Structure Of Myofibrillar Protein Research Articles

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.

Modification of myofibrillar protein structural characteristics: Effect of ultrasound-assisted first-stage thermal treatment on unwashed Silver Carp surimi gel

The hardness properties of unwashed surimi gel are considered as the qualities of gelation defect. This research investigated the effect of ultrasound-assisted first-stage thermal treatment (UATT) on the physicochemical properties of unwashed Silver Carp surimi gel, and the enhancement mechanism. UATT could reduce protein particle size, which significantly reduced from 142.22 μm to 106.70 μm after 30 min of UATT compared with the nature protein. This phenomenon can promote the protein crosslinking, resulting in the hardness of surimi gel increased by 15.08 %. Partially unfolded structure of myofibrillar protein and exposures of tryptophan to water, lead to the increase in the zeta potential absolute value, driven by UATT. The reduced SH group level and the conformational conversion of proteins from random coiling to α-helix and β-sheet, which was in support of intermolecular interaction and gel network construction. The results are valuable for processing protein gels and other food products.

Myofibrillar protein hydrolysis under hydroxyl radical oxidative stress: Structural changes and their impacts on binding to selected aldehydes

In this study, a hydroxyl radical oxidation system was established to simulate the oxidation process in fermented meat products. This system was employed to examine the structural changes in myofibrillar proteins (MPs) resulting from tryptic hydrolysis after a hydroxyl radical oxidative regime. The effect of these changes on the ability of MPs to bind selected aldehydes (3-methyl butanal, pentanal, hexanal, and heptanal) was also investigated. Moderate oxidation (H2O2 ≤ 1.0 mM) unfolded the structure of MPs, facilitating trypsin-mediated hydrolysis and increasing their binding capacity for the four selected aldehydes. However, excessive oxidation (H2O2 ≥ 2.5 mM) led to cross-linking and aggregation of MPs, inhibiting trypsin-mediated hydrolysis. The oxidised MPs had the best binding capacity for heptanal. The interaction of the oxidised trypsin-hydrolysed MPs with heptanal was driven by hydrophobic interactions. The binding of heptanal affected the structure of the oxidised trypsin-hydrolysed MPs and reduced their α-helix content.

Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians)

Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m2/g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the β-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate–polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products.

Effect of prolonged cooking at low temperatures on the eating quality of Tibetan pork: meat quality, water distribution, and microstructure

Abstract Tibetan pigs inhabit the plateau regions and engage in extensive exercise. Their meat is firm and less palatable, and appropriate cooking conditions can improve the flavor of the meat. This study aimed to explore the impact of cooking temperatures and times on the cooking loss rate, moisture content, tenderness, and color of Tibetan pork to elucidate their effects on the eating quality of this meat. The results indicated a negative correlation between temperature and moisture content, which decreased from 72% to 65% as the temperature increased. Meanwhile, the oxidation of myofibrillar proteins substantially increased with cooking temperature and time, resulting in a gradual augmentation of the cooking loss and shear force of the pork. The migration of bound water and the release of free water from the pork were faster after treatment at 80 °C compared with 50 °C. The results of infrared spectroscopy suggested that prolonged cooking led to the conversion of α-helix into β-sheet in the secondary structure of myofibrillar proteins. The microstructures observed through scanning electron microscopy exhibited a gradual degradation of connective tissues in the muscles at high temperatures, and the fiber structure of the muscles became more condensed and granular, blurring the textural appearance of the muscles. These results indicated that prolonged cooking time at a low temperature (steaming for 6 h at 50°C ) was conducive to the optimal tenderness of Tibetan pork. This study provides a theoretical basis for improving the meat quality of Tibetan pork products and developing more rational processing methods.

Recent advances and challenges in the interaction between myofibrillar proteins and flavor substances.

