provides a method for improving the quality characteristics of reduced-salt surimi gel by adding protamine, comprising the following steps:

[0007] S1. air crushing: crushing the surimi to obtain surimi A;

[0008] S2, adding salt and pounding: mixing the minced fish A obtained in step S1 with salt and pounding to obtain minced fish B;

[0009] S3, adding protamine to crush: the fish paste B obtained in step S2 is mixed with protamine, put into a crushing machine, and the water content of the system is adjusted to obtain fish paste C;

[0010] S4, water bath heating: heating the surimi C obtained in step S3 to obtain surimi gel D;

[0011] S5, cooling: cooling the surimi gel D obtained in step S4, and letting it stand to obtain a surimi gel final product.

[0012] In one embodiment of the present invention, the pounding time in step S1 is 5 to 15 minutes.

[0013] In one embodiment of the present invention, the mass of the salt added in step S2 is 0.5-3% of the mass of the surimi A.

[0014] In one embodiment of the present invention, the pounding time in step S2 is 5 to 15 minutes.

[0015] In one embodiment of the present invention, the protamine in step S3 is food grade protamine.

[0016] In one embodiment of the present invention, the amount of protamine added in step S3 is 1-20% of the mass of the surimi B.

[0017] In one embodiment of the present invention, the amount of protamine added in step S3 is 6-10% of the mass of the surimi B, preferably 8%.

[0018] In one embodiment of the present invention, the pounding time in step S3 is 5 to 15 minutes.

[0019] In one embodiment of the present invention, the water content of the system is adjusted to 65-85% by directly adding ice water to the surimi.

[0020] In one embodiment of the present invention, the heating in step S4 is to place the surimi C in a water bath at 35-45° C. for 55-65 minutes, and then in a water bath at 85-95° C. for 25-35 minutes.

[0021] In one embodiment of the present invention, the cooling in step S5 is to first cool the surimi gel D in ice water for 20 to 30 minutes, then cool the surimi gel D at 0 to 4° C. for 15 to 25 minutes, and finally stand it for 8 to 14 hours to obtain a surimi gel product.

[0022] The invention also provides a surimi gel product prepared according to the method.

[0023] The present invention also provides an application of the surimi gel product in the food field.

[0024] The invention also provides an application of protamine in the field of minced meat foods.

[0025] Beneficial effects of the present invention:

[0026] (1) When preparing surimi gel, adding protamine to it helps to improve the texture of surimi gel and increase the strength of surimi gel.

[0027] (2) The addition of protamine can replace the salt added during the preparation of surimi gel, so that the prepared surimi gel still has good texture properties under salt reduction conditions. At the same time, the prepared surimi gel has higher gel strength and ability to bind water molecules.

[0028] (3) Protamine can improve the network structure of surimi gel and enhance the cross-linking of myosin heavy chain molecules (MHC), making the surface of surimi gel smooth, with smaller pore size and fewer voids. When the amount of protamine added reaches 8% or more, the prepared surimi gel has a smooth surface microstructure, a small pore size, and no obvious large cavities.

[0029] (4) Protamine can improve the unfolding of the secondary structure of proteins in surimi gel, reduce the β-fold content and increase the β-turn content, thereby enhancing the gel strength of surimi gel and enabling it to establish a tighter three-dimensional gel network.

[0030] (5) The addition of protamine significantly increases the content of acidic organic matter such as propionic acid in the fish surimi gel, which brings fat and soybean flavor to the fish surimi gel; increases the content of ethyl disulfide, which brings cabbage and roasted onion flavor to the fish surimi gel; and also increases the content of the pyrazine compound 2,3-dimethylpyrazine, which brings caramel, cocoa, and peanut butter flavors to the fish surimi gel.

[0031] (6) The surimi gel prepared by the present invention, under the condition of reduced salt, can not only act as a natural preservative for the surimi gel, but also significantly improve the gel strength of the surimi gel by adding protamine, thereby providing a new technical method for regulating the quality characteristics of reduced-salt surimi gel products and developing new products of reduced-salt surimi gel. BRIEF DESCRIPTION OF THE DRAWINGS

[0032] Figure 1 It is the relaxation three-dimensional map of the surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2.

[0033] Figure 2 Graph showing the gel strength of surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2. Different letters indicate significant differences among the groups (p<0.05).

[0034] Figure 3 It is the microstructure of the surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2 under a cold field scanning electron microscope.

[0035] Figure 4 It is the Fourier transform infrared spectrum curve of the surimi gel in Examples 1-5 and Comparative Examples 1-2.

[0036] Figure 5 Graph showing the relative content of protein secondary structures in surimi gels in Examples 1 to 5 and Comparative Examples 1 to 2. Different letters indicate significant differences among the groups (p<0.05).

[0037] Figure 6 It is the SDS-PAGE gel electrophoresis diagram of the surimi gel and the positioning standard (Marker) in Examples 1 to 5 and Comparative Examples 1 to 2. The numbers on the left represent the molecular weight corresponding to each band of the positioning standard, and the letters on the right represent the positions of different proteins.

[0038] Figure 7 It is the GC-IMS three-dimensional topographic map of the surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2.

[0039] Figure 8 It is the GC-IMS two-dimensional spectra of the surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2.

[0040] Fig. 9 It is a relative difference diagram of the surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2.

[0041] Fig.10 It is the organic fingerprint of the surimi gel in Examples 1 to 5 and Comparative Examples 1 to 2. DETAILED DESCRIPTION

[0042] The present invention will be further described below through specific implementation examples.

[0043] Source of raw materials

[0044] Protamine was purchased from Wuhan Boruiyuan Biological Co., Ltd.

[0045] Silver carp surimi was purchased from Liaoning Anjing Food Co., Ltd.

[0046] Performance Test:

[0047] 1. Texture test:

[0048] The surimi gel was taken out after standing in the refrigerator for 12 hours, and the surimi gel was equilibrated at room temperature (25°C) for 30 minutes and cut into cylinders (25 mm in diameter and 30 mm in height). Its texture characteristics were measured using the P50 probe of the TA.XT.plus texture analyzer. The speed before and after the test was 2 mm / s, the test speed was 1 mm / s, and the pressure was pressed down twice in succession, the deformation was 50%, and the trigger force was 5g.

[0049] 2. Relaxation time and relative content test of different types of water:

[0050] The water distribution and relaxation time of the samples were measured using a Niumag pulsed nuclear magnetic resonance analyzer. The fish paste gel was cut into cylindrical slices (Φ = 25 mm, h = 5 mm), and the transverse relaxation time (T2) was measured using a CPMG pause sequence. Each sample was scanned three times, and all measurements were performed at 25°C to obtain the nuclear magnetic resonance relaxation time of the sample and the relative content of different types of water. The data were reversed at the end of the test.

[0051] 3. Gel strength test:

[0052] The gel strength of surimi gel was measured using a texture analyzer spherical metal probe (P / 5S). The surimi gel was cut into a cylinder with a height of 30 mm. The speed before, during and after the test was 1 mm / s, the trigger force was 5 g, the puncture ratio was 30%, and the time was 30 s. The breaking force and breaking distance were measured, and the gel strength was calculated. The value of the gel strength is the product of the breaking force and the breaking distance (g×cm).

[0053] 4. Microstructure characterization:

[0054] The microstructure of each group of surimi gel samples was studied using a SU8010 scanning electron microscope. The samples were cut into 2-3 mm slices and freeze-dried. The freeze-dried samples were then carefully gold-plated in an argon atmosphere. The samples were observed at 1000 times magnification at an accelerating voltage of 10 kV to obtain high-resolution images.

[0055] 5. Protein secondary structure relative content test:

[0056] The surimi gel was cut into slices of about 5 mm and then sent to a freeze dryer for freeze drying. The purpose of slicing is to ensure that the freeze drying is complete. After freeze drying, the dried surimi gel sample was ground into fine powder. 1.5 mg of surimi gel freeze-dried powder was mixed and ground with 150 mg of potassium bromide powder, and then the mixed powder was pressed into transparent thin slices. The samples were analyzed using a Nicolet iS5 infrared spectrometer. The samples were measured at 400-4000 cm -1 32 scans were performed within the range, with a resolution of 4 cm -1 The relative intensities of all samples were analyzed using OMNIC 9.2 software and PeakFit 4.12 software.

[0057] 6. Electrophoresis of surimi gel:

[0058] 27mL of sodium dodecyl sulfate solution (85℃) was added to the chopped gel (3.0g) and heated at 85℃ for 1h to dissolve the total protein in the surimi gel. Subsequently, the undissolved substances were removed by centrifugation at 6000g for 20min, and the protein concentration of the supernatant was adjusted to 2mg / mL, and then fully mixed with the Loading Buffer reagent and boiled for 5min. The electrophoresis process used 12% separation gel and 5% concentration gel, and the sample volume per lane was 10μL. Electrophoresis was performed at a voltage of 80V for 30min to make the initial bands of the sample flat; electrophoresis was performed at a voltage of 120V for 60min to separate the bands. After the electrophoresis, it was stained with Coomassie Brilliant Blue R-250 for 1 day, and then destained with a decolorizing solution until the bands were clear, and photographed with a chemiluminescence imaging analysis system.

[0059] 7. Volatile organic compound test:

[0060] The volatile organic compounds of each group of samples were analyzed using a FlavourSpe flavor analyzer. The sample (3.0 g) was transferred to a headspace bottle (20 mL) with a Teflon gasket and incubated at 500 rpm and 60°C for 15 min. Subsequently, a heated syringe at a temperature of 85°C automatically injected 500 μL of the gas in the headspace bottle into the syringe in a spray-free mode. The IMS temperature was maintained at 45°C and the column temperature was set to 60°C. The flow rate and length of the IMS drift tube were 150 mL / min and 5.3 cm, respectively, and the voltage applied across the tube was 400 V / cm; the radiation source was beta radiation (tritium, 3H) and positive ion mode. The carrier gas initially flowed at a rate of 2 mL / min for 2 min. The flow rate of nitrogen was steadily increased to 15 mL / min over the subsequent 8 min time frame. Afterwards, the flow rate was further increased to 50 mL / min over a span of 5 min. During the last 15 min, the flow rate increased linearly to a maximum of 150 mL / min. Identification of volatile compounds was achieved by comparison of KI and drift time with the GAS library in GC-IMS.

[0061] Embodiment 1:

[0062] A method for improving the quality characteristics of reduced-salt surimi gel by using protamine, comprising the following steps:

[0063] S1. Air pounding of surimi: taking out the raw silver carp surimi, slow freezing it in a refrigerator at 4°C for 24 hours, and air pounding the surimi in a pounding machine for 10 minutes to obtain air pounded surimi A;

[0064] S2, pounding the surimi with salt: mixing the surimi A described in step S1 with salt, pounding the surimi with salt for 10 minutes in a pounding machine, wherein the mass of the salt added during the pounding is 1% of the mass of the surimi A, to obtain surimi B after pounding with salt;

[0065] S3, pounding the surimi with protamine: the surimi B described in step S2 is mixed with protamine, the mass of the added protamine being 2% of the mass of the surimi B, and the mixture is put into a pounding machine, the water content of the system is adjusted to 75%, and the surimi is pounded with protamine for 10 minutes in the pounding machine to obtain the surimi C with the target protamine added;

[0066] S4, water bathing of the surimi gel: the surimi C in step S3 is water bathed in 40° C. warm water for 60 min, and then water bathed in 90° C. hot water for 30 min to obtain the surimi gel D after water bathing with the target amount of protamine added;

[0067] S5. Precool the surimi gel D after the water bath in step S4 in ice water for 20 to 30 min, then cool the precooled surimi gel in a 4° C. refrigerator for 20 min, and then stand in a 4° C. refrigerator for 12 h to obtain a surimi gel final product with a target protamine addition amount (i.e., target gel strength).

[0068] Embodiment 2:

[0069] The preparation was carried out in accordance with the preparation process of Example 1, except that the protamine added in step S3 was 4% of the mass of the surimi.

[0070] Embodiment 3:

[0071] The preparation was carried out in accordance with the preparation process of Example 1, except that the protamine added in step S3 was 6% of the mass of the surimi.

[0072] Embodiment 4:

[0073] The preparation was carried out in accordance with the preparation process of Example 1, except that the protamine added in step S3 was 8% of the mass of the surimi.

[0074] Embodiment 5:

[0075] The preparation was carried out in accordance with the preparation process of Example 1, except that the protamine added in step S3 was 10% of the mass of the surimi.

[0076] Comparative Example 1:

[0077] The preparation was carried out in accordance with the preparation process of Example 1, except that the mass of the salt added in step S2 was 2% of the mass of the surimi, and protamine was not added in step S3.

[0078] Comparative Example 2:

[0079] The preparation was carried out in accordance with the preparation process of Example 1, except that protamine was not added in step S3.

[0080] Result analysis:

[0081] 1. Texture property analysis: Table 1 shows the texture property analysis of surimi gel with different protamine addition amounts. Protamine has a significant effect on the texture property of reduced-salt surimi gel. The hardness, elasticity, cohesiveness and chewiness of Examples 1, 2, 3, 4 and 5 increase with the increase of protamine addition amount, and are significantly higher than those of Comparative Examples 1 and 2. This means that the addition of protamine improves the texture property of reduced-salt surimi.

[0082] Table 1 Texture characteristics of surimi gel with different protamine addition amounts

[0083]

[0084] 2. Relaxation three-dimensional spectrum analysis: Figure 1 The relaxation 3D spectra of surimi gel with different protamine addition amounts. The peaks from left to right can be divided into T 21 (0.01~10ms), T 22 (10~200ms) and T 23 (>200ms) three categories, representing bound water, immobile water and free water. 21 , A 22 , A 23 The relative contents of bound water, non-mobile water and free water in the surimi gel are shown in Table 2. 21 The relaxation time is significantly higher than that of Comparative Example 1. 21 The relaxation time of Examples 1, 2, 3, 4, and 5 was 1.34 Å, which showed that the binding ability of the reduced-salt surimi gel to water molecules was not as good as that of the conventional salt surimi gel. 21 The peak significantly shifts to a lower relaxation time, which indicates that with the increase of protamine addition, the mobility of water molecules in the gel network gradually decreases. In addition, analysis of the relative content of different forms of water shows that the free water content of Comparative Example 2 is the highest and the bound water content is the lowest, which indicates that the ability of the gel network to capture water decreases under reduced salt conditions. 22 , A 23 The value gradually decreases, A 21 The value gradually increases, that is, the semi-free water and free water in the surimi gel are gradually converted into bound water. When the amount of protamine added reaches 8% (Example 4) or more, its semi-free water content and free water content are lower than those in Comparative Example 1, and the bound water content is higher than that in Comparative Example 1, indicating that protamine can improve the binding capacity of the gel network to water molecules under reduced salt conditions.

[0085] Table 2 NMR relaxation time of surimi gel with different amounts of protamine added and relative content of different types of water

[0086]

[0087] 3. Gel strength analysis: Figure 2The graph shows the gel strength of surimi gel with different protamine addition amounts. Under reduced salt conditions, myosin exists in the form of insoluble fibers and is difficult to completely dissolve and disperse, so the gel strength of Comparative Example 2 is significantly lower than that of Comparative Example 1. After the addition of protamine, the gel strength of surimi gel changes with the amount of protamine added. The gel strength of Examples 1, 2, 3, 4, and 5 increases significantly, which is better than Comparative Example 1. In the range of 2% to 8% protamine addition, the gel strength shows a positive correlation with the amount of protamine added. When the amount of protamine added is 8% (Example 4), the gel strength of surimi gel is the highest.

[0088] 4. Cold field scanning electron microscope observation: Figure 3 The microstructure of surimi gel under cold field scanning electron microscope with different amounts of protamine added. It can be clearly seen from the figure that there are many depressions in the gel structure shown in the electron microscope images of comparative examples 1 and 2, the surface is rough and the gaps are large, which shows that the reduction of salt concentration has an adverse effect on the cross-linking of myofibrillar protein. However, with the continuous increase of the amount of protamine added, the surface of the surimi gel gradually becomes smooth, the pore size gradually decreases, and the gaps become fewer and fewer. When the amount of protamine added reaches 8% or more, the resulting gel has a smooth surface microstructure, a small pore size, and no obvious large cavities.

[0089] 5. Protein secondary structure analysis: Figure 4 The Fourier transform infrared spectral curves of the surimi gel with different protamine addition amounts are shown in Figure 2. The infrared spectral curves of all embodiments and comparative examples have absorption peaks at similar positions, but with slight deviations in specific positions and sizes, indicating that changes in salt content and protamine addition amount affect the protein structure, but no new functional groups are formed.

[0090] Figure 5 β-folding (1600-1640cm) of surimi gel with different protamine addition amounts -1 ), irregular curl (1640-1650cm -1 ), α-helix (1650-1660cm -1 ) and β-turn (1660-1700cm -1) Relative content diagram of four protein secondary structures. It can be observed that the α-helix content of Comparative Example 2 is significantly higher than that of Comparative Example 1, which proves that the decrease in salt concentration has an adverse effect on the unfolding of the myosin secondary structure. With the addition of protamine, the content of each secondary structure has changed significantly. Compared with Comparative Example 2, the α-helix content of each embodiment decreased significantly, and there was no significant difference from Comparative Example 1. This shows that protamine makes up for the defect of insufficient unfolding of the myosin secondary structure caused by the reduction in salt content, and the gel formation situation improves. In addition, although the addition of protamine slightly decreases the β-fold content, the β-turn content is significantly increased, which may lead to the enhancement of gel strength and the establishment of a tighter three-dimensional gel network, which is consistent with the low-field nuclear magnetic resonance ( Figure 1 , Table 2), gel strength ( Figure 2 ) are consistent with the results described.

[0091] 6. Analysis of protein cross-linking degree: Figure 6 The SDS-PAGE gel electrophoresis diagram of surimi gel and positioning standard (Marker) with different amounts of protamine added. The intensity bands of all surimi samples in the figure are clearly visible, including myosin heavy chain (MHC), actin (Actin), tropomyosin (TM) and troponin-T (TN-T), which is a typical pattern of fish protein. The MHC and actin bands are obviously more intense than other bands, and they are the two most important bands in the surimi gel. According to the spectrum results, with the changes in salt concentration and protamine concentration, the structure and quantity of myosin heavy chain have undergone major changes. The stronger the MHC band intensity, the less non-disulfide covalent bonds and molecular cross-links formed by myofibrillar proteins. As can be seen from the figure, compared with Comparative Example 1, the myosin heavy chain (MHC) band of Comparative Example 2 becomes thicker, indicating that the reduction in salt concentration leads to a reduction in cross-linking between myosins. As the concentration of protamine increases, the MHC bands gradually become lighter and thinner. The decrease in band intensity means that the MHC molecules are more cross-linked, and they strengthen the gel structure by forming non-disulfide covalent bonds.

[0092] 7. Determination of flavor substances: GC-IMS can detect and qualitatively characterize the volatile organic compounds contained in the experimental samples for analysis of the flavor substances in the samples. Figure 7 It is a three-dimensional topographic map of volatile organic compounds. The 3D map shows the distribution of all volatile organic compounds in different groups and can reflect the peak position and peak intensity of each compound in the sample. Similar ion peak distributions indicate that the types of substances in each sample are similar, but peak signals of different intensities show that the concentrations of similar compounds in each group are different. Figure 8A two-dimensional topographic map of VOCs, used to preliminarily determine the differences in VOCs. Each point to the right of the ion peak represents a VOC found in the sample. The concentration of the substance is represented by color (red: high concentration, white: low concentration). Fig. 9 This is a difference comparison chart. Blue means that the volatile compounds are lower than the control group, and red means the opposite. Fig.10 The fingerprint spectrum used to accurately evaluate the changes in volatile organic compounds is shown. The same column in the fingerprint spectrum represents the same ingredient, and the darker the color, the higher the concentration. As can be seen from the figure, no odor is generated after the addition of protamine. As the amount of addition increases, the concentration of each volatile organic compound changes, which shows that the addition of protamine stimulates the expression of the flavor of lightly salted fish paste gel.

[0093] According to the instrument database, all signals in the spectra were identified, and a total of 34 volatile components were identified in 7 samples, covering 11 major categories of substances such as esters, acids, ketones, and alcohols. The relative contents are shown in Table 3. Most of the identified volatile organic compounds showed oil aroma and fruit aroma. Compared with Examples 1-5, the content of some flavor components in Comparative Examples 1 and 2 decreased, which may be caused by the reduction in salt concentration. With the addition of protamine, the content of acidic organic matter such as propionic acid increased significantly, bringing fat and soybean flavors to the fish paste gel; the content of ethyl disulfide increased significantly, bringing cabbage and roasted onion flavors; the content of pyrazine compound 2,3-dimethylpyrazine increased significantly, bringing caramel, cocoa, and peanut butter flavors.

[0094] Table 3 Relative contents of volatile flavor substances in surimi gel with different amounts of protamine added

[0095]

[0096]

[0097]

[0098] In summary, protamine is a useful additive for the development of light-salt surimi gel. It can not only serve as a natural preservative and quality improver for surimi gel, but also enhance the flavor of surimi gel in a light-salt environment. It can effectively make up for the quality deterioration of surimi gel in a light-salt environment, and provide a new method for the development of new light-salt surimi products.

[0099] The above description is only a preferred specific implementation manner of the present invention, but the protection scope of the present invention is not limited thereto. Any technician familiar with the technical field can make equivalent replacements or changes according to the technical scheme and inventive concept of the present invention within the technical scope disclosed by the present invention, which should be covered by the protection scope of the present invention.

Claims

1. A method for improving the quality characteristics of reduced-salt surimi gel using protamine, characterized in that: The steps include: S1. air crushing: crushing the surimi to obtain surimi A; S2, adding salt and pounding: mixing the minced fish A obtained in step S1 with salt and pounding to obtain minced fish B; S3, adding protamine to crush: the fish paste B obtained in step S2 is mixed with protamine, put into a crushing machine, and the water content of the system is adjusted to obtain fish paste C; S4, water bath heating: heating the surimi C obtained in step S3 to obtain surimi gel D; S5, cooling: cooling the surimi gel D obtained in step S4, and letting it stand to obtain a surimi gel final product.

2. The method according to claim 1, characterized in that The pounding time in step S1 is 5 to 15 minutes.

3. The method according to claim 1, characterized in that: The mass of the salt added in step S2 is 0.5-3% of the mass of the surimi A, and the pounding time is 5-15 minutes.

4. The method according to claim 1, characterized in that: The amount of protamine added in step S3 is 1-20% of the mass of the surimi B.

5. The method according to claim 1, characterized in that The pounding time in step S3 is 5 to 15 minutes, and the water content of the system is adjusted to 65 to 85% by directly adding ice water to the fish paste.

6. The method according to claim 1, characterized in that The heating in step S4 is to place the surimi C in a water bath at 35-45° C. for 55-65 minutes, and then in a water bath at 85-95° C. for 25-35 minutes.

7. The method according to claim 1, characterized in that The cooling in step S5 is to first cool the surimi gel D in ice water for 20 to 30 minutes, then cool the surimi gel D at 0 to 4° C. for 15 to 25 minutes, and finally let it stand for 8 to 14 hours to obtain a surimi gel product.

8. The surimi gel product prepared according to the method according to any one of claims 1 to 7.

9. Use of the surimi gel product according to claim 8 in the food field.

10. Application of protamine in minced meat food.

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