Structure Of Myofibrillar Protein Research Articles

The influence of pH-ultrasonic-induced myofibrillar protein conformation of Penaeus vannamei (Litopenaeus vannamei) on emulsification and digestion characteristics of fish oil oleogel-based emulsions.

pH-induced and ultrasound treatment can both adjust spatial conformation to improve the interfacial stability, and fish oil oleogel could be used to enhance oil binding capacity. The relationship between stabilization mechanism and lipid digestion was revealed, considering the protein conformation and interfacial characteristics. The results showed that pH-ultrasonic-induced myofibrillar proteins (MPs) at pH 7.0 had higher interfacial adsorption capacity and surface hydrophobicity as well as more stable secondary structures, which lowered the particle size and enhanced the interfacial stability. In the stomach, the particle size increased along with the decrease in electrostatic repulsion, and β-sheets significantly increased, which promoted aggregation and flocculation. In the small intestine, the reduction of β-sheets favored the interfacial replacement and facilitated the lipid digestion. Therefore, pH-ultrasonic-modified method improved the structure and function of MPs, facilitated the interfacial stability and intestinal digestion.

Stability of large yellow croaker (Pseudosciaena crocea) as affected by temperature abuse during frozen storage: Quality attributes, myofibril characteristics, and microstructure

Temperature abuse occurs frequently during transportation and frozen storage, which affects the quality of frozen aquatic products. Recrystallization generated by temperature abuse leads to irreversible damage to the muscle tissue and microstructure, and exacerbates undesirable oxidation reactions, thus reducing the quality of frozen aquatic products. In this study, a modeling system of temperature abuse alternating between −24 °C and −7 °C was established to evaluate the effect of temperature abuse on the stability of frozen large yellow croaker. The results revealed that temperature abuse caused water migration with the extension of storage time, as well as poorer texture, color, and freshness. Furthermore, the structure of myofibrillar protein (MP) was severely damaged, with a gradual decrease in total sulfhydryl groups and Ca2+-ATPase activity, a loosening of the secondary structure, and a disruption of the protein conformation. The confocal laser scanning microscopy (CLSM) analysis also found that temperature abuse exacerbated protein aggregation. Therefore, temperature abuse during transportation and frozen storage could affect the stability of large yellow croaker negatively, and it mainly originated from the growth of ice crystals and the effect of recrystallization. The study was supposed to provide new insights into the improvement of frozen aquatic products quality.

Research on the spoilage potential and metabolic patterns of specific spoilage bacteria in grouper (Epinephelus lanceolatus) during cold storage

Pseudomonas fragi and Serratia liquefaciens are key spoilage microorganisms in aerobically packed groupers during cold storage. Spoilage bacteria were inoculated into fillets to investigate their spoilage potential. The results showed that P. fragi had stronger degradation activity, and the P. fragi inoculated group had higher total volatile basic nitrogen (TVB-N) and K values, lower water holding capacity (WHC), and textural qualities. The P. fragi inoculated group had higher levels of carbonyl groups and lower levels of sulfhydryl groups, indicating higher levels of protein oxidation. The secondary and tertiary structure of myofibrillar protein (MP), scanning electron microscopy, and low-field nuclear magnetic resonance (LF-NMR) analyses showed that P. fragi degraded myofibrils more and induced water loss from the muscle. Metabolomics analyses indicated that purine metabolism and glycine, serine, and threonine metabolism were important pathways associated with P. fragi spoilage; linoleic acid metabolism and β-alanine metabolism were important pathways for S. liquefaciens spoilage.

Revealing protein aggregation behaviour and dispersion properties induced by molecular interactions between sucrose esters and myofibrillar protein in an aqueous phase system

The effects of sucrose esters (SE) with varying hydrophilic-lipophilic balance (HLB) values (SE 11, 13, 15) and different concentrations (0.01, 0.1, 1.0 mM) on the dispersion properties and structure of myofibrillar proteins (MPs) in the aqueous phase were investigated. The results demonstrated that the SE 11 and SE 13 reduced the particle size and enhanced the distribution uniformity of the MPs. All of the SE exhibited a slight reduction in the ζ-potential absolute values of the MPs. Meanwhile, the SE 11 significantly reduced the turbidity of the MPs, especially in the 0.1 mM group. Macroscopic and microscopic images showed that the optimum dispersion state was in the SE 11–0.1 group. Furthermore, the interactions between SE and MPs exerted a significant impact on the proteins structure. The SE 13 and SE 15 caused significant changes, which presented concentration correlation, in the tertiary and secondary spatial structures of the MPs. Nevertheless, slight structural changes were observed in MPs with different SE11 concentrations. The SE did not alter the molecular weight of the MPs, i.e. it did not induce irreversible aggregation, nor degradation of the proteins. These results were verified by the surface hydrophobicity, UV–Vis spectroscopy, intrinsic fluorescence, circular dichroism, and SDS-PAGE. Molecular docking simulation showed that hydrophobic interactions and hydrogen bonds were the main interaction force between SE 11 and MPs. Therefore, our findings provided meaningful insights into the dispersion state of the MPs aqueous containing SEs and contributed to the practical application of non-ionic surfactants in meat protein processing.

Effects of ultrahigh pressure heat-assisted technology on the physicochemical and gelling properties of myofibrillar protein from Penaeus vannamei

This study investigated the changes in conformation and gelling properties of myofibrillar protein (MP) from Penaeus vannamei under various ultrahigh pressure (UHP)-heat assisted technologies. The results indicated that UHP heat-assisted technology enhanced the cross-linking of the gel network by causing a rearrangement of the secondary structure of MP. Microstructural analysis revealed that MP gels treated with UHP heat-assisted technology exhibited a more uniform gel network structure. Additionally, UHP heat-assisted technology improved the binding capacity of water molecules within the gel network, particularly in the two-stage UHP heat-assisted (PBH) condition at 400 MPa. Gels prepared under this condition demonstrated the highest gel strength, measuring 386.4 g·mm. Furthermore, in vitro simulated digestion showed that PBH method significantly improved the digestibility of MP gels, suggesting that the UHP heat-assisted technology had the potential to produce easily digestible MP gel-based aquatic foods.

Inhibitory effect of L-arginine on the oxidative aggregation behavior of myofibrillar proteins in the Antarctic krill (Euphausia superba): pH and antioxidation

In this study, the effect of L-arginine (L-Arg) on the oxidative aggregation of myofibrillar proteins (MPs) in Antarctic krill was evaluated. The results showed that the oxidized aggregation of MPs was significantly inhibited after the addition of 20 mM L-Arg compared to the oxidized group, the solubility of MPs significantly increased by 25.74 %, the turbidity reduced from 0.56 to 0.18. These effects were primarily attributed to the addition of L-Arg, which prevented the unfolding of the spatial structure of MPs after oxidation, inhibited the formation of disulfide bonds and dityrosine, and improved the stability of MPs structure. Analysis of carbonyl content and hydroxyl radical (•OH) inhibitory capacity showed that carbonyl formation and hydroxyl radicals were effectively reduced by the pH and guanidinium group of L-Arg. The pH of L-Arg exhibited a significantly higher effect than the guanidinium group in inhibiting the oxidative aggregation of MPs.

Cryoprotective effect of magnetic field-assisted freezing in combination with curdlan on myofibrillar protein of Litopenaeus vannamei: Oxidative aggregation, protein structure and thermal stability

To counteract the negative effects of conventional freezing methods on frozen surimi products, the present study investigated the effects of magnetic field (MF) freezing in combination with different amounts of curdlan (CUR) on oxidative denaturation, structural alterations, and thermal stability of myofibrillar protein (MP) in shrimp surimi. The results indicated that the intervention of magnetic fields alone improved the quality of frozen muscle proteins. Under the dual intervention of magnetic field-assisted freezing and CUR, small ice crystals formed with MF6 treatment resulted in significantly lower solubility, turbidity, and mean particle size than the control group (p < 0.05). Moreover, the oxidation of MP was also significantly slowed down by inhibiting the formation of hydrophobic groups and carbonyl groups, maintaining a high content of sulfhydryl groups. MF6 also exhibited a high Ca2+-ATPase activity. The α-helix content, the increase in fluorescence intensity under this condition also tend to make the secondary and tertiary structures of myofibrillar protein more stable. Meanwhile, electrophoretic profiles and CLSM showed that this condition maintains the integrity of the MP. In addition, the MF6 samples also had high protein thermal stability. However, excess CUR reduces the excellence of MP cryoprotection. As a result, MF6 has better protection and improvement effects on protein function, structure and thermal stability, and CUR was also found to have the potential for cryoprotectant development.

Effect of chitosan on thermal gelling properties of pork myofibrillar protein and its mechanism.

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.

Contribution of ultrasound‐assisted protein structural changes in marinated beef to the improved binding ability of spices and flavor enhancement

AbstractBACKGROUNDMarination is an important part of air‐dried beef processing, and traditional methods are inefficient and produce inconsistent results. Ultrasound, as a novel technology, can be combined with traditional marination methods. The study aimed to investigate the improvement of beef flavor by ultrasound‐assisted marination. At the same time, the potential relationship between the alteration of meat protein and flavor quality by ultrasound‐assisted marinating was further investigated to enable better flavor modulation and research.RESULTSHeadspace solid‐phase microextraction–gas chromatography–mass spectrometry revealed that the spice flavor of beef was significantly enhanced by 500 W ultrasound‐assisted marination. Meanwhile, the experimental results demonstrated that the ultrasound‐assisted marination promoted the unfolding of beef myofibrillar protein structure, which increased the number of hydrophobic and hydrogen bonding sites, enhanced the electrostatic effect and improved the functional properties of the protein. Ultrasound‐assisted marination significantly enhanced the binding ability of beef myofibrillar proteins to flavor compounds compared with conventional marination. An electronic nose confirmed that this resulted in a significant increase in the flavor of the marinated meat.CONCLUSIONUltrasound‐assisted marination effectively enhanced the flavor of marinated meat, which was closely related to the development of protein conformation. The results of this study have important implications for the food industry and the role of protein unfolding processes in flavor modulation. In particular, the findings can be practically applied to improving meat flavor under ultrasound‐assisted marination. © 2024 Society of Chemical Industry.

The Effect of Ultrasound Treatment on the Structural and Functional Properties of Tenebrio molitor Myofibrillar Protein.

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.

Mechanism of tumbling-curing to improve beef quality: Insights from the structural and functional properties of myofibrillar protein

Beef is highly nutritious but lacks tenderness and emulsification properties. This study aimed to investigate the impact of static curing (SC), tumbling-curing (TC), pulsating vacuum tumbling-curing (PVTC), and vacuum tumbling-curing (VTC) on the structural and functional properties of myofibrillar proteins and the mechanisms involved in enhancing beef quality. VTC significantly enhanced beef tenderness, water-holding capacity (WHC) and cooking yield. Additionally, the shear force was reduced by 58% and the cooking yield and WHC were increased by 6% compared with SC. There was an increase in the myofibrillar protein (MP) α-helix content and sulfhydryl content, while there was a reduction in the surface hydrophobicity and dityrosine content. These changes led to the enhancement of the functional properties of beef, such as protein emulsification and solubility. VTC minimized the damage caused by the curing process to the secondary and tertiary structures of MP by reducing their aggregation and oxidation. When compared with other curing methods, VTC proved to be an effective technology for enhancing beef tenderness and emulsification properties, therefore, essential in promoting ultra-processed beef products.

Insight into the effects of large yellow croaker roe (Larimichthys Crocea) phospholipids on the conformational and functional properties of pork myofibrillar protein

The large yellow croaker roe phospholipids (LYPLs), rich in polyunsaturated fatty acids, is a potential phospholipid additive for meat products. In this work, the effects of LYPLs on the structural and functional properties of myofibrillar protein (MP) were determined, and compared with egg yolk phospholipids (EYPLs) and soybean phospholipids (SBPLs). The results revealed that LYPLs, similar to SBPLs and EYPLs, induced a transformation in the secondary structure of MP from α-helix to β-sheets and random coils, while also inhibited the formation of carbonyl and disulfide bonds within MP. All three phospholipids induced MP tertiary structure unfolding, with the greatest degree of unfolding observed in MP containing LYPLs. The MP with LYPLs had the highest surface hydrophobicity, emulsification properties and gel strength. In addition, MP with LYPLs added also demonstrated superior rheological properties and water-holding capacity compared with SBPLs and EYPLs. In conclusion, adding LYPLs endowed MP with improved functional properties.

Preparation and characterization of fish-derived protein gel as a potential dysphagia food: Co-mingling effects of inulin and konjac glucomannan mixtures

The study aimed to create a fish-derived protein gel with inulin/konjac glucomannan (KGM) mixture for dysphagia. The inulin/KGM complex improved the swallowing properties of myofibrillar protein (MP) emulsion gel. Interactions, physicochemical, and flavor properties were analyzed. Inulin/KGM mixture inhibited hydrophobic groups exposure, and maintained MP structure during thermal induction. Inulin/KGM-protein gels exhibited shear-thinning behavior, low deformation resistance and hardness. IDDSI test also indicated inulin/KGM gels is suitable for dysphagia. Inulin/KGM mixture improved flavor by increasing ethanol and 2-octen-ol while decreasing ichthyological substances such as hexanal and nonanal, enhancing the sensory experience of patients with dysphagia. An 8% inulin/KGM mixture effectively modulated mechanical, swallowing, and sensory properties of MP emulsion gels, offering insights for future marine-derived dysphagia foods development.

Influence of EGCG (Epigallocatechin Gallate) on Physicochemical-Rheological Properties of Surimi Gel and Mechanism Based on Molecular Docking.

The influence of epigallocatechin gallate (EGCG) on the physicochemical-rheological properties of silver carp surimi gel was investigated. The gel strength, texture, water-holding capacity (WHC), dynamic distribution of water, and rheological properties of surimi gels added with different levels (0, 0.02, 0.04, 0.06, 0.08, and 0.1%) of EGCG were measured. The results showed that with the increase of EGCG content, the gel strength, hardness, WHC, and immobilized water contents of surimi gels showed a trend of first increasing and then decreasing, and EGCG 0.02% and EGCG 0.04% showed better gel performance as compared with the control. EGCG 0.02% had the highest gel strength (406.62 g·cm), hardness (356.67 g), WHC (64.37%), and immobilized water contents (98.958%). The gel performance decreased significantly when the amounts of EGCG were higher than 0.06%. The viscosity, G', and G″ of the rheological properties also showed the same trends. The chemical interaction of surimi gels, secondary structure of myofibrillar protein (MP), and molecular docking results of EGCG and silver carp myosin showed that EGCG mainly affected the structure and aggregation behavior of silver carp myosin through non-covalent interactions such as those of hydrogen bonds, hydrophobic interactions, and electrostatic interactions. The microstructures of EGCG 0.02% and EGCG 0.04% were compact and homogeneous, and had better gel formation ability. The lower concentrations of EGCG formed a large number of chemical interactions such as those of disulfide bonds and hydrophobic interactions inside the surimi gels by proper cross-linking with MP, and also increased the ordered β-sheet structure of MP, which facilitated the formation of the compact three-dimensional network gel.

Effects of slightly acidic electrolyzed water and ginger (Zingiber officinale Roscoe) juice on the quality and myofibrillar protein structure of silver carp (Hypophthalmichthys molitrix) fillets during cold storage

This study aimed to investigate the effects of slightly acidic electrolyzed water (SAEW) pretreatment combined with ginger (Zingiber officinale Roscoe) juice (GJ) on the quality, sensory characteristics, and myofibrillar protein structure of silver carp (Hypophthalmichthys molitrix). The results revealed that the SAEW-GJ delayed microbial spoilage by reducing the total viable counts and Pseudomonas spp. Moreover, the freshness of silver carp fillets was maintained by maintaining lower total volatile base nitrogen (TVB-N), ATP-related compounds, and free amino acids (FAAs). SAEW-GJ delayed myofibrillar protein oxidations by inhibiting the generation of carbonyl groups and maintaining a higher Ca2+-ATPase activity and sulfhydryl content. We also observed that SAEW-GJ treatment maintained myofibrillar organized secondary structure by keeping higher α-helix content and stabilized tertiary structure during cold storage. These results suggested that the SAEW-GJ could be used to enhance the quality of silver carp and prolong the shelf life by at least 6 days during cold storage.

Unlocking the molecular modifications of plasma-activated water-induced oxidation through redox proteomics: In the case of duck myofibrillar protein (Anas platyrhynchos)

Plasma-activated water (PAW) contains multiple active species that alter the structure of myofibrillar protein (MP) to enhance their gel properties. This work investigated the impact of PAW on the oxidation of cysteine in MP by label-free quantitative proteomics. PAW treatment caused the oxidation of 8241 cysteine sites on 2815 proteins, and structural proteins such as nebulin, myosin XVIIIB, myosin XVIIIA, and myosin heavy chain were susceptible to oxidation by PAW. Bioinformatics analysis, including Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway, subcellular localization, and STRING analysis, indicated that these proteins with differential oxidation sites were mainly derived from the cytoplasm and membrane, and were involved in multiple GO terms and KEGG pathways. This is one of the first reports of the redox proteomic changes induced by PAW treatment, and the results are useful for understanding the possible mechanism of PAW-induced oxidation of MP.

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

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. 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-1 γ/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-1 γ/β filled in the pores of MP gel network to form denser and more uniform structure. Oleogels prepared with 60 g kg-1 γ/β could effectively improve the quality of MP gel and have promising application prospects in surimi products. © 2024 Society of Chemical Industry.

Effects of multi-frequency ultrasound-assisted immersion freezing processing on myofibrillar protein structure and lipid oxidation of large yellow croaker (Larimichthys crocea) during long-time frozen storage

In this study, large yellow croaker (Larimichthys crocea) was frozen using multi-frequency ultrasound-assisted freezing (MUIF) with different powers (160 W, 175 W, and 190 W, respectively) and stored at −18 °C for ten months. The effect of different ultrasound powers on the myofibrillar protein (MP) structures and lipid oxidation of large yellow croaker was investigated. The results showed that MUIF significantly slowed down the oxidation of MP by inhibiting carbonyl formation and maintaining high sulfhydryl contents. These treatments also held a high activity of Ca2+-ATPase in the MP. MUIF maintained a higher ratio of α-helix to β-sheet during frozen storage, thereby protecting the secondary structure of the tissue and stabilizing the tertiary structure. In addition, MUIF inhibited the production of thiobarbituric acid reactive substances value and the loss of unsaturated fatty acid content, indicating that MUIF could better inhibit lipid oxidation of large yellow croaker during long-time frozen storage.

Effect of ultrasound-assisted L-lysine treatment on pork meat quality and myofibrillar protein properties during postmortem aging.

This paper aimed to investigate the effects of ultrasound-assisted L-lysine treatment on meat quality and myofibrillar proteins (MPs) properties of pork longissimus dorsi during postmortem aging. The results revealed that the L-lysine (Lys) and/or ultrasound treatment significantly increased (p < 0.05) the water-holding capacity and tenderness of the pork during postmortem aging, while the ultrasound-assisted Lys treatment had the lowest cooking loss, pressurization loss, Warner-Bratzler shear force, and hardness. In addition, L-lysine and/or ultrasound treatment increased (p < 0.05) pH value, T21, and myofibrillar fragmentation index, while the ultrasound-assisted Lys treatment had the highest value. Meanwhile, the protein solubility was increased with Lys and/or ultrasound treatment during postmortem aging, and ultrasound-assisted Lys treatment had the highest solubility, reaching 88.19%, 92.98%, and 91.73% at 0, 1, and 3 days, respectively. The result of protein conformational characteristics showed that Lys and/or ultrasound treatment caused the unfolding of the α-helix structure, resulting in the exposure of more hydrophobic amino acids and buried sulfhydryl groups, ultimately enhancing MPs solubility. In summary, ultrasound-assisted Lys treatment altered the structure of MPs, resulting in the enhancement of the water-holding capacity and tenderness of the pork. PRACTICAL APPLICATION: This study showed that ultrasound-assisted L-lysine (Lys) treatment could enhance the water-holding capacity and tenderness of pork during postmortem aging. The results might provide a reference for the application of ultrasound-assisted Lys treatment on the improvement of pork meat quality. To facilitate practical applications in production, the development of medium and large-sized ultrasound equipment for conducting small-scale and pilot experiments is crucial for future research.

Dietary supplementation with quercetin: an ideal approach for improving meat quality and oxidative stability of broiler chickens

This study aimed to improve the eating quality of yellow-feathered broiler chicks by feeding them corn-soybean meal diets supplemented with 250, 500, and 1,000 mg/kg quercetin. we examined the impact of varying doses of dietary quercetin on the sensory quality of chicken breast meat as well as on the antioxidant enzymes, antioxidant-related signaling molecules, structure and thermal stability of myofibrillar protein (MPs), and microstructure of myogenic fibers in the meat during 24 h of postslaughter aging. Additionally, we investigated the potential correlations among antioxidant capacity, MP structure, and meat quality parameters. The results indicated that dietary supplementations with 500 and 1,000 mg/kg quercetin improved the physicochemical properties and eating quality of yellow-feathered broiler chicken breast meat during 12 to 24 h postslaughter. Additionally, quercetin improved the postslaughter oxidative stress status and reduced protein and lipid oxidation levels. It also increased hydrogen bonding interactions and α-helix content during 6 to 12 h postslaughter and decreased β-sheet content during 12 to 24 h postslaughter in chicken breast MP. This resulted in improved postslaughter MP structure and thermal stability. The correlation results indicated that the enhancement of antioxidant capacity and MP structure enhanced the physicochemical and edible qualities of yellow-feathered broiler chicken breast meat. In conclusion, the current findings suggest that dietary supplementation with quercetin is an ideal approach for improving the eating quality of chicken meat, thereby broadening our understanding of theoretical and technological applications for improving the quality of chicken.