Myofibrillar proteins are an important component of proteins. Flavor characteristics are the key attributes of food quality. The ability of proteins to bind flavor is one of their most fundamental functional properties. The dynamic balance of release and retention of volatile flavor compounds in protein-containing systems largely affects the sensory quality and consumer acceptability of foods. At present, research on flavor mainly focuses on the formation mechanism of flavor components, while there are few reports on the release and perception of flavor components. This review introduces the composition and structure of myofibrillar proteins, the classification of flavor substances, the physical binding and chemical adsorption of myofibrillar proteins and volatile flavor substances, as well as clarifies the regulation law of flavor substances from the viewpoint of endogenous flavor characteristics and exogenous environment factors, to provide a theoretical reference for the flavor regulation of meat products.

Effect of interaction between resveratrol and myofibrillar protein on the production of bound heterocyclic amines

To elucidate the pathways and mechanisms by which polyphenols inhibit protein-bound heterocyclic amines (HAs), the influence of resveratrol on bound/free HAs and the structure changes of myofibrillar proteins (MP) in the system of creatinine/MP/glucose model was studied. The results demonstrate that resveratrol significantly reduced bound and free HAs in the reaction systems (P < 0.05), and facilitates the transition from bound to free HAs. In addition, resveratrol altered the secondary structure of MP and had a static quenching effect on MP fluorescence. The strong interactions between resveratrol and MP are mainly hydrogen bonding and hydrophobic interactions. Furthermore, the results of molecular docking demonstrated that resveratrol exposed more hydrophobic amino acids (Ala, Lys and Pro) at the 556–578 amino acid sites of myosin. These results indicate that resveratrol controls the formation of bound HAs by reducing exposure to amino acids involved in the HAs reaction and promoting exposure to non-precursor amino acids.

Effect of three unsaturated fatty acids on the protein oxidation and structure of myofibrillar proteins from rainbow trout (Oncorhynchus mykiss)

In this study, the impact of three unsaturated fatty acids (Oleic acid: OA, Eicosapentaenoic acid: EPA, Docosahexaenoic acid: DHA) on the oxidation and structure of rainbow trout myofibrillar protein (MP) was explored. The findings revealed a notable increase in carbonyl content (P < 0.05) and a significant decrease in total sulfhydryl content (P < 0.05) of MP with the concentration increase of the three unsaturated fatty acids. Endogenous fluorescence spectroscopy and surface hydrophobicity analyses showed that unsaturated fatty acids can cause unfolding and exposure of hydrophobic groups in MP. In addition, SDS-PAGE showed that disulfide bonds were associated with MP cross-linking and aggregate size induced by unsaturated fatty acids. Overall, three unsaturated fatty acid treatments facilitated the oxidation of myofibrillar proteins, and the extent of protein oxidation was closely associated with the concentration of unsaturated fatty acids.

The impact of pressure-shift freezing on the three-dimensional network structure and properties of myofibrillar proteins in surimi gel derived from freshwater fish

Freezing treatment can prolong the shelf life of surimi products, but it will lead to deterioration of surimi gel quality. This study compared the effects of three different processing methods — non-freezing processing (control), conventional air freezing (CAF), and pressure-shift freezing (PSF) — on the three-dimensional (3D) network structure of grass carp surimi gel. After PSF treatment, the pores in the 3D gel network structure were denser compared to the control group which facilitates interaction of water and network structure. Furthermore, the ultraviolet and fluorescence spectral analysis indicated that PSF treatment mitigates the decline in stability of the tertiary structure of myofibrillar protein (MP) during freezing. The microstructure of MP showed that PSF treatment promotes the cross-linking of MP to form protein aggregates and then promotes the gelation of MP. Industrial relevancePSF can increase the commodity value of low-value freshwater fish products and has potential in the development of new products of surimi gels. This study reported a novel idea and theoretical basis for the application of PSF technology in the frozen food and aquatic product processing industry.

Effects of plasma-activated slightly acidic electrolyzed water on salmon myofibrillar protein: Insights from structure and molecular docking

The present study investigated the impact of plasma-activated water (PAW), slightly acidic electrolytic water (SAEW) and plasma-activated slightly acidic electrolytic water (PASW) treatment on myofibrillar protein (MP) in salmon fillets. Additionally, the interaction mechanism between myosin and reactive oxygen species was explored by molecular docking. Compared with the control group (719.26 nm), PASW treatment group exhibited the smallest particle size (408.97 nm). The PASW treatment exhibited efficacy in reducing MP aggregation and inhibiting protein oxidation. In comparison with other treatments, PASW treatment demonstrated a greater ability to mitigate damage to the secondary and tertiary structures of MP. O3 and H2O2 interact with myosin through hydrogen bonding. Specifically, O3 interacts with Lys676, Gly677, and Met678 of myosin while H2O2 binds to Thr681, Asp626, Arg680, and Met678. This study offers novel insights into the impact of PASW on MP, and provides a theoretical foundation for its application in aquatic product processing.

Cryoprotective effect of glycopeptide complex from abalone viscera on frozen surimi and its underlying mechanism

AbstractFreezing 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.

Exploring the impact of malondialdehyde and 4-hydroxy-2-nonena on myofibrillar protein structure: A proteomic analysis

In this investigation, the impacts of malondialdehyde (MDA), 4-hydroxy-2-nonena (HNE), and their combinations on the structural characteristics of myofibrillar proteins (MP) were examined using endogenous fluorescence, Fourier transform infrared spectrum (FTIR) and Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE). The potential binding mechanisms were also explored using LC-MS/MS and proteomics techniques. The findings indicated that various reactive carbonyl compounds (RCCs) displayed distinct oxidation performances in the oxidation of myofibrillar proteins. Samples containing HNE (HMP and MHMP groups) exhibited a more pronounced ability to oxidize MP than those containing MDA, as evidenced by their higher carbonyl content and lower sulfhydryl content. The MHMP group demonstrated the greatest surface hydrophobicity and Schiff base content but the lowest fluorescence intensity, suggesting that MDA and HNE synergistically altered MP conformation. Moreover, the alteration by RCCs notably modified the secondary structure of MP. Among these, HMP triggered the unfolding of MP molecules, resulting in the lowest α-helix and highest β-sheet ratio. The SDS‒PAGE results suggested that MDA oxidation promoted the crosslinking of MP molecules. At the same time, HNE caused the degradation of MP, as indicated by the decrease in the intensity of the high-molecular-weight bands. Proteomic analysis suggested that lysine residues distributed in the tail region of myosin were the main binding sites for MDA, whereas HNE preferentially modified methionine located at the myosin head. Additionally, HNE-induced protein degradation dominated RCC-induced oxidation reactions. These findings provide deeper insights into the mechanisms underlying quality changes induced by lipid oxidation products in MP-based food systems.

The underlying mechanism between emulsification stability and in vitro digestion in golden pompano (Trachinotus ovatus) myofibrillar protein-fish oil oleogel emulsion under ultrasonic treatments

Fish oil contains rich EPA and DHA, but their low absorption rate and bioavailability in the gastrointestinal tract limit their physiological activity. Ultrasonic treatments can modify the spatial structure of myofibrillar proteins and influence their function. The microstructure, viscoelastic properties, spatial conformation, size and charge, interfacial characteristics were investigated in the emulsions with fish oil oleogels to clarify the mechanism between emulsification stability and lipid digestion by ultrasonic treatment. The results showed that ultrasonic-treated (120 s or 150 W) fish myofibrillar protein had higher interfacial protein concentration and formed the more stable interfacial adsorption layer to wrap the fish oil oleogel with higher viscoelastic properties. The surface charge density was affected by adsorbed proteins, and higher interfacial adsorption capacity enhanced electrostatic repulsion and reduced the size. CLSM images also indicated that the droplet distribution was more uniform with smaller particle size. The increase in β-sheets facilitated interfacial adsorption and emulsion stability, and hydrophobic force and disulfide bonds promoted the interactions between myofibrillar protein and fish oil oleogel. In the stomach, the demulsification and flocculation occurred, and β-sheets increased along with hydrophobic forces and disulfide bonds, facilitating flocculation and aggregation as well as the increase in particle size. The electