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Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Summary: The objective of this study was to evaluate the effect of slurry ice (SI) in physicochemical changes, water migration, myofibrillar protein characterisation, and extended shelf life during cold storage of pufferfish (Takifugu obscurus). SI provided faster cooling rate, better structural stability of muscle tissue, and a significant reduction in total viable count (TVC). In addition, the use of SI treatment resulted in a considerable reduction in total volatile basic nitrogen (TVB‐N) and pH. The results of the texture profile analysis (TPA) demonstrated that SI had a significant inhibitory effect on the reduction of hardness, springiness, resilience, and chewiness. In addition, SI treatment better maintained a well‐structured myofibrillar protein stabilising the tertiary structure. Low‐field nuclear magnetic resonance (LF‐NMR) and magnetic resonance imaging (MRI) revealed that SI treatment could retard the water migration. Furthermore, the results of confocal laser scanning microscopy (CLSM) and scanning electron microscopy (SEM) indicated that SI treatment of pufferfish effectively slowed down the degradation of their myofibrillar protein fraction throughout the cold storage. [ABSTRACT FROM AUTHOR]

Summary: Bighead carp has the largest production amount among freshwater fish in China, but its physicochemical properties change rapidly with the denaturation of their myofibril protein (MP). The protein–polysaccharide complexes have shown interesting physicochemical properties as stabilisers and emulsifiers. In this study, arabinoxylans (AXs) were prepared and mixed with bighead carp MP to form a composite gel. The effect of AXs on the thermal stability, emulsification and emulsion stability of the composite gel was investigated. The results showed that fraction precipitated by 60% ethanol (F60) and by 90% (F90) improved the denaturation temperature of bighead carp MP from 65.99 °C to 67.39 °C and 68.22 °C, respectively. The emulsifying capacity of F60 (0.54 m2 g−1) was similar to that of sucrose (0.52 m2 g−1). The effect of F90 on the emulsion stability of bighead carp MP was better than that of F60. The elasticity of bighead carp MP was improved by F60 and F90. The hydroxyl group interactions, hydrophobic interactions and electrostatic forces exist between the macromolecules. AXs of fresh maize bran could prevent protein denaturation and improve the emulsion capacity and gel properties of bighead carp MP. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

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. [ABSTRACT FROM AUTHOR]

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The myofibrillar protein (MP) of duck meat is prone to excessive oxidation during thermal processing, resulting in a decline in its overall quality. In this paper, the effect of shikimic acid on the oxidative structure of duck muscle fibrin was studied. The findings showed that, at a mass ratio of 1:50,000 (g/g) between shikimic acid and MP, the carbonyl content of MP was reduced by 74.20%, while the sulfhydryl content was increased by 73.56%. MP demonstrated the highest denaturation temperature, whereas its thermal absorption was the lowest. The percentage of α-helixes and β-sheets increased by 16.72% and 24.74%, respectively, while the percentage of irregular structures decreased by 56.23%. In addition, the surface hydrophobicity index of MP exhibited a significant decrease (p < 0.05), while there was a significant increase in its free radical-scavenging ability (p < 0.05). Molecular fluorescence spectrum analysis showed that shikimic acid could bind to MP, altering the internal environment of MP and enhancing its thermal stability. FTIR analysis showed that shikimic acid could enhance the distribution of protein particle sizes by reducing irregular structures, the proportion of β-rotation, and the degree of protein aggregation. It is hoped that this research can offer scientific support for improving meat processing technology. [ABSTRACT FROM AUTHOR]

Myofibrillar proteins primarily consist of myosin, actin, myogenin, and actomyosin. These proteins form complex networks within muscle fibers and are crucial to the physical and chemical properties of meat. Additionally, myofibrillar proteins serve as significant substrates for the adsorption of volatile flavor compounds, including aldehydes, alcohols, ketones, and sulfur and nitrogen compounds, which contribute to the overall flavor profile of meat products. A series of chemical reactions occur during the processing, storage, and transportation of meat products. Oxidation is one of the most significant reactions. Oxidative modification can alter the physical and chemical properties of proteins, ultimately impacting the sensory quality of meat products, including flavor, taste, and color. In recent years, considerable attention has been focused on the effects of protein oxidation on meat quality and its regulation. This study investigates the impact of myofibrillar protein oxidation on the sensory attributes of meat products by analyzing the oxidation processes and the factors that initiate myofibrillar protein oxidation. Additionally, it explores the control of myofibrillar protein oxidation and its implications on the sensory properties of meat products, providing theoretical insights relevant to meat processing methods and quality control procedures. [ABSTRACT FROM AUTHOR]

BACKGROUND: The effect of oleogels prepared with peanut oil and different concentrations of γ‐oryzanol and β‐sitosterol mixture (γ/β; 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/β 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/β 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−1γ/β 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 β‐sheet structure. The results of light microscopy and confocal laser scanning microscopy indicated that oleogels prepared with 60 g kg−1γ/β filled in the pores of MP gel network to form denser and more uniform structure. CONCLUSION: Oleogels prepared with 60 g kg−1γ/β could effectively improve the quality of MP gel and have promising application prospects in surimi products. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

BACKGROUND RESULTS CONCLUSION Previous studies have demonstrated that the addition of chitosan can improve the quality and functional properties of meat products. However, the underlying mechanism remains unclear. In this study, the effect and mechanism of the addition of chitosan on the gel properties of myofibrillar protein (MP) were investigated.The results indicated that the gel strength and the water‐holding capacity of MP‐chitosan gel increased significantly when chitosan was added at 2.5–10 mg mL−1. Myofibrillar protein samples with 10 mg mL−1 added chitosan exhibited the highest elasticity and viscosity during gel formation and strengthening. The addition of chitosan also caused a modification in both the secondary and tertiary structure of MP, resulting in an enhanced exposure of hydrophobic and sulfhydryl groups in comparison with the control. Chitosan inhibited the conversion of immobilized water into free water and the formation of water channels during the thermal gelation process of MP. The denaturation enthalpy (ΔH) of myosin decreased as the concentration of chitosan exceeded 5 mg mL−1. The microstructure showed that the incorporation of chitosan (5–10 mg mL−1) facilitated the formation of compact and well organized MP gel networks.The addition of chitosan can enhance the functional properties of meat protein and facilitate heat‐induced gelation, making it a promising ingredient for improving the quality of processed meat products. © 2024 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Copyright of Food & Fermentation Industries is the property of Food & Fermentation Industries and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The gel properties and molecular conformation of Spanish mackerel myofibrillar protein (MP) induced by soy protein isolate–inulin conjugates (SPI–inulin conjugates) were investigated. The addition of SPI–inulin conjugates significantly enhanced the quality of the protein gel. An analysis of different additives was conducted to assess their impact on the gel strength, texture, water-holding capacity (WHC), water distribution, intermolecular force, dynamic rheology, Raman spectrum, fluorescence spectrum, and microstructure of MP. The results demonstrated a substantial improvement in the strength and water retention of the MP gel with the addition of the conjugate. Compared with the control group (MP), the gel strength increased from 35.18 g·cm to 41.90 g·cm, and WHC increased from 36.80% to 52.67% with the inclusion of SPI–inulin conjugates. The hydrogen bond content was notably higher than that of other groups, and hydrophobic interaction increased from 29.30% to 36.85% with the addition of SPI–inulin conjugates. Furthermore, the addition of the conjugate altered the secondary structure of the myofibrillar gel, with a decrease in α-helix content from 62.91% to 48.42% and an increase in β-sheet content from 13.40% to 24.65%. Additionally, the SPI–inulin conjugates led to a significant reduction in the endogenous fluorescence intensity of MP. Atomic force microscopy (AFM) results revealed a substantial increase in the Rq value from 8.21 nm to 20.21 nm. Adding SPI and inulin in the form of conjugates is an effective method to improve the gel properties of proteins, which provides important guidance for the study of adding conjugates to surimi products. It has potential application prospects in commercial surimi products. [ABSTRACT FROM AUTHOR]

• This paper provides a new choice of freezing method by using 20 % ethanol, 20 % propylene glycol, 10 % glycerol, and 10 % sodium chloride aqueous solution as immersion freezing medium. • The freezing rate of IF was 2.66 cm/h, which was 6.33 times higher than that in AF groups. • Compared with AF and BF, the ice crystals were smaller and more uniformly shaped, with properties of lower water migration and less texture softening after cryogenic liquid freezing of IF and LNF group aquatic products. • Immersion freezing showed the same superiority in maintaining the freshness of fish fillets and retaining the protein structure as liquid nitrogen storage. The freezing of aquatic products without causing significant changes in quality is recently attracting much attention. In this study, the effects of air freezing (AF, -20 °C), blast freezing (BF, -35 °C), liquid nitrogen freezing (LNF), and immersion freezing (IF, -35 °C) by 20 % ethanol, 20 % propylene glycol, 10 % glycerol, and 10 % sodium chloride aqueous solutions, respectively, on muscle qualities and myofibrillar protein properties of the red drum were investigated. The results indicated that the freezing rate of IF was 2.66 cm/h, which was 6.33 times higher than that in AF groups. Compared with AF and BF, the ice crystals were smaller and more uniformly shaped, with properties of lower water migration and less texture softening after cryogenic liquid freezing of IF and LNF group aquatic products. Immersion freezing showed the same superiority in maintaining the freshness of fish fillets and retaining the protein structure as liquid nitrogen storage. Overall, IF has similar effects to LNF in maintaining muscle qualities and myofibrillar protein properties. This study describes a new freezing method that uses 20 % ethanol, 20 % propylene glycol, 10 % glycerol, and 10 % sodium chloride aqueous solutions as immersion freezing medium. The multi-compound freezing medium has the potential to be used for the freezing of aquatic products. [ABSTRACT FROM AUTHOR]

Summary: Freshness and physicochemical properties of myofibrillar protein (MP) from decapitated Harpiosquillid mantis shrimp (HMS) treated with pulsed electric field (PEF), followed by soaking in 2% chitooligosaccharide (D‐P‐COS) and whole HMS (U‐W) during storage in iced water of 3 days were investigated. Lower rate of increase in K‐value, freshness index, in D‐P‐COS was observed in comparison with U‐W. For physicochemical properties of MP, MP from U‐W had gradual decrease in ATPase activity throughout the storage of 3 days, whereas no drastic alteration was attained in MP from D‐P‐COS. Surface hydrophobicity and carbonyl contents of MP from both samples upsurged up to 3 days, nevertheless the increases were more pronounced in D‐P‐COS. The secondary conformation changes were affected by decapitation, treatment and storage time. Decapitation and treatments maintained freshness, however, slightly enhanced physicochemical changes of MP from HMS. [ABSTRACT FROM AUTHOR]

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 β‐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. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The objective of this study was to explore the impacts of various ultrasonic powers (0, 300, 500, 700, and 900 W) on the structure and functional attributes of the myofibrillar protein (MP) of Tenebrio molitor. As the ultrasonic intensity escalated, the extraction efficiency and yield of the MP rose, while the particle size and turbidity decreased correspondingly. The reduction in sulfhydryl group content and the increase in carbonyl group content both suggested that ultrasonic treatment promoted the oxidation of the MP to a certain extent, which was conducive to the formation of a denser and more stable gel network structure. This was also affirmed by SEM images. Additionally, the findings of intrinsic fluorescence and FTIR indicated that high-intensity ultrasound significantly altered the secondary structure of the protein. The unfolding of the MP exposed more amino acid residues, the α-helix decreased, and the β-helix improved, thereby resulting in a looser and more flexible conformation. Along with the structural alteration, the surface hydrophobicity and emulsification properties were also significantly enhanced. Besides that, SDS–PAGE demonstrated that the MP of T. molitor was primarily composed of myosin heavy chain (MHC), actin, myosin light chain (MLC), paramyosin, and tropomyosin. The aforementioned results confirmed that ultrasonic treatment could, to a certain extent, enhance the structure and function of mealworm MP, thereby providing a theoretical reference for the utilization of edible insect proteins in the future, deep-processing proteins produced by T. molitor, and the development of new technologies. [ABSTRACT FROM AUTHOR]

Summary: Most dietary fibres improved rheological properties but negatively impacted digestibility. However, the effect of psyllium husk powder (PHP) on digestibility has not been yet reported. Thus, this study aimed to evaluate the rheological properties and digestibility of chicken myofibrillar protein (MP) containing different concentrations of PHP (0%, 0.5%, 1.0%, 1.5%) at 0.45 m NaCl. To assess the rheological properties of MP, viscosity, hydrophobicity, disulphide bond, SDS–PAGE, cooking yield and gel strength were evaluated. The addition of PHP enhanced water retention capacity and protein–protein interactions in the MP system. To evaluate the effect of PHP on digestibility, protein digestibility, SDS–PAGE and microstructure observations were performed. It was confirmed that the addition of PHP improved the protein digestibility of MP by measuring the differences in protein content (%). Therefore, the addition of PHP into MP gel improved not only the rheological properties but also the protein digestibility during in vitro digestion. [ABSTRACT FROM AUTHOR]

Myofibrillar proteins are mainly responsible for the structure-forming properties of emulsified meat products due to their gelling abilities. To enhance the gel characteristics of myofibrillar protein, the effect of lipids in different physical states on MP gelation was studied. In this study, chicken fat (CF), refined palm oil (RPO), and palm stearin (ST) were used to emulsify the extracted chicken myofibrillar protein (MP). The whiteness, water holding capacity, gel strength, solubility, emulsifying stability index, thermal and rheological properties, protein separation, and microstructure of MP gels were evaluated. The results demonstrated that RPO addition increased the physicochemical parameters, followed by CF and ST, and the ratio between MP and lipid was 4 to 1. MP-RPO also showed better thermal properties, characterized by a high peak temperature of peak 3 during differential scanning calorimetry analysis. MP-ST was the most unstable, indicated by the lowest peak temperature, while MP-CF did not differ significantly from MP-RPO. The frequency sweep test showed that RPO has the highest G' and lowest tan δ values, indicating a strong network formation. The changes in electrophoresis bands demonstrated that myosin might be involved in creating heat-induced MP gel, with no difference between lipid types. Additionally, the microstructure showed that MP-RPO gel had smaller oil droplets coated with interfacial protein film. Hence, RPO might be the best lipid source when emulsifying chicken protein due to its high water holding capacity with excellent thermal and rheological properties. [ABSTRACT FROM AUTHOR]

Polyphenol compounds can modify myofibrillar proteins to improve the quality of fish and surimi. Nevertheless, research into the precise mechanisms of interaction between phenolic substances and sea bass myofibrillar proteins is lacking. This study aimed to explore the interaction mechanism between five phenolic compounds (caffeic acid (CFA), gallic acid (GA), chlorogenic acid (CHA), resveratrol (RES), and catechin (CAT)) with sea bass myofibrillar protein (MP). The results of UV–vis absorption spectroscopy, Fourier transform infrared (FT-IR) spectroscopy, and fluorescence spectroscopy (namely, multi-spectroscopy) showed that all five phenolic compounds could spontaneously form new complexes with MP, with a binding molar ratio of 1:1. The interaction between CFA and MP is predominantly electrostatic, while the interaction between GA and MP is mainly hydrophobic. The rest of phenolic compounds and MP are mediated by hydrogen bonds and van der Waals forces. And molecular dynamics (MD) simulations indicated that CHA-myosin had the minimum root mean square deviation, while CFA-myosin had the smallest Rg value. In addition, the amino acid Lys-179 was the key residue for the interaction between five phenolic compounds and myosin. This study contributes to a better understanding of the interaction between phenolic compounds and sea bass MP, which could develop the processing of aquatic food products. [ABSTRACT FROM AUTHOR]

In order to investigate the effect of ultrasound on the structure and physical stability of chicken myofibrillar protein (MP) under low-salt conditions (0.15 mol/L NaCl), as well as the oxidizing effect of free radicals generated by ultrasound on MP, this study investigated the changes in the structure and oxidative properties of MP under low-salt conditions after ultrasound treatments (20 kHz, 450 W for 0, 3, 6, 9, and 12 min). The results showed that compared with the control group, the solubility, physical stability, and absolute ζ-potential of MP under low-salt conditions increased significantly (P < 0.05) with ultrasonic treatment time, whereas the turbidity and particle size decreased significantly (P < 0.05). The solubility was increased to 58.5% after 12 min of ultrasonic treatment. After ultrasonic treatment, the surface hydrophobicity and molecular flexibility were significantly increased, indicating that ultrasonic treatment caused the highly aggregated structure of myofibrillar protein to unfold and the internal hydrophobic groups to be exposed under low-salt conditions. After ultrasonic treatment for more than 6 min, the free sulfhydryl content of MP began to gradually decrease, whereas the content of disulfide bonds increased. After ultrasonic treatment for 12 min, the contents of free radicals, carbonyl groups and dimerized tyrosine (by 20.55%) were significantly increased (P < 0.05), while the free amino group content was decreased significantly (P < 0.05). In conclusion, ultrasonic treatment changed the structural properties of MP under low-salt conditions and increased its physical stability, thereby contributing to the formation of emulsions. Ultrasonic treatment can generate free radicals; ultrasonic treatment time for 6 min can exacerbate the oxidation of MP. So, attention should be paid to the oxidizing effect of free radicals generated by ultrasound on MP when applying ultrasonic treatment to improve the functional properties of MP.

To develop low-salt meat products and achieve the reduction in costs of meat production, the effect of konjac gum on the gel properties of soy protein isolate (SPI)-myofibrillar protein (MP) composite at various salt concentrations was investigated in this study. For the purpose of evaluating the effects of SPI, konjac gum, salt concentration, and other factors on MP gel formation, rheological properties and microstructures of the SPI-MP composite gels were analyzed using a rheometer and scanning electron microscopy. The obtained results indicated that at low salt concentration (0.3 mol/L NaCl), the gel strength of 3% MP-1% SPI composite gel significantly increased (P

In order to solve the problems of short shelf life of refrigerated Micropterus salmoides and the deterioration of quality during refrigerated storage, three preservatives including trehalose (Tre), ginger extract (GE) and Nisin were selected for single factor experiment. L9(34) orthogonal experiment was used to optimize the ratio of the compound preservative. The total viable count (TVC), pH, total volatile basic nitrogen (TVB-N) content, sensory evaluation, water holding capacity, moisture distribution, texture properties and myofibrillar protein (MP) oxidation stability indexes of Micropterus salmoides during refrigerated storage were measured with the optimal ratio of the compound preservative. The optimal ratio of the compound preservative (3.0% Tre, 0.06% GE and 0.06% Nisin) was obtained by single factor experiment and orthogonal experiment. The results showed that on the 8th day of refrigeration, the logarithm of TVC of control group (CK group) was 6.01, which exceeded the specified limit of spoilage. At the 16th day of storage, the logarithm of TVC of EG2 group was still lower than 6.00, the content of TVB-N was not more than 20 mg/100 g and the pH was less than 7.20. Compared with CK group, free water content in compound preservative groups (EG1 group and EG2 group (that was preferred group)) were significantly decreased, water holding capacity were significantly increased (P

The effects of the addition of curdlan gel with two different forms, thermal reversible curdlan gum (TRC) and thermal irreversible curdlan gum (TIRC) on the gelling properties and in vitro digestibility of myofibrillar proteins (MP) gel were investigated. The results showed that the gel strength and water holding capacity of MP gel significantly increased with increasing TRC or TIRC concentration (P0.05). Therefore, this study provides a theoretical basis for the effect of TRC or TIRC on the formation and in vitro digestion of MP gel, and lays a technical support for the application of curdlan gum in meat industry.

To further develop a protein-polysaccharide composite fat replacer in low-fat meat products, this used pumpkin seed protein (PSP) and carrageenan to prepare a composite emulsion fat replacer, and added it to myofibrillar protein (MP) to form heat induced gel. The effects of the composite emulsion formed by PSP and carrageenan at various additive amounts on the properties of MP gels were investigated through the determination of gel moisture distribution, textural properties, microstructure, rheological properties, and other indexes. The results showed that when PSP and carrageenan composite emulsion was added at 50%, the water-holding properties and strength of the gel significantly improved (P

Abstract Freezing technology is important for the long‐term preservation of aquatic products such as surimi. However, mechanical damage caused by ice crystals would lead to quality deterioration. Abalone viscera glycopeptide (AVGP) complex was prepared by hydrolysis technology, which exhibited ice recrystallization ability and antioxidant activity. Moreover, effects of AVGP on Ca2+‐ATPase activity, total sulfhydryl content, secondary structure of myofibrillar protein (MP), rheological properties, and gel properties of surimi frozen were investigated. Results showed that surimi treated with AVGP could improve the gel strength and rheological properties of surimi, reduce the gel ice crystal holes, and improve the degradation of gel matrix caused by freeze–thaw. AVGP can significantly inhibit the decrease of Ca2+‐ATPase activity and total sulfhydryl group content. When the addition of AVGP exceeded 4% (w/w), its freezing protection effect on MP was better than that of commercial antifreeze agents. Moreover, the α‐helix and β‐fold contents in the 4% AVGP group were significantly higher than those in the control group, indicating that the addition of an appropriate amount of AVGP can protect the secondary structure of MP. Therefore, AVGP could serve as a new food ingredient with antifreeze and antioxidant functions for frozen surimi.

Abstract Polysaccharides are widely used as quality improvers for meat products. However, the mechanisms of how different ionic polysaccharides regulate the gelling properties of myofibrillar protein (MP) are still unclear. This study aimed to elucidate the contribution of different ionic polysaccharides to MP gelation and its mechanism. The enhancement of hydrogen bond, hydrophobic interaction, and disulfide bond between carboxymethyl cellulose sodium (CMC‐Na, anionic polysaccharide) and MP made them bind tightly, which contributes to the improvement of gel strength, water‐holding capacity, and viscoelasticity. Konjac glucomannan (neutral polysaccharide) mainly relied on physical filling to support the gel network and improve the gel characteristics. The electrostatic attraction between cationic polysaccharides and MP enhanced the binding between them. However, due to the large structure of chitosan (cationic polysaccharide) sugar chain, it can only attach to the surface of protein, which limits the interaction between them. These findings will provide guidance for the application of polysaccharides as food quality improvers or fat substitutes and the design of new low‐fat restructured meat products.

In order to screen for meat tenderization treatment methods targeting a large number of eliminated laying hens in poultry farms, the ultrasound combined with calcium chloride and biological enzyme methods were used to tenderize chicken breast meat. The shear force was chosen as the key indicator, and the optimal ultrasound parameters were selected. The texture, water retention, protein distribution, total thiol and amino acid contents as well as the microstructure changes were mainly analyzed. Results showed that the optimal ultrasound parameters were ultrasound of 240 W, frequency of 22 kHz, water bath temperature of 35 ℃, and treatment time of 10 minutes. Compared to the untreated group, the shear force of chicken breast meat significantly decreased (P

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. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

To develop low-salt meat products and achieve the reduction in costs of meat production, the effect of konjac gum on the gel properties of soy protein isolate (SPI)-myofibrillar protein (MP) composite at various salt concentrations was investigated in this study. For the purpose of evaluating the effects of SPI, konjac gum, salt concentration, and other factors on MP gel formation, rheological properties and microstructures of the SPI-MP composite gels were analyzed using a rheometer and scanning electron microscopy. The obtained results indicated that at low salt concentration (0.3 mol/L NaCl), the gel strength of 3% MP-1% SPI composite gel significantly increased (P<0.05) to 97 g relative to 43 g of the 4% MP gel, and the water-holding capacity also increased from 36% to 50%. However, the gel strength and water-holding capacity were decreased when the replacement amount of SPI increased (2% MP-2% SPI composite) compared with 3% MP-1% SPI composite. The gel strength decreased from 177 g of 4% MP to 89 g of 2% MP-2% SPI composite with at 0.6 mol/L NaCl concentration. The gel strength and water holding capacity of the MP-SPI composite gel were increased after adding high amount of konjac gum. At 0.3 mol/L NaCl concentration, the gel strength of 2% MP-2% SPI composite increased from 66 g to 93 g after adding 1% konjac gum, and the water holding capacity also increased from 44% to 65%. Therefore, konjac gum can eliminate the disruption of SPI on the gel formation of MP. The results of scanning electron microscopy revealed that the strong water-holding capacity of konjac gum and the filling effect of SPI led to the increase in gel strength. Consequently, at the concentration of 0.3 mol/L salt, 0.5%~1% konjac gum could improve the characteristics of MP protein gel with low SPI substitution (1%). [ABSTRACT FROM AUTHOR]

In order to solve the problems of short shelf life of refrigerated Micropterus salmoides and the deterioration of quality during refrigerated storage, three preservatives including trehalose (Tre), ginger extract (GE) and Nisin were selected for single factor experiment. L9(34) orthogonal experiment was used to optimize the ratio of the compound preservative. The total viable count (TVC), pH, total volatile basic nitrogen (TVB-N) content, sensory evaluation, water holding capacity, moisture distribution, texture properties and myofibrillar protein (MP) oxidation stability indexes of Micropterus salmoides during refrigerated storage were measured with the optimal ratio of the compound preservative. The optimal ratio of the compound preservative (3.0% Tre, 0.06% GE and 0.06% Nisin) was obtained by single factor experiment and orthogonal experiment. The results showed that on the 8th day of refrigeration, the logarithm of TVC of control group (CK group) was 6.01, which exceeded the specified limit of spoilage. At the 16th day of storage, the logarithm of TVC of EG2 group was still lower than 6.00, the content of TVB-N was not more than 20 mg/100 g and the pH was less than 7.20. Compared with CK group, free water content in compound preservative groups (EG1 group and EG2 group (that was preferred group)) were significantly decreased, water holding capacity were significantly increased (P<0.05), and the hardness, chewiness and sensory scores of Micropterus salmoides were better than CK group. The related indexes of MP oxidation stability showed that the total sulfhydryl content and Ca2+-ATPase activity in compound preservative groups (EG1 group and EG2 group (that was preferred group)) were significantly higher than those in CK group (P<0.05), while the surface hydrophobicity and carbonyl group content were significantly lower than those in CK group (P<0.05), meanwhile, the protective effect of EG2 group on the oxidation stability of MP was better than that of EG1 group. The correlation analysis showed that there was significant correlation (P<0.01) among the indexes of Micropterus salmoides fillets treated with compound preservatives. Comprehensive analysis showed that the quality deterioration of refrigerated Micropterus salmoides could be effectively delayed and the MP oxidation of refrigerated Micropterus salmoides could be significantly inhibited, among which the optimal ratio group (EG2 group) had the best comprehensive effect. This study would provide a theoretical basis for the development and application of water retention and preservation technology for refrigerated Micropterus salmoides. [ABSTRACT FROM AUTHOR]

To further develop a protein-polysaccharide composite fat replacer in low-fat meat products, this used pumpkin seed protein (PSP) and carrageenan to prepare a composite emulsion fat replacer, and added it to myofibrillar protein (MP) to form heat induced gel. The effects of the composite emulsion formed by PSP and carrageenan at various additive amounts on the properties of MP gels were investigated through the determination of gel moisture distribution, textural properties, microstructure, rheological properties, and other indexes. The results showed that when PSP and carrageenan composite emulsion was added at 50%, the water-holding properties and strength of the gel significantly improved (P<0.05), textural properties improved, and cooking loss and freeze-thaw stability significantly reduced (P<0.05). The rheological properties showed that the G' of the gel was always higher than the G". Therefore, a gel structure with elasticity and a denser and homogeneous microstructure was formed. Collectively, the gel properties of MP improved with the addition of 50% PSP and carrageenan composite emulsion. [ABSTRACT FROM AUTHOR]

The effects of the addition of curdlan gel with two different forms, thermal reversible curdlan gum (TRC) and thermal irreversible curdlan gum (TIRC) on the gelling properties and in vitro digestibility of myofibrillar proteins (MP) gel were investigated. The results showed that the gel strength and water holding capacity of MP gel significantly increased with increasing TRC or TIRC concentration (P<0.05), and reached the maximum value at 0.4%, which was confirmed by dynamic rheological behavior. Meanwhile, the addition of TRC or TIRC promoted the transformation of α-helix into β-sheet, and the hydrophobic interaction and disulfide bond were the primary forces of mixed gels. The microstructures revealed that the addition of TRC or TIRC promoted the formation of the dense and uniform protein network structure. However, the modes of interactions between TRC or TIRC and MP induced the different patterns for the gel formation, resulting in the differences in the microstructure of MP gels. In addition, the addition of TRC or TIRC inhibited protein hydrolysis into small peptides and amino acids, which significantly decreased in vitro protein digestibility (P<0.05). Especially when the supplemental level was 0.3% (w/w), the digestibility was reduced from 77.53% to 71.66%. However, no significant effect on the in vitro digestibility of MP gels was observed for each addition form of curdlan (P>0.05). Therefore, this study provides a theoretical basis for the effect of TRC or TIRC on the formation and in vitro digestion of MP gel, and lays a technical support for the application of curdlan gum in meat industry. [ABSTRACT FROM AUTHOR]

Chicken claw products with their unique texture are loved by consumers, and cooking is a key step to affect the taste of chicken claw consumption, through the moderate hydrolysis of proteins and a series of physicochemical changes, so that the chicken claw gets tender and presents a crispy taste, but the current research on the optimal cooking conditions for chicken claw is still relatively small. In the present work, combinations of time (11, 13, 15, 17, and 19 min) and temperature (82, 86, 90, 94, and 98°C) were applied to the cooking of chicken claws. The effects of different cooking conditions on the quality characteristics of chicken claws were investigated, with special emphasis on the cooking loss rate, color, texture properties, lipid oxidation, myofibrillar fragmentation index (MFI), and total sulfhydryl content. The results showed that the cooking loss rate, lipid oxidation, and MFI value of chicken claws gradually increased, and the total color difference (∆E), puncture force, shear force, and total sulfhydryl content gradually decreased with the increase of cooking temperature and cooking time. Overall, chicken claws cooked at 86, 90, and 94°C for 15 and 17 min had better texture and flavor. Cooking treatment had a significant effect on the quality characteristics of chicken claws. Overall, chicken claws cooked at 86, 90 and 94°C for 15 and 17 min had better texture and flavor. [ABSTRACT FROM AUTHOR]

Copyright of Modern Food Science & Technology is the property of Editorial Office of Modern Food Science & Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The present study demonstrates the effects of pH-shifting treatments and magnetic field-assisted pH-shifting treatments on the properties of myofibrillar protein (MP) in frozen meat. The solubility results indicate that the pH-shifting treatments increased the solubility of MP from 16.8% to a maximum of 21.0% (pH 9). The values of surface hydrophobicity and protein particle size distribution indicate that the pH-shifting treatment effectively inhibited protein aggregation through electrostatic interactions. However, under higher pH conditions (pH 10, 11), the treatments assisted by the magnetic field increased the degree of aggregation. The total thiol content and SDS-PAGE results further suggest that the magnetic field-assisted pH-shifting treatment accelerated the formation of covalent bonds among MPs under the alkaline environment. The results of the Differential Scanning Calorimetry (DSC) and protein secondary structure analysis indicate that the magnetic field promoted the unfolding of protein structures in an alkaline environment, markedly reducing the effective pH levels of pH-shifting. Electron paramagnetic resonance (EPR) data indicate that the phenomenon might be associated with the increased concentration of free radicals caused by the magnetic field treatment. In summary, the application of magnetic field-assisted pH-shifting treatments could emerge as a potent and promising strategy to improve the protein properties in frozen meat. [ABSTRACT FROM AUTHOR]

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

In this study, ultrafiltration fractions (<3 k Da, LMH; >3 k Da, HMH) and solid-phase extraction fractions (hydrophilic hydrolysate, HIH; hydrophobic hydrolysate, HOH) from trypsin hydrolysate purified from croceine croaker (Pseudosciaena crocea) isolate were obtained to investigate the cryoprotective effects of the different fractions, achieved by means of maceration of turbot fish meat after three freeze-thaw cycles. Alterations in the texture, color, moisture loss, myofibrillar protein oxidation stability and conformation, and microstructure of the fish were analyzed after freezing and thawing. The results demonstrate that HIH maximized the retention of fish texture, reduced moisture loss, minimized the oxidation and aggregation of myofibrillar proteins, and stabilized the secondary and tertiary structures of myofibrillar proteins compared to the control group. In conclusion, the HIH component in the trypsin hydrolysates of croceine croaker significantly contributes to minimizing freeze damage in fish meat and acts as an anti-freezing agent with high industrial application potential. [ABSTRACT FROM AUTHOR]

Dried abalones are precious products, in which candy abalone is the most treasured one, owing to its unique taste. After rehydration and simmering, the core part tastes extraordinarily tender and viscoelastic, just like a soft candy which may almost melt in mouth. However, the reason for this has yet to be elucidated. The purpose of this study is to research the formation mechanism of the candy-like core in candy abalone. First of all, we characterized the viscoelasticity, microstructure and protein changes of candy abalone during the simmering process. The texture results indicated that the springiness and adhesiveness of candy abalone showed an increase. Scanning and transmission electron microscopy suggested that myofibrillar protein in candy abalone formed a dense three-dimensional network hydrogel structure. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis revealed such a hydrogel structure might be derived from the degradation of the myofibrillar protein during the drying process. Also, we identified degraded peptides mainly stemmed from paramyosin by mass spectrometry. Moreover, molecular dynamics simulation revealed that the hydrogen bonds and hydrophobic interactions are mainly responsible for the self-assembly of peptides during the rehydration and simmering stages. Different from reported protein hydrogels, the rheological and morphological properties of the formed peptide hydrogels in candy abalone have significant changes. In this study, we found that the myofibrillar protein of fresh abalone degraded into peptides during the drying process, which further cross-linked to form a peptide hydrogel during the rehydration and simmering stages, thereby producing a unique viscoelastic candy-like core in candy abalone. [ABSTRACT FROM AUTHOR]

The utilization of improper thawing methods can potentially compromise the quality of food, while the degeneration of myofibrillar protein during the thawing process directly impacts the alteration of physical and chemical properties of food. The effects of high-pressure thawing (HPT), water immersion thawing (WIT), and air thawing (AT) on the quality and myofibrillar protein (MP) denaturation of salmon were investigated. The thawing times of WIT, AT, and HPT-300 MPa were 23.6, 116.6, and 10.1 min, respectively, suggesting that HPT improved the rate of thawing. Compared with conventional thawing methods, the color difference of HPT-100 MPa and the water loss of HPT-150 MPa were reduced by 56.77% and 6.77%, respectively, and textural deterioration was weakened, preserving the quality of thawed salmon. In the current study, 200 and 300 MPa were the pressure thresholds for the degradation of salmon myosin and actin proteins, respectively. Meanwhile, HPT induced noticeable changes in the stability, secondary structure, and micromorphology of salmon MPs, which affected various physical and chemical properties of thawed salmon samples, such as water loss, color, and texture. In particular, the spatial structure stability of MP can be better maintained at HPT-100 MPa and HPT-150 MPa. HPT can be an alternative strategy to the traditional thawing of salmon. [ABSTRACT FROM AUTHOR]

Copyright of Modern Food Science & Technology is the property of Editorial Office of Modern Food Science & Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

In this study, the effect of ultrasound-assisted non-covalent binding of different polyphenols (tannins, quercetin, and resveratrol) on the structure and functional properties of myofibrillar proteins (MP) from the golden threadfin (Nemipterus virgatus) was investigated. The effect of ultrasound-assisted polyphenol incorporation on the structure and properties of MP was evaluated by multispectral analysis, interfacial properties, emulsification properties and antioxidant properties et al. The results revealed that the protein–polyphenol interaction led to a conformational change in the microenvironment around the hydrophobic amino acid residues, resulting in an increase in the equilibrium of the MP molecules in terms of affinity and hydrophobicity. Ultrasound assisted polyphenols addition also led to a significant decrease of the oil/water interfacial tension (from 21.22 mN/m of MP to 8.66 mN/m of UMP-TA sample) and a significant increase of the EAI (from 21.57 m2/g of MP to 28.79 m2/g of UMP-TA sample) and ES (from 84.76 min of MP to 124.25 min of UMP-TA). In addition, ultrasound-assisted polyphenol incorporation could enhance the antioxidant properties of MP, with the DPPH and ABTS radical scavenging rate of UMP-TA increase of 47.7 % and 55.2 % in comparison with MP, respectively. The results demonstrated that the noncovalent combination with polyphenols under ultrasound-assisted conditions endowed MP with better functional properties, including solubility, emulsification, foaming, and antioxidant properties through structure change. This study can provide innovative theoretical guidance for effectively preparing aquatic protein–polyphenol non-covalent complexes with multiple functions and improving the processing and utilization value of aquatic proteins.

In order to explore the effects of cooking pressure and holding time on the structure of chicken myofibrillar protein eggs, in this study, chicken breast meat was used as the main raw material, and atmospheric pressure, micro-pressure (4 kPa) and high-pressure (70 kPa) were selected to cook for 15~35 min. The changes of carbonyl content, sulfhydryl content, microstructure and protein secondary structure of myofibrillar protein during cooking were studied. The results showed that with the extension of holding time, the carbonyl content showed an upward trend, and the carbonyl content increased by 1.22 times, 1.38 times and 1.19 times respectively with normal pressure, micro pressure and high pressure cooking. The content of sulfhydryl group showed a downward trend, and the content of sulfhydryl group decreased by 29.6%, 29.8% and 31.4% respectively after normal pressure, micro pressure and high pressure cooking. With the extension of holding time, the content of β-sheet and random coil in the secondary structure of myofibrillar protein increased, and the content of α-helix decreased. The degree of damage to the structure of chicken breast protein was high pressure>micro pressure>normal pressure. The results of this study would provide data reference and technical support for the production of sauced chicken prefabricated products.

Transglutaminase (TGase), an efficient protein cross-linking agent, has been widely applied in the meat industry to enhance the quality of meat products by modifying the structure of myofibrillar protein (MP) and consequently improving the heat-induced gel properties of MP. Meanwhile, degree of cross-linking (DCL) is the most important indicator to evaluate the cross-linking effect catalyzed by TGase, which is of particular importance for analyzing the effect of covalent cross-linking catalyzed by TGase on the conformational characteristics, physicochemical properties, and gel properties of MP. Therefore, this article systematically reviews the influential factors of DCL in TGase-catalyzed covalent cross-linking of MP, and dissects the molecular mechanisms of the effect of exogenous additives and novel processing technologies on TGase-catalyzed cross-linking. The aim of this article is to establish the relationship among structural modification, molecular mechanism and quality improvement for TGase-modified MP, which will provide innovative theoretical and technical support for the development of new types of meat products.

Myofibrillar protein (MP) is an important protein in muscle, which can form a three-dimensional gel network structure upon heat treatment, ultimately influencing the quality of meat products. In the meat industry, hydrocolloids from different are incorporated to enhance the gel strength, water-holding capacity and functional properties of MP gel and finally optimize the quality of meat products. However, many factors affect the interaction between MP and hydrocolloids during the formation of heat-induced MP gelation, which in turn affects MP gel properties. In this article, the gelation mechanism of MP is systematically reviewed, the interaction mechanism between different hydrocolloids and MP is discussed, and the key factors influencing the regulatory effect of hydrocolloids on the formation of heat-induced MP gel and the effect of hydrocolloids on MP gel properties are summarized. We anticipate that this review will lay a theoretical foundation for establishing the key technical system based on hydrocolloids to regulate the quality of meat products and also provide technical guidance for future practical application.

In this study, the effects of five common oxidative decontaminating agents (H2O2 solution, ClO2 solution, NaClO solution, ozonated water and slightly acidic electrolytic water) on the bacterial decontamination of tilapia fillets and their influence on the texture, color and myofibrillar protein (MP) oxidation in tilapia fillets were investigated. The results showed that a decontamination rate of 80% was attained by immersion in 1 500 mg/L H2O2 solution for 8 min, 200 mg/L ClO2 solution for 10 min, 200 mg/L NaClO solution for 10 min, 9 mg/L ozonated water for 10 min, or 30 mg/L slightly acidic electrolytic water for 20 min. Compared with the control group, treatment with decontaminating agents increased the hardness and L* value of tilapia fillets, decreased the a* value, MP content, total sulfhydryl group content, and raised the content of carbonyl groups and the amount of surface hydrophobic groups. The degree of protein denaturation in the slightly acidic electrolytic water and NaClO solution groups was the highest; the fluorescence intensity of MP was decreased after decontamination treatments, with the greatest decrease being found in the slightly acidic electrolytic water-treated group; the relative contents of α-helix and β-turn in MP were decreased, while the relative contents of β-fold and random coil were increased, with the most significant changes in the secondary structure of MP being observed in the slightly acidic electrolytic water-treated group (P < 0.05). MP underwent degradation to different extents, and the degradation degree of the slightly acidic electrolytic water group was higher than that of the other treatment groups. In summary, the oxidation of fish MP occurred to varying degrees after oxidative decontamination treatments, with slightly acidic electrolytic water treatment having the strongest oxidative effect.

In this study, the binding properties and structural changes associated with the interaction of Coregonus peled myofibrillar protein (MP) and different concentrations (6, 30, 150, and 300 µmol/g) of chlorogenic acid (CA) were investigated. The CA-MP complexes were formed at 25 °C, and the physical and chemical properties (total sulfhydryl groups, surface hydrophobicity), changes in secondary and tertiary structure (measured by Fourier-infrared spectroscopy, synchrotron fluorescence, and 3D fluorescence), and binding properties (measured by UV spectra, fluorescence quenching, and thermodynamic parameters) of the CA-MP complexes were measured. The results showed that at concentrations of 300 µmol/g CA, the total sulfhydryl content and surface hydrophobicity of MP decreased abruptly by 25.65% and 40.26%, respectively (P

Arginine (Arg), a safe basic amino acid, modulates interprotein interactions and impacts the processing characteristics of myofibrillar proteins (MP) in meat products, as numerous studies have demonstrated. This study aimed to explore the effects of varying concentrations of Arg (0.025, 0.050, 0.100, 0.200 %) on the physicochemical properties and gel behavior of yak MP. Utilizing yak MP as the substrate, we assessed and analyzed the physicochemical attributes and gel performance of the MP-Arg composite system. The findings revealed that Arg facilitates MP unfolding and internal group exposure, effectively mitigating oxidative tertiary structure alterations. Arg exerts potent antioxidant activity on MP, augmenting their water-holding capacity, which ameliorates gel properties. In this experiment, 0.05 % Arg maximally inhibited oxidative damage to MP, with protection being concentration-dependent. Collectively, these findings suggest that Arg effectively inhibits the oxidative degradation of MP structure and promotes the formation of enhanced gel characteristics.