Effect of partial substitution of complex phosphates with sodium bicarbonate on aggregation, conformation and gel properties of beef-pork-chicken complex myofibrillar proteins.

BACKGROUND: Complex phosphates (CP) can improve the physicochemical properties and gelation properties of myofibrillar fibrous protein (MP) in mixed meat products, but an excessive intake of phosphates over a long period of time is harmful to health. The present study investigated the effects of partial or complete substitution of CP with sodium bicarbonate (SB) on the physicochemical properties and gel properties of beef-pork-chicken mixed myofibrillar protein (BPC-MP), aiming to evaluate the feasibility of this method in reducing the amount of phosphate in mixed meat products. RESULTS: Under the optimal substitution conditions, the turbidity of BPC-MP was reduced by 37.8%, the net negative potential was increased by 28.9% and the modulus of elasticity (G') was increased. The tertiary structure indexes of protein (including fluorescence intensity, surface hydrophobicity and active thiol content) were significantly changed, whereas the α-helix and ß-turn angle contents in the secondary structure of protein were significantly increased. In addition, the water retention ability and strength of gel were also improved, which were increased by 20.7% and 42.6%, respectively. The results of scanning electron microscopy showed that the SB substitution group had a more compact and ordered microstructure. CONCLUSION: The results showed that partial substitution of CP with SB reduced the amount of phosphate added to BPC-MP and had a positive effect on the physicochemical and gel properties of BPC-MP. © 2024 Society of Chemical Industry.

Cryoprotective effect of epigallocatechin gallate replacing sucrose on Hypophythalmichthys molitrix surimi during frozen storage.

BACKGROUND: The present study aimed to investigate the cryoprotective effect of epigallocatechin gallate (EGCG) replacing sucrose on surimi during frozen storage. Substitution or partial substitution of 0.1% EGCG for sucrose (1.5%) was added to surimi, and the surimi samples without and with commercial cryoprotectants (4% sucrose and 4% sorbitol) were used as the control group. RESULTS: The results obtained suggest that, with the increase in frozen storage time, the structural performance of surimi protein gradually weakened (e.g. the decrease in the surface hydrophobicity, the increase in the total sulfhydryl and solubility, and the protein myosin heavy chain bands became shallow) and surimi gel quality gradually deteriorated (e.g. the decrease in water-holding capacity, gel strength and all texture profile attributes). However, compared with the other three group surimi samples during the frozen period, the surimi proteins with partial replacement of sucrose by EGCG had a higher total sulfhydryl group content and solubility of proteins, as well as lower surface hydrophobicity of protein, suggesting that the addition of EGCG as a partial substitute for sucrose can enhance the antifreeze ability of surimi. Meanwhile, the surimi gel with the partial replacement of sucrose by EGCG had a higher water retention capacity, gel strength and texture attributes (e.g. hardness, springiness, cohesiveness, chewiness, and resilience), indicating that the addition of EGCG as a partial substitute for sucrose can inhibit the deterioration of surimi gel quality. CONCLUSION: Overall, EGCG partially replacing sucrose can play an alternative cryoprotectant with a lower sweetness to prevent the quality of surimi from deteriorating. © 2024 Society of Chemical Industry.

Characteristics of hairtail surimi gels treated with myofibrillar protein-stabilized Pickering emulsions.

BACKGROUND: Hairtail (Trichiurus haumela) surimi exhibits poor gelation properties and a dark gray appearance, which hinder its utilization in high-quality surimi gel products. The effect of Pickering emulsions stabilized by myofibrillar proteins (MPE) on the gel properties of hairtail surimi has been unclear. In particular, the impact of MPE under NaCl and KCl treatments on the quality of hairtail surimi gels requires further elucidation. RESULTS: Pickering emulsions stabilized by myofibrillar proteins and treated with NaCl or KCl (Na-MPE, K-MPE) were added to hairtail surimi in amounts of 10-70 g kg-1. The addition of 50 g kg-1 Na-MPE and K-MPE improved the gel strength, textural properties, whiteness, and water-holding capacity (WHC) of hairtail surimi. The relative content of ß-turn and ß-sheet in the surimi gels increased and the relative content of random coils and α-helix decreased with the addition of oil. The addition of Na-MPE and K-MPE did not affect the secondary structure of surimi gels but stimulated the gelation of hairtail surimi gels. Hairtail surimi containing K-MPE demonstrated similar performance in terms of hardness, microstructure, and WHC compared with the addition of Na-MPE. CONCLUSION: The quality of hairtail surimi gels can be improved by the addition of Na-MPE or K-MPE. The K-MPE proved to be an effective option for enhancing the properties of hairtail surimi gels at 50 g kg-1 to replace Na-MPE. © 2024 Society of Chemical Industry.

Effect of γ-oryzanol/ß-sitosterol-based oleogels on the physicochemical and gel properties of Nemipterus virgatus myofibrillar protein.

BACKGROUND: The effect of oleogels prepared with peanut oil and different concentrations of γ-oryzanol and ß-sitosterol mixture (γ/ß; 20, 40, 60, 80 and 100 g kg-1) on the physicochemical and gel properties of myofibrillar protein (MP) was investigated. RESULTS: The solubility and average particle size of MP first decreased and then increased with increasing γ/ß concentration. Peanut oil or oleogels could induce the exposure of hydrophobic amino acids and the unfolding of MP, thus significantly increasing the surface hydrophobicity, sulfhydryl content and absolute value of zeta potential, which reached maximum values when the γ/ß concentration was 60 g kg-1 (P < 0.05). The addition of peanut oil decreased the gel strength and water holding capacity of MP gel. However, oleogels prepared with 60 g kg-1 γ/ß could significantly increase the hydrophobic interactions and disulfide bond content of MP gel (P < 0.05), which promoted the crosslinking and aggregation of MP, enhancing the gel properties. Peanut oil had no significant influence on the secondary structure of MP, while oleogels promoted the transition of MP conformation from α-helix to ß-sheet structure. The results of light microscopy and confocal laser scanning microscopy indicated that oleogels prepared with 60 g kg-1 γ/ß filled in the pores of MP gel network to form denser and more uniform structure. CONCLUSION: Oleogels prepared with 60 g kg-1 γ/ß could effectively improve the quality of MP gel and have promising application prospects in surimi products. © 2024 Society of Chemical Industry.

Insight into the effect of large yellow croaker roe phospholipids on the physical properties of surimi gel and their interaction mechanism with myofibrillar protein.

BACKGROUND: The present study aimed to investigate the effects of large yellow croaker roe phospholipids (LYCRPLs) on the physical properties of surimi gels and to clarify their interaction mechanism with myofibrillar proteins (MPs) in terms of chemical forces and the spatial conformation. RESULTS: LYCRPLs could improve the gel strength, textural properties, rheological properties and water-holding capacity of surimi gels. Moreover, the interaction mechanism between LYCRPLs with MPs was revealed through intermolecular forces, Fourier transform infrared spectroscopy and ultraviolet visible absorption spectroscopy. The findings demonstrated that LYCRPLs enhanced the surface hydrophobicity and particle size of MPs, facilitating expansion and cross-linking of MPs. CONCLUSION: These results provide a theoretical basis for improving the characteristics of surimi gels and thus facilitate the application of LYCRPLs in the aquatic food industry. © 2023 Society of Chemical Industry.

Effect of low-voltage electrostatic field-assisted partial freezing on large yellow croaker protein properties and metabolomic analysis during storage.

BACKGROUND: Large yellow croaker is highly perishable during storage because of high protein and moisture content. The degradation of the fish is mainly attributed to microbial growth and enzyme activity, so it is important to find an efficient storage method to extend its shelf life. METHODOLOGY: This study investigated the effect of a low-voltage electrostatic field combined with partial freezing treatment on the physicochemical properties of myofibrillar protein (MP) and metabolomic analysis of large yellow croaker during preservation. The samples in chilled storage (C), partial freezing storage (PF) and 6 kV/m low-voltage electrostatic field partial freezing storage (LVEF-PF) were analyzed during an 18 day storage period. RESULTS: In comparison with the C and PF groups, LVEF-PF delayed the oxidation of MP by inhibiting the formation of carbonyl groups (2.25 nmol/mg pro), and maintaining higher sulfhydryl content (29.73 nmol/mg pro). Fourier transform infrared (FTIR) spectroscopy and fluorescence spectroscopy analysis also demonstrated that the LVEF-PF treatment maintained the stability of the protein structure by increasing the a-helix ratio (19.88%) and reducing the random coil ratio (17.83%). Scanning electron microscopy showed that, compared with the LVEF-PF group, there was more degeneration and aggregation of MP in the C and PF groups after 18 days' storage. The results of untargeted metabolomic analysis showed that 415 kinds of differential metabolites were identified after storage, and the difference levels of differential metabolites were least between the samples treated with LVEF-PF stored on the ninth day and the fresh samples. The main differential metabolic pathways during storage were amino acid metabolism and lipid metabolism. CONCLUSION: The LVEF-PF treatment could maintain the stability of myofibrillar protein in large yellow croaker during storage. These results showed a potential application of the LVEF-PF method for aquatic product preservation. © 2023 Society of Chemical Industry.

Covalent and non-covalent interaction of myofibrillar protein and cyanidin-3-O-glucoside: focus on structure, binding sites and in vitro digestion properties.

BACKGROUND: The aim of this study was to investigate the effects of covalent and non-covalent interactions between myofibrillar protein (MP) and cyanidin-3-O-glucoside (C3G) on protein structure, binding sites, and digestion properties. Four methods of inducing covalent cross-linking were used in the preparation of MP-C3G conjugates, including tyrosinase-catalyzed oxidation, alkaline pH shift treatment, free radical grafting, and ultrasonic treatment. A comparison was made between MP-C3G conjugates and complexes, and the analysis included sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), C3G binding ratio, liquid chromatography-tandem mass spectrometry (LC-MS/MS), protein side-chain amino acids, circular dichroism spectroscopy, three-dimensional fluorescence, particle size, and in vitro simulated digestion. RESULTS: Covalent bonding between C3G and amino acid side chains in MP was confirmed by LC-MS/MS. In covalent bonding, tryptophan residues, free amino groups and sulfhydryl groups were all implicated. Among the 22 peptides covalently modified by C3G, 30 modification sites were identified, located in lysine, histidine, tryptophan, arginine and cysteine. In vitro simulated digestion experiments showed that the addition of C3G significantly reduced the digestibility of MP, with the covalent conjugate showing lower digestibility than the non-covalent conjugate. Moreover, the digestibility of protein decreased more during intestinal digestion, possibly because covalent cross-linking of C3G and MP further inhibited trypsin targeting sites (lysine and arginine). CONCLUSION: Covalent cross-linking of C3G with myofibrillar proteins significantly affected protein structure and reduced protein digestibility by occupying more trypsin binding sites. © 2023 Society of Chemical Industry.

Study on the interaction and gel properties of pork myofibrillar protein with konjac polysaccharides.

BACKGROUND: Natural myofibrillar protein (MP) is sensitive to changes in the microenvironment, such as pH and ionic strength, and therefore can adversely affect the final quality of meat products. The aim of this study was to modify natural MP as well as to improve its functional properties. Therefore, the quality improvement effect of konjac polysaccharides with different concentrations (0, 1.5, 3, 4.5 and 6 g kg-1 protein) on MP gels was investigated. RESULTS: With a concentration of konjac polysaccharides of 6 g kg-1 protein, the composite gel obtained exhibited a significant improvement of water binding (water holding capacity increased by 7.71%) and textural performance (strength increased from 29.12 to 37.55 N mm, an increase of 8.43 N mm). Meanwhile, konjac polysaccharides could help to form more disulfide bonds and non-disulfide covalent bonds, which enhanced the crosslinking of MP and maintained the MP gel network structure. Then, with the preservation of α-helix structure (a significant increase of 8.11%), slower protein aggregation and formation of small aggregates, this supported the formation of a fine and homogeneous network structure and allowed a reduction in water mobility. CONCLUSION: During the heating process, konjac polysaccharides could absorb the surrounding water and fill the gel system, which resulted in an increase in the water content of the gel network and enhanced the gel-forming ability of the gel. Meanwhile, konjac polysaccharides might inhibit irregular aggregation of proteins and promote the formation of small aggregates, which in turn form a homogeneous and continuous gel matrix by orderly arrangement. © 2023 Society of Chemical Industry.

Effects of faba bean protein isolate on rheological properties of pork myofibrillar protein gels and quality characteristics of pork low-fat model sausages.

BACKGROUND: This study aimed to assess the effect of faba bean (Vicia faba L.) protein isolate (FBPI) on the rheological properties of pork myofibrillar protein gels (MPGs) and the quality characteristics of pork low-fat model sausages (LFMSs). RESULTS: Pork MPGs with 5 or 10 g kg-1 FBPI had higher cooking yield, gel strength, and viscosity than controls. The addition of FBPI to MPGs increased the protein surface hydrophobicity and decreased sulfhydryl groups. Adding FBPI to MPGs changed the protein profile and microstructure. The cooking loss and expressible moisture of LFMSs with 5, 10, or 15 g kg-1 FBPI were lower than those of controls and showed similar results to those with 15 g kg-1 soy protein isolate (SPI). Hardness values of LFMSs with FBPI and SPI were no different, and were higher than those of controls. CONCLUSION: The addition of FBPI potentially improves rheological properties of MPGs and the functional properties of LFMSs, including water-holding capacity and textural properties. © 2024 Society of Chemical Industry.

Progress in the application of novel cryoprotectants for the stabilization of myofibrillar proteins.

In this review, the physicochemical and conformational changes of myofibrillar proteins (MPs) of freeze-induced mince-based aquatic foods were comprehensively summarized in depth. Studies have demonstrated that temperature fluctuation and long-time freezing negatively affect food quality, resulting in texture alteration, drip fluid, flavor degradation, and nutrition loss due to MPs denaturation, aggregation, and oxidation. Attempts have been made in ice-recrystallization inhibition, freezing point depression, and ice shape and growth control for better cryopreservation. Moreover, to further minimize the quality deterioration, cryoprotectants were acknowledged to reduce the denaturation and aggregation of the MPs effectively. Recently, interest in novel functional ingredients, including oligosaccharides, protein hydrolysates, and natural polyphenols demonstrated excellent cryoprotective effects while avoiding health concerns and undesirable flavor caused by traditional sugar-based or phosphates-based cryoprotectants. Therefore, the present review provides a systematic overview of these low molecular weight multifunctional substances with a particular sequence and highlights their underlying mechanism in the inhibition of ice recrystallization the stabilization of MPs.

Effects of 2,2'-Azobis(2-methylpropionamidine) Dihydrochloride Stress on the Gel Properties of Duck Myofibrillar Protein Isolate.

The aim of this study was to investigate the biochemical properties and gel-forming capacity of duck myofibrillar proteins under the effects of 2,2'-azobis(2-methylpropionamidine) dihydrochloride (AAPH)-mediated oxidation. Duck myofibrillar proteins were extracted and treated with different concentrations of AAPH solutions (0, 1, 3, 5, 10 mmol/L) and then analysed for carbonyl content, dynamic rheology, protein profiles and gel-forming properties (colour, water holding capacity, gel strength and microstructure). The results showed that with increasing AAPH concentration, the carbonyl content of the proteins exhibited an increasing trend (p < 0.05); SDS-PAGE pattern changes indicated that moderate oxidation (3 mmol/L AAPH) induced myosin aggregation via covalent bonds including disulfide, enhanced protein-protein interactions, and thus affected the gel strength of the DMPs' heat-induced gels. However, high oxidation (5 and 10 mmol/L AAPH) led to the partial degradation of the myosin heavy chain (MHC) isoforms, as evidenced by lower storage modulus and irregular microstructures, which significantly reduced gelation ability. These results suggest that the internal relationship between alkylperoxyl radical-induced oxidation should be taken into account in the processing of duck meat, as mild protein oxidation is conducive to improving gel quality.

Oxidation of Cathepsin D by Hydroxy Radical: Its Effect on Enzyme Structure and Activity against Myofibrillar Proteins Extracted from Coregonus peled.

In this study, cathepsin D was oxidized in vitro with different concentrations of H2O2, and the activity, structure, and extent of myofibrillar protein degradation by oxidized cathepsin D were evaluated. The sulfhydryl content of cathepsin D decreased to 9.20% after oxidation, while the carbonyl content increased to 100.06%. The ß-sheet in the secondary structure altered due to oxidation as well. The changes in the intrinsic fluorescence and UV absorption spectra indicated that oxidation could cause swelling and aggregation of cathepsin D molecules. The structure of cathepsin D could change its activity, and the activity was highest under 1 mM H2O2. Cathepsin D could degrade myofibrillar proteins in different treatment groups, and the degree of degradation is various. Therefore, this study could provide a scientific basis for the mechanism of interaction among hydroxyl radical oxidation, cathepsin D, and MP degradation.

Using nanocellulose to improve heat-induced cull cow meat myofibrillar protein gels: effects of particle morphology and content.

BACKGROUND: Enhancing protein gel properties is essential to improve the texture of meat products. In this study, the improvement effects of three types of nanocellulose, i.e. rod-like cellulose nanocrystals (CNC), long-chain cellulose nanofibers (CNF) and spherical cellulose nanospheres (CNS) with different concentrations (1, 3, 5, 10, 15 and 20 g kg-1 ), on cull cow meat myofibrillar protein (MP) gel were investigated. RESULTS: Compared with needle-shaped CNC and spherical CNS, the addition of 10 and 20 g kg-1 long-chain CNF had the most significant improvement effect on gel hardness and water-holding capacity, respectively (P < 0.05), increasing to 160.1 g and 97.8%, respectively. In addition, the incorporation of long-chain CNF shortened the T2 relaxation time and induced the formation of the densest network structure and promoted the phase transition of the gel. However, excessive filling of nanocellulose would destroy the structure of the gel, which was not conducive to the improvement of gel properties. Fourier transform infrared results showed that there was no chemical reaction between the three nanocellulose types and MP, but the addition of nanocellulose was conducive to gel formation. CONCLUSION: The improvement of MP gel properties by adding nanocellulose mainly depends on its morphology and concentration. Nanocellulose with higher aspect ratio is more beneficial to the improvement of gel properties. For each nanocellulose type, there is an optimal addition amount for MP gel improvement. © 2023 Society of Chemical Industry.

Myofibrillar protein can form a thermo-reversible gel through elaborate deamidation using protein-glutaminase.

BACKGROUND: Novel thermo-reversible hydrogels that undergo gelation in feedback to external stimuli have numerous applications in the food, biomedical, and functional materials fields. Muscle myofibrillar protein (MP) has long been known for thermally irreversible gelation. Once the reversible gelation of MP is achieved, its scope for research and application will expand. RESULTS: The work reported here achieved, for the first time, a thermo-reversible MP gelation by elaborate deamidation using protein glutaminase (PG). The protein concentration and PG reaction time within windows of 1.0-2.5% and 8 h or 12 h were observed to be vital for creating thermo-reversible gels. The gel strength increased with protein concentration. The gel displayed a perforated lamellar microstructure, which resulted in a high water-holding capacity. The rheological results revealed the thermo-reversibility of the gel was robust for up to five cycles of heating and cooling. The thermally reversible gelation is closely related to the reversible assembly between individual α-helix and helical coiled coil. Hydrophobic interactions proved to be predominantly involved in the formation and stabilization of the gel network structure. CONCLUSION: This work increases the scope of research into the thermo-responsive behavior of MP-based gel. It can foster advances in research into the applications of muscle proteins and into the use of PG as a novel ingredient in the food industry. © 2022 Society of Chemical Industry.

Evaluation on the effect of ice glazing with different compound additives on the quality of frozen stored (-23 °C) large yellow croaker (Pseudosciaena crocea).

BACKGROUND: Compounded ice glazing has been used in large yellow croaker to improve its quality during frozen storage. The ice glazing liquid is prepared by compound use of trehalose and tea polyphenols, and the moisture, protein-related properties and freshness of the fish have been evaluated during 300 days of frozen storage. RESULTS: The results showed that the addition of trehalose effectively reduced the loss of water. At the same time, it was difficult for ice crystals to grow under the action of trehalose, the average diameter could still be maintained at 111.25-119.85 µm. The combination with tea polyphenols could effectively maintain the protein structure and keep the total volatile base nitrogen (TVB-N) and K value within 11.84 mg/100 g and 13.18%, so that the freshness of the fish was always at the first level. CONCLUSION: In a word, the ice glazing with 5% trehalose and 8% tea polyphenols had the best preservation effect, which was recommended for the frozen storage. © 2022 Society of Chemical Industry.

Effect of konjac oligo-glucomannan on emulsifying properties of myofibrillar protein.

BACKGROUND: The high viscosity of konjac glumannan (KGM) limits its application in meat processing. In this work, the effects of konjac oligo-glucomannan (KOG), as a derivative of KGM, on the emulsifying properties of myofibrillar protein (MP) and the related mechanism were investigated. RESULTS: It was found that the addition of KOG had no significant effect on the secondary structure of MP, but altered the tertiary conformation of MP, resulting in exposure of tyrosine residues to polar microenvironments and decreased intrinsic fluorescence intensity. In addition, the addition of KOG increased the emulsifying activity of MP, resulting in decreased particle size and improved physical stability of the emulsion. The emulsifying activity of MP reached the maximum value when 1.0 wt% KOG was added. Moreover, the interfacial tension and interfacially adsorbed protein content of MP/KOG emulsions decreased with the increase in KOG concentration. CONCLUSION: These findings demonstrated that KOG mainly interacted with MP and changed the amphipathy of the KOG-MP at the oil-water interface, forming a stable interface film to improve the emulsifying properties of MP. © 2023 Society of Chemical Industry.

Ultrasound-assisted phosphorylation of goose myofibrillar proteins: improving protein structure and functional properties.

BACKGROUND: Goose meat is rough and embedded with dense connective tissue, impairing protein solubility. Therefore, to improve the functional properties of goose myofibrillar protein (GMP), ultrasound was used to assist the phosphorylation of GMP. RESULTS: The fact that GMP attached covalently with the phosphate group of sodium tripolyphosphate (GMP-STP) was disclosed directly by Fourier transform infrared spectroscopy. Furthermore, ultrasound significantly improved the hydrophobicity and solubility of GMP-STP, which could be attributed to the conversion of α-helix to ß-sheet, ß-turns, and random coils by sonication. The spatial stabilization of the protein phosphorylation process was boosted by ultrasound, making the droplets more dispersed, and thus an improvement in the functional properties of GMP-STP was observed. Water-holding capacity, oil-binding capacity, and emulsifying and foaming properties were best at an ultrasound power of 400 W. CONCLUSION: Ultrasound-assisted phosphorylation has great potential to modulate the structure-function relationship of proteins. © 2023 Society of Chemical Industry.

Evaluation and relationship analysis of pea protein on structure and heat-induced gel performance of myofibrillar protein.

BACKGROUND: Surimi products occupy a large market in the food industry, and the gel performance is an important index to evaluate them. Thus, it is of great significance and practical value to find better food ingredients to regulate the structure and gel performance of surimi products. In this study, we used pea protein (PP) to restructure fish myofibrillar proteins (MPs) to achieve regulation of protein gel performance. RESULTS: PP could enhance MP gel performance in terms of compressive strength, water-holding capacity, and some texture parameters. This may be the result of an increasing ß-sheet content and a decreasing trend in the α-helix content, along with enhancements in hydrophobic interactions, nonspecific associations, and ionic bonds in a mixed PP-MP gel. The compressive strength, texture, and water-holding capacity of MP gel were positively correlated with surface hydrophobicity, active sulfhydryl, turbidity, and ß-sheet of the mixed PP-MP system. CONCLUSION: The findings suggest that PP can regulate the gel performance by remodeling the structure of MP. The regulation and correlation analysis between gel performance, structure, and physicochemical properties were explored and established to provide a theoretical basis for improving the quality of surimi products. This study will broaden the application of PP in the field of food processing and provide theoretical guidance for the manufacture of new surimi products. © 2023 Society of Chemical Industry.

Insights into peptide profiling of sturgeon myofibrillar proteins with low temperature vacuum heating.

BACKGROUND: Protein oxidation during food processing causes changes in the balance of protein-molecular interactions and protein-water interactions, ultimately leading to protein denaturation, which results in the loss of a range of functional properties. Therefore, how to control the oxidative modification of proteins during processing has been the focus of research. RESULTS: In the present study, the intrinsic fluorescence value of the myofibrillar proteins (MP) decreased and the surface hydrophobicity value increased, indicating that the heat treatment caused a significant change in the conformation of the MP. With an increase in heating temperature, protein carbonyl content increased, total sulfhydryl content decreased, and protein secondary structure changed from α-helix to ß-sheet, indicating that protein oxidation and aggregation occurred. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that heat treatment can lead to the degradation of proteins, especially myosin heavy chain, although actin had a certain thermal stability. In total, 733 proteins were identified by proteomics, and the protein oxidation caused by low temperature vacuum heating (LTVH) was determined to be mild oxidation dominated by malondialdehyde and 4-hydroxynonenal by oxidation site division. CONCLUSION: The present study has revealed the effect of LTVH treatment on the protein oxidation modification behavior of sturgeon meat, and explored the effect mechanism of LTVH treatment on the processing quality of sturgeon meat from the perspective of protein oxidation. The results may provide a theoretical basis for the precise processing of aquatic products. © 2023 Society of Chemical Industry.

Effect of two-stage heating treatment on physicochemical properties of shrimp (Penaeus vannamei) meat.

BACKGROUND: Changes in the physicochemical properties of shrimp meat treated with two-stage heating were investigated. Currently, shrimp products in the processing process are susceptible to uneven dehydration, shrimp meat shrinkage, which results in rough and hard texture, poor chewiness, and seriously affects the edible quality as well as economic benefits. Improving the utilization value of shrimp resources, expanding its market shares, optimizing the tenderness of shrimp is the key to developing new types of fresh and ready-to-eat shrimp products. RESULTS: The results indicated that preheating at 30 °C could not affect the quality of shrimp meat significantly (P > 0.05). As the preheating temperature increased from 40 °C to 50 °C, the hardness and shear force of shrimp meat decreased due to the exposure of protein hydrophobic groups, protein aggregation and degradation, muscle fraction broken, and weight loss increase. Further increase in preheating temperature would lead to further aggregation and gelation of proteins, causing hardness and shear force increase. Besides, the results of microstructure showed that preheating at 40 °C and 50 °C could cause the shrimp muscles to become loose. CONCLUSION: This study showed that the preheating temperature ranging from 40 °C to 50 °C could effectively improve the tenderness of shrimp meat. This study might be useful for developing tenderized shrimp products in the future. © 2022 Society of Chemical Industry.