Method for treating goose meat quality by regulating pulsed electric field through protonation signal amplification

Abstract

The invention discloses a method for treating goose meat quality by regulating and controlling a pulsed electric field through protonation signal amplification, which is characterized by comprising the following steps: (1) cutting fresh goose meat into blocks, and soaking the blocks in a lactic acid solution with the mass concentration of 30% for 45 minutes; and (2) performing high-voltage pulse electric field treatment on the goose meat obtained in the step (1) for 1 minute under the conditions that the intensity is 15kV / cm, the pulse number is 9, the frequency is 60-100Hz, and the treatment time is 1 minute, so that the quality regulation and control of the goose meat are completed, and the method has the advantages that a protonation signal change program in the pulse electric field treatment process is simple, convenient, economical and feasible, and the improvement of various qualities such as flavor, tenderness, water and oil retention and the like of the goose meat product is synchronously realized.

Description

Technical Field

[0001] The invention belongs to the technical field of meat product processing, and in particular relates to a method for processing goose meat quality by amplifying protonation signals and regulating pulse electric fields. Background Art

[0002] China is one of the world's largest producers of goose meat. Goose meat has great market potential due to its rich nutritional value, low cholesterol content and green and healthy attributes. However, there are great limitations in the deep processing of goose meat products, mainly because goose meat products have the disadvantages of coarse goose meat myofibrils, bland flavor and difficult to control edible quality during processing. The physical, chemical and sensory quality characteristics of livestock and poultry meat directly affect its processing adaptability and consumers' willingness to buy, so it is very important to study its processing technology and the development of quality control methods.

[0003] High-voltage pulsed electric field technology (PEF) has the characteristics of short processing time and low energy consumption. It can retain the original flavor of food after processing. Based on its electroporation effect, it is often used for cold sterilization of livestock and poultry meat and aquatic products to achieve sterilization and preservation while maintaining the flavor and nutritional properties unchanged. By applying high-voltage pulses to food instantly, the cell membrane structure is damaged or disintegrated, resulting in changes in ion permeability, thereby generating transmembrane potential to achieve permeabilization. When applying an external high-voltage pulsed electric field for sterilization, the water distribution in the myofibrils is changed to increase the space between fibers to improve water holding capacity, or the microstructure of the muscle fibers is changed by a strong electric field to improve the tenderness of the meat. Although high-voltage pulsed electric fields can achieve efficient sterilization at low temperatures, their tenderizing effects on different meats vary. According to the latest research, PEF may indirectly affect the pH value and color of meat by destroying animal cell membranes and generating heat during the processing process. PEF technology can increase the pickling rate, but excessive processing is not conducive to its texture and taste. For fish products, due to their short sarcomeres and small diameters, and tightly arranged myofibrils, PEF treatment may cause excessive dissolution of protein in fish, reducing its juiciness and tenderness during cooking. In addition, PEF technology may cause changes in the interactions within and between protein molecules through the action of the electric field, hiding some flavor precursors, which is not conducive to the original flavor perception and characteristic odor formation of meat products. The existing application of pulsed electric fields for sterilization of meat products still mainly relies on the optimization of process parameters such as electric field voltage, number of pulses, total energy input, processing time, and pulse width to regulate other physical and chemical quality parameters of meat products. Therefore, under the premise of applying PEF technology to ensure the safety of food microorganisms, other new quality control technologies and combination strategies should be developed to optimize parameters for different types of meat to achieve a synergistic regulation effect of safety quality and sensory quality. So far, there has been no report in public literature or patents on the use of protonated signal amplification pulsed electric field technology to regulate the quality of goose meat. Summary of the invention

[0004] The technical problem to be solved by the present invention is to provide a method for processing goose meat quality by regulating pulse electric field through protonation signal amplification, which can significantly improve the flavor and texture.

[0005] The technical solution adopted by the present invention to solve the above technical problems is: a method for treating goose meat quality by amplifying protonation signals and regulating pulse electric fields, comprising the following steps:

[0006] (1) Cut fresh goose meat into pieces and immerse them in a lactic acid solution;

[0007] (2) The goose meat obtained in step (1) is subjected to high-voltage pulse electric field treatment to complete the quality control of the goose meat.

[0008] Preferably, the lactic acid solution in step (1) is a lactic acid solution with a mass concentration of 30%, and the immersion time is 45 minutes.

[0009] Preferably, the mass ratio of the goose meat to the lactic acid solution in step (1) is 1:3.

[0010] Preferably, in step (2), the high-voltage pulse electric field strength is 15 kV / cm, the number of pulses is 9, the frequency is 60-100 Hz, and the treatment time is 1 min.

[0011] Compared with the prior art, the advantages of the present invention are: a method for processing goose meat quality by regulating pulse electric field through protonation signal amplification, the method adopts lactic acid protonation pretreatment on goose meat, and induces changes in its interaction with flavor compounds by changing the structure of goose myofibrillar protein, so as to amplify the regulating effect of pulse electric field technology on goose meat quality, further combine with pulse electric field technology, and simultaneously regulate the conductivity of pulse electric field technology, so as to achieve improvement in multiple qualities of goose meat products such as flavor, tenderness, water and oil retention, enhance the release of goose meat flavor, strengthen the generation of characteristic goose meat flavor, significantly improve the edible quality of goose meat, and finally obtain goose meat with good flavor and texture, which provides new ideas for livestock and poultry meat processing technology and has broad application prospects. BRIEF DESCRIPTION OF THE DRAWINGS

[0012] Figure 1 The effect of protonation reaction on the solubility of goose myofibrillar protein;

[0013] Figure 2 The effect of protonation reaction on the water holding capacity of goose myofibrillar protein;

[0014] Figure 3 The effect of protonation reaction on the oil retention of goose myofibrillar protein;

[0015] Figure 4 The effect of protonation reaction on the cooking loss of goose myofibrillar protein;

[0016] Figure 5 The effect of protonation reaction on the primary structure of goose myofibrillar protein;

[0017] Figure 6 The effect of protonation reaction on the circular dichroism spectrum of goose myofibrillar protein;

[0018] Figure 7 The effect of protonation reaction on the secondary structure content of goose myofibrillar protein;

[0019] Figure 8 The effect of protonation reaction on the intrinsic fluorescence of goose myofibrillar protein;

[0020] Fig. 9 The effect of protonation reaction on the surface hydrophobicity of goose myofibrillar protein.

[0021] Fig.10 The effect of protonation / deprotonation combined with high voltage pulsed electric field technology on the flavor of goose meat;

[0022] Fig.11 To study the effect of protonation / deprotonation combined with high voltage pulsed electric field technology on the water holding capacity of goose meat;

[0023] Fig.12 To study the effect of protonation / deprotonation combined with high voltage pulsed electric field technology on the elasticity of goose meat;

[0024] Fig.13 The effect of protonation / deprotonation combined with high voltage pulsed electric field technology on the tenderness of goose meat;

[0025] Fig.14 The effect of protonation / deprotonation combined with high-voltage pulsed electric field technology on the microstructure of goose meat. DETAILED DESCRIPTION

[0026] The present invention is further described in detail below with reference to the accompanying drawings.

[0027] 1. Experimental determination method

[0028] 1. Extraction of goose myofibrillar protein

[0029] Remove the fascia from the fresh goose breast and cut into 2cm 3The meat pieces were washed and drained and minced in a meat grinder. Add 4 times the mass of Tris-EDTA extract to the minced meat, homogenize in an ice bath, centrifuge at 8000g for 20min, remove the supernatant, add 4 times the mass of SSS reagent (0.1mol / LKCl, 0.02mol / LK2HPO4 / KH2PO4, 2mmol / LMgCl2, 1mmol / L EGTA, pH7.0), homogenize, centrifuge at 8000g for 10min, and remove the supernatant. Repeat the experimental operation 3 times. Take the precipitate and add 4 times the mass of SSS reagent containing 1% TritonX-100, homogenize, and centrifuge at 8000g for 10min. Take the precipitate and add 4 times the mass of SSS, homogenize and centrifuge to remove the supernatant, add 0.1mol / LKCl, mix and homogenize, filter with gauze, and centrifuge the filtrate at 8000g for 10min. Take the precipitate, add 0.1 mol / L NaCl, mix well, and centrifuge at 8000g for 10 min. Remove the supernatant to obtain the purified myofibrillar protein.

[0030] 2. Determination of physicochemical properties of goose myofibrillar protein

[0031] (1) Centrifuge the protein sample at 1000 g for 10 min at 4°C, and use a biuret protein content detection kit to determine the protein concentration C0 before centrifugation and the protein concentration C1 of the supernatant after centrifugation. Solubility (%) = C1 / C0×100%.

[0032] (2) Centrifuge goose myofibrillar protein with an initial mass of m0 at 8000 g for 15 min at 4°C, remove the supernatant and record the weight of the precipitate m1. Water holding capacity (%) = m1 / m0×100%.

[0033] (3) Take 0.5 g of goose myofibrillar protein and mix it with 6 mL of soybean oil, let it stand for 30 minutes, centrifuge it at room temperature at 8000 g for 15 minutes, remove the supernatant and record the weight of the precipitate m2. Oil retention (g / 100 g) = (m2-0.5) / 0.5×100%.

[0034] (4) Place goose myofibrillar protein in a beaker, cover with plastic wrap, and heat in a water bath. Record the mass of the empty beaker m0, the total mass of the beaker and sample before heating m1, and the total mass of the beaker and sample after heating m2. Cooking loss (%) = (m1-m2) / (m1-m0)×100%.

[0035] 3. Determination of the structure and function of goose myofibrillar protein

[0036] (1) Determination of the primary structure of goose myofibrillar protein: The concentration of the protein sample solution was adjusted to 1 mg / mL, 5 μL of loading buffer was added to 20 μL of the sample, and the mixture was placed in a metal bath at 100°C for 8 min. The samples were separated using 12% separation gel and 5% concentration gel, and electrophoresed at 80 V for 30 min and 120 V for 90 min. After the electrophoresis, the gel was stained, and after destaining, the gel was scanned using an optical density scanner, the Gel Doc XR+ imaging system, and the image scanning software. The protein molecular weight of each band was identified by comparison with a broad-spectrum color protein marker.

[0037] (2) Determination of the secondary structure of goose myofibrillar protein: The concentration of the protein sample solution was adjusted to 0.5 mg / mL, and the CD spectrum was scanned at 190-260 nm. The scanning rate, response, and bandwidth were 50 nm / min, 0.25 s, and 1.0 nm, respectively. The average of three scans was taken to calculate the content of each secondary structure, including α-helix, β-sheet, β-turn, and random coil.

[0038] (3) Determination of intrinsic fluorescence of goose myofibrillar protein: The concentration of the protein sample solution was adjusted to 1 mg / mL, and its intrinsic fluorescence was measured using an ELISA reader. The protein solution was excited at 290 nm, and the excitation and emission spectra at 285-315 nm were recorded.

[0039] (4) Determination of the surface hydrophobicity of goose myofibrillar protein: The concentration of the protein sample solution was adjusted to 0.05, 0.1, 0.15, 0.2, and 0.25 mg / mL, and 10 μL of 8 mmol / LANS was added to 2 mL of the protein solution and stirred for 1 min. Incubate at 37°C in the dark for 10 min. The fluorescence intensity was measured using an ELISA reader, with the excitation and emission wavelengths being 370 and 480 nm, respectively. The initial slope of the fluorescence intensity versus the protein solution concentration was calculated to obtain the surface hydrophobicity.

[0040] 4. Determination of volatile flavor compounds in the headspace of goose meat

[0041] The fascia fat was removed from fresh goose meat, and 5 g of the sample was added to a headspace extraction bottle. The sample was extracted at 50 °C for 60 min using a 75 μm Carboxen / polydimethylsiloxane solid phase microextraction head. Volatile compounds were separated using a 30 m × 250 μm × 0.25 μm VLCOL capillary column, and helium was used as a carrier gas. The sample was kept at 35 °C for 3 min, heated to 140 °C at 4 °C / min, kept for 1 min, and heated to 250 °C at 10 °C / min, kept for 3 min. The mass spectrum was obtained in EI mode (0.9 kV) and scanned in the range of m / z 45-600. The detector temperature was set to 250 °C. Volatile compounds were identified based on retention time and mass spectra in the NIST14 database.

[0042] 5. Determination of water holding capacity of goose meat

[0043] The initial mass of goose meat was measured by an analytical balance and recorded as m0. The goose meat was wrapped with neutral filter paper and centrifuged at 9000g for 20 minutes at room temperature. After removing the supernatant and filter paper, the weight of the goose meat was recorded as m1. Water holding capacity (%) = m1 / m0×100%.

[0044] 6. Determination of elasticity and tenderness of goose meat

[0045] (1) The elasticity and hardness of goose meat were measured using a TA.XT PlusC physical property analyzer. The P / 50 probe was selected, and the pre-test speed was set to 5 mm / s, the test speed to 1 mm / s, the post-test speed to 5 mm / s, the pressure strain to 50%, and the trigger force to 5.0 g. The elasticity of the goose meat was recorded.

[0046] (2) The shear force of goose meat was measured using a TA.XT PlusC physical property analyzer. The blade was lowered perpendicular to the direction of the goose muscle fibers. The pre-test speed was set to 2 mm / s, the test speed was set to 2 mm / s, and the post-test speed was set to 15 mm / s. The shear force of goose meat was recorded.

[0047] 7. Determination of goose meat microstructure

[0048] Use a fine scalpel to cut the goose meat into 1mm pieces along the muscle fiber direction. 3 The squares were immediately placed in 2.5% glutaraldehyde for electron microscopy at 4°C for 48 hours. After drying with filter paper, they were washed three times with 0.1M phosphate buffer solution (pH 7.0) at room temperature for 15 minutes each time. They were fixed in 1% osmium tetroxide for 2 hours at room temperature and then washed with 0.1M phosphate buffer solution. They were dehydrated with 30%, 50%, 70%, 80%, 90%, and 100% ethanol for 10 minutes each time. The samples were soaked in propylene oxide and embedded in epoxy resin. After polymerization, sections were prepared with an ultrathin slicer. After staining with uranyl acetate and lead citrate, the microstructure of goose meat was observed under a transmission electron microscope. 2. Specific embodiments

[0050] Example group: Protonation combined with high voltage pulse electric field treatment of goose meat

[0051] Treatment 1A: Fresh goose meat was quickly removed of fascia and fat at 4°C and cut into 2.5 cm squares along the muscle fiber direction. 3 The blocks were immediately placed in a 30 wt % lactic acid solution (with an ionic strength of about 6.76 × 10 -3 S / m 2) for 45 minutes, with the solid-liquid mass ratio of goose meat to protonated solution (lactic acid solution) being 1:3; the goose meat was placed in a high-voltage pulsed electric field with an electric field intensity of 15 kV / cm, 9 pulses, a frequency of 50-100 Hz, and a treatment time of 1 minute, recorded as the LA+PEF 1min group.

[0052] Treatment 1B: Same as treatment 1A, except that the high voltage pulse electric field treatment time was 10 min, denoted as LA+PEF10min group.

[0053] Control 1C: Same as treatment 1A, except that no high voltage pulse electric field treatment was performed, denoted as LA group.

[0054] Control 1D: Fresh goose meat was not processed and was recorded as the CG group.

[0055] Control 1E: fresh goose meat was placed in a high voltage pulsed electric field with an electric field strength of 15 kV / cm, a pulse number of 9, a frequency of 50-100 Hz, and a treatment time of 1 min, recorded as the CG+PEF 1 min group.

[0056] Control 1F: fresh goose meat was placed in a high-voltage pulsed electric field with an electric field strength of 15 kV / cm, 9 pulses, a frequency of 50-100 Hz, and a treatment time of 10 min, recorded as the CG+PEF 10 min group.

[0057] Comparative Example 1: Deprotonation combined with high voltage pulse electric field treatment of goose meat

[0058] Treatment 2A: Fresh goose meat was quickly removed of fascia and fat at 4°C and cut into 2.5 cm pieces along the muscle fiber direction. 3 The blocks were immediately placed in a 30 wt % sodium lactate solution (with an ionic strength of approximately 3.66 × 10 -1 S / m 2 ) for 45 minutes, the solid-liquid mass ratio of goose meat to deprotonated solution (sodium lactate solution) was 1:3; the goose meat was placed in a high-voltage pulse electric field with an electric field intensity of 15 kV / cm, 9 pulses, a frequency of 50-100 Hz, and a treatment time of 1 minute, recorded as the SL+PEF1min group.

[0059] Treatment 2B: Same as treatment 2A, except that the high voltage pulse electric field treatment time was 10 min, denoted as SL+PEF10min group.

[0060] Control 2C: Same as treatment 2A, except that no high voltage pulse electric field treatment was performed, denoted as SL group.

[0061] Comparative Example Group 2: Protonation Treatment of Goose Meat

[0062] Treatment group 3A: The fat and fascia of fresh goose meat were removed to extract goose myofibrillar protein, and the protein sample solution was prepared with phosphate buffer (pH 7). The pH value of the protein solution was adjusted to pH 7 and stored at 4°C for 24 h, which was recorded as the pH 7+24h group.

[0063] Control group 3B: Same as treatment 3A, except that the pH value of the protein solution was adjusted to pH 5 using a phosphate buffer with a lactic acid concentration of 56.2 mM, recorded as pH 5+24h group.

[0064] Control group 3C: Same as treatment 3A, except that the pH value of the protein solution was adjusted to pH 3 using a phosphate buffer with a lactic acid concentration of 5.75 M, recorded as pH 3+24h group.

[0065] Control group 3D: Same as treatment 3A, except that the cells were stored at 4°C for 48 h, referred to as pH 7+48h group.

[0066] Control group 3E: Same as treatment 3B, except that the cells were stored at 4°C for 48 h, referred to as pH 5+48h group.

[0067] Control group 3F: Same as treatment 3C, except that the cells were stored at 4°C for 48 h, referred to as pH 3+48h group.

[0068] 2. Experimental Results Analysis

[0069] 1. Effect of protonation reaction on the physicochemical properties of goose myofibrillar protein

[0070] Depend on Figure 1 It can be seen that the solubility of goose myofibrillar protein changed significantly after protonation treatment (P<0.05). The solubility of the protein in the pH 7+24h group was 3.6 times that of the pH 5+24h group. When the pH dropped to 3, the solubility of goose myofibrillar protein increased by 1.75 times compared with that at pH 5. The solubility of goose myofibrillar protein stored for 48h showed the same trend as that stored for 24h. This indicates that the hydrophobic groups inside the protein molecules changed after protonation treatment. When the pH value of the protein was near the isoelectric point, the electrostatic repulsion was lost, and then aggregation occurred to form precipitation. Therefore, the solubility of the pH 5 group was the lowest. With the increase of protonation intensity, the charge distribution of the amino acid side chains changed again, and the electrostatic repulsion between goose myofibrillar protein molecules increased, becoming relatively dispersed from the precipitation state, so the solubility of the pH 3 group was partially restored. It shows that the protonation treatment changes the spatial structure of goose myofibrillar protein, which may be accompanied by the rupture of disulfide bonds between subunits.

[0071] like Figure 2As shown in the figure, protonation caused the water holding capacity of goose myofibrillar protein to decrease significantly. The water holding capacity of the pH 7+24h group was 1.3 times that of the pH 5+24h group. As the protonation intensity increased, the water holding capacity decreased instead, reaching 73.1% in the pH 3+24h group. The water holding capacity of the pH 5+48h group was the lowest, only 53.1%. The water holding capacity of goose myofibrillar protein in the 48h storage group was lower than that in the 24h storage group, but the increase and decrease trends were consistent. The oil holding capacity of goose myofibrillar protein also showed the same trend as the water holding capacity ( Figure 3 ), the oil holding capacity of the pH 7+24h group was about 30% higher than that of the pH 5+24h group, and the pH 3+24h group was 13% higher than that of the pH 5+24h group, indicating that the simple change of protonation intensity has a negative impact on the oil holding capacity, and the effect does not change linearly with the protonation signal. At the same time, the water holding capacity of goose myofibrillar protein directly affects the moisture content and sensory attributes of meat products, while the oil holding capacity is related to its ability to absorb fat, which helps to enhance the taste and flavor. These characteristics work synergistically to affect the overall quality of meat products, indicating that different protonation intensity treatments can significantly regulate meat quality parameters.

[0072] The cooking loss of goose myofibrillar proteins is directly related to the reduction of moisture content of the meat, which leads to changes in its color and aroma. Figure 4 As shown in the figure, the cooking loss increased significantly after protonation treatment, and the cooking loss of goose myofibrillar protein in the pH 5+48h group was the highest, reaching 61.5%. When the intensity of protonation treatment was further enhanced, the pH value of goose myofibrillar protein was far away from the isoelectric point, and the cooking loss was significantly reduced. The cooking loss of goose myofibrillar protein in the pH 3 group was less than that in the pH 5 group. This shows that the protonation treatment caused the denaturation of goose myofibrillar protein, the ionic bonds and hydrogen bonds in the protein molecules were destroyed, resulting in the exposure of hydrophobic groups, and the denaturation process was accompanied by a decrease in protein solubility, thereby increasing the cooking loss.

[0073] 2. Effect of protonation reaction on the structure of goose meat myofibrillar protein

[0074] like Figure 5As shown in the figure, the intensity of the actin and myosin heavy chain bands weakened after protonation treatment, indicating that the relative molecular weight of goose myofibrillar protein changed and the protein was partially hydrolyzed. This shows that protonation treatment strengthens the oxidation of myosin heavy chain, forming disulfide bonds and carbonyl groups, leading to protein degradation, so that the solubility is reduced, and the rearrangement of the structure will affect the functional properties of goose myofibrillar protein. During the processing and storage of meat products, structural changes such as degradation and aggregation of goose myofibrillar protein directly affect the properties of meat flavor, tenderness and storage stability. Protein degradation leads to relaxation and denaturation of muscle fiber structure, affecting the texture of meat. Protein aggregation affects the structure and stability of myofibrils and affects the tenderness of meat. In addition, the structural changes of goose myofibrillar protein will affect the content of various amino acids and peptides in meat products and change their flavor characteristics.

[0075] like Figure 6 As shown in Figure 2, the goose myofibrillar protein in the pH 7 group has a maximum peak at 192nm, followed by two negative characteristic shoulder peaks, indicating the presence of an α-helical structure. After the protonation reaction, the position of the maximum peak of the goose myofibrillar protein changes, and the α-helical content decreases, which is consistent with the secondary structure fitting data obtained by computer ( Figure 7 ) results were consistent. After the protonation intensity increased, the α-helix content in the pH 3+24h group decreased by 9.1% compared with the pH 7+24h group, the β-fold content decreased insignificantly, and the β-turn and random coil contents increased by 6.3% and 3.4%, respectively. This indicates that the protonation reaction causes the hydrophobic center in the protein molecule to be exposed, resulting in the reduction and breakage of the intramolecular hydrogen bonds. The reduction of α-helix is ​​related to protein aggregation, and the β-turn is often located on the surface of the protein, which is a relatively stable structure. This indicates that with the increase of protonation intensity, the structure of goose myofibrillar protein may become more compact, forming a protein matrix with a stable and compact structure.

[0076] like Figure 8 As shown in the figure, the strongest emission peak of goose myofibrillar protein is at 286nm. The wavelength of the maximum fluorescence emission peak does not change after the protonation reaction, but the fluorescence intensity decreases significantly, indicating that the aromatic amino acid tryptophan originally embedded in the protein structure is exposed to the polar microenvironment after the protonation reaction, causing the protein to unfold and increase its hydrophobicity. At the same time, the electrostatic interaction between goose myofibrillar protein molecules is enhanced, resulting in the aggregation of protein molecules. The initially exposed tryptophan residues are wrapped in aggregates, thereby reducing the generation of fluorescence. In addition, the increase in solvent polarity may affect the stability of the tryptophan chromophore embedded in the protein molecule. It shows that protonation causes changes in the tertiary structure of the protein, thereby affecting a series of properties of meat products, including tenderness, flavor, and suitability for processing operations.

[0077] 3. Effect of protonation reaction on the surface hydrophobicity of goose myofibrillar protein

[0078] like Fig. 9 As shown in the figure, the surface hydrophobicity of goose myofibrillar protein increased significantly after protonation treatment. The surface hydrophobicity of the pH 3+24h group was 11.7 times that of the pH 7+24h group. As the treatment time increased, the surface hydrophobicity of the pH 3+48h group was 23.2 times that of the pH 7+48h group. This indicates that the rearrangement of the charge distribution of amino acid residues caused by protonation significantly affects the surface hydrophobicity of the protein, and the surface hydrophobicity can reflect the changes in protein structure. At the same time, the extension of the protonation treatment time further increases the surface hydrophobicity of goose myofibrillar protein. This indicates that protonation causes protein denaturation, the internal hydrophobic groups are exposed, and the hydrophilic interaction is converted into hydrophobic interaction. At the same time, the protein is partially oxidized during the protonation process, resulting in an increase in surface hydrophobicity. As the protonation intensity increases, the increase in hydrophobic interactions causes the protein structure to shrink, forming a denser microstructure, which not only affects the adsorption kinetics of the protein, but also enhances the hardness and palatability of the meat due to the formation of a cohesive structure.

[0079] Different background pH conditions correspond to different protonation intensities. The lower the background pH, the higher the free proton concentration, the protonation signal generated during the electric field, and the polarization level within the protein molecule. Figure 1-Figure 9 The results showed that although the change of protonation signal level alone under non-electric field conditions significantly affected the ultrastructure of myofibrillar protein, it could not improve the quality of goose meat. On the contrary, the protonation of amino acid residues caused conformational changes such as protein aggregation and denaturation, which had a significant negative impact on important quality characteristics such as meat water and oil retention, cooking loss, etc.

[0080] 4. Effect of protonation combined with high-voltage pulsed electric field technology on the flavor of goose meat

[0081] Depend on Fig.10It can be seen that goose meat contains volatile flavor compounds such as aldehydes, alcohols, ketones, acids, and esters. After high-voltage pulsed electric field treatment, the relative abundance of various flavor substances increased significantly. Most aldehyde substances are produced by fat oxidation, with rich types and high content. Due to their low threshold, they are important flavoring substances in goose meat, which can give goose meat fruity and fat aromas. The relative abundance of aldehyde substances in the CG+PEF 1min group was 1.16 times that of the CG group, and the CG+PEF 10min group was 2.29 times that of the CG group. The relative abundance of aldehyde substances in the LA+PEF 1min group pretreated with protonation was 10.13 times that of the CG+PEF 1min group, and the relative abundance of aldehyde substances in the LA+PEF 10min group was 5.93 times that of the CG+PEF 10min group. The abundance of aldehyde substances in the SL+PEF 1min group pretreated with deprotonation was only 27.21% of that in the LA+PEF 1min group. The relative abundance of alcohol substances in the CG+PEF 1min group was 1.59 times that of the CG group, and the CG+PEF 10min group was 1.67 times that of the CG group. After the protonation reaction, the high-voltage pulsed electric field treatment was given. The relative abundance of typical aromatic alcohols such as 1-octen-3-ol was 4.81 times that of the unprotonated reaction group, giving the goose meat characteristic flavors such as cooked mushroom and fruity flavors. At the same time, the caprylic acid content increased significantly, adding aroma to the goose meat. In addition, after the protonation treatment, alcohol substances combined with lactic acid, and an esterification reaction occurred to generate ester substances that gave the goose meat a pineapple aroma. Therefore, the protonation treatment can enhance the regulation effect of pulsed electric field technology on the flavor of goose meat, and a large amount of flavor substances are released.

[0082] 5. Effect of protonation combined with high voltage pulse electric field technology on water holding capacity of goose meat

[0083] Depend on Fig.11 It can be seen that after high-voltage pulsed electric field treatment, the water holding capacity of goose meat was significantly improved, and the water holding capacity of the CG+PEF 1min group increased by 7.57% compared with the CG group. The water holding capacity of goose meat in the CG+PEF 1min group was higher than that in the CG+PEF 10min group, indicating that the water holding capacity of goose meat was the best when the high-voltage pulsed electric field treatment was performed for 1 minute. After the protonation reaction, the high-voltage pulsed electric field treatment was performed for another 1 minute, at which time the water holding capacity of goose meat was the best, reaching 86.52%. The water holding capacity of goose meat in the deprotonation pretreatment group was worse than that in the protonation pretreatment group, indicating that the protonation pretreatment combined with the high-voltage pulsed electric field had a better effect on improving the water holding capacity of goose meat, thus confirming that changing the protonation signal during the high-voltage pulsed electric field treatment is a response factor for regulating water holding capacity.

[0084] 6. Effect of protonation combined with high-voltage pulsed electric field technology on the elasticity and tenderness of goose meat

[0085] Fig.12 The effect of protonation combined with pulsed electric field technology on the elasticity of goose meat. Fig.12 As shown in the figure, the elasticity of goose meat was significantly improved after high-voltage pulse treatment, among which the elasticity of the CG+PEF 1min group was 1.17 times that of the CG group, and the elasticity decreased after PEF treatment for 10 minutes, indicating that the high-voltage pulse electric field treatment for 1 minute had a better effect on the elasticity of goose meat. After the protonation reaction, the high-voltage pulse electric field was applied for 1 minute, and the elasticity of goose meat was the best at this time. The elasticity of goose meat in the LA+PEF 1min group was 1.62 times that of the PEF 1min group. The elasticity of goose meat in the deprotonation pretreatment group was worse than that in the protonation pretreatment group, indicating that the high-voltage pulse electric field under protonation conditions had the best effect on the elasticity of goose meat.

[0086] Fig.13 The effect of protonation combined with high voltage pulse electric field technology on the tenderness of goose meat. Fig.13 As shown in the figure, protonation significantly improved the tenderness of goose meat. After 1 minute of combined high-voltage pulsed electric field treatment, the shear force of goose meat in the LA+PEF 1min group was 74.7% of that in the CG group. Since the shear force is inversely proportional to the tenderness of meat products, it shows that compared with the CG group, the high-voltage pulse treatment significantly improved the tenderness of goose meat after the protonation signal was enhanced. The shear force of goose meat in the PEF 10min group was higher than that in the PEF 1min group, indicating that long-term application of high-voltage pulsed electric field treatment made the tenderness of goose meat worse, which is consistent with the effect on the hardness of goose meat. The effect of deprotonation treatment on the tenderness of goose meat was not significant. Therefore, protonation combined with short-time electric pulse treatment has the best effect on the regulation of goose meat tenderness.

[0087] 7. Effect of protonation combined with high-voltage pulsed electric field technology on the microstructure of goose meat

[0088] like Fig.14 As shown in the figure, protonation can stabilize the cross section of myofibrils. The Z line and M line of goose meat in the protonation group and the protonation combined with short-term high-voltage pulse electric field treatment group are clearly visible, while the M line in the sarcomere disappears after protonation combined with long-term high-voltage pulse electric field treatment. In addition, the goose meat grid in the deprotonated group basically disappears, and the microstructural damage of the surface goose meat is obvious. When the protonation combined with high-voltage pulse electric field treatment for 1 minute, the muscle density is small, indicating that the muscle tissue is more compact at this time, and the smaller gaps between muscle fibers and more complete sarcomere structure are usually associated with higher water holding capacity and better texture. Short-term high-voltage pulse electric field promotes the interaction between muscle molecules, resulting in rearrangement and aggregation of the cross-sectional area. This reorganization increases the gel strength and forms a tighter network structure. Therefore, protonation combined with short-term high-voltage pulse electric field treatment can significantly reduce the microstructural damage of the cross section of goose meat muscle.

[0089] In summary, the regulatory effect of single protonation on goose meat quality is poor, which may lead to structural degradation such as excessive aggregation of goose myofibrillar protein and excessive unfolding, which is not conducive to the water retention, oil retention and flavor fidelity of goose meat products. However, using protonation signal to amplify the regulatory effect of high-voltage pulsed electric field can enhance the release of goose meat flavor, strengthen the generation of characteristic goose meat flavor, and significantly improve the edible quality of goose meat, especially key qualities such as tenderness.

[0090] The above description is not intended to limit the present invention, and the present invention is not limited to the above examples. Any changes, modifications, additions or substitutions made by a person skilled in the art within the spirit and scope of the present invention shall also fall within the protection scope of the present invention.

Claims

1. A method for treating goose meat quality by amplifying protonation signals and regulating pulse electric fields, characterized in that The following steps are involved: (1) Cut fresh goose meat into pieces and immerse them in a lactic acid solution; (2) The goose meat obtained in step (1) is subjected to high-voltage pulse electric field treatment to complete the quality control of the goose meat.

2. The method for treating goose meat quality by amplifying protonation signals and regulating pulse electric fields according to claim 1, characterized in that: The lactic acid solution described in step (1) is a lactic acid solution with a mass concentration of 30%, and the immersion time is 45 minutes.

3. The method for treating goose meat quality by amplifying protonation signals and regulating pulse electric fields according to claim 1, characterized in that: The mass ratio of the goose meat described in step (1) to the lactic acid solution is 1:

3.

4. The method for treating goose meat quality by amplifying protonation signals and regulating pulse electric fields according to claim 1, characterized in that: The high-voltage pulse electric field strength described in step (2) is 15 kV / cm, the number of pulses is 9, the frequency is 60-100 Hz, and the treatment time is 1 min.

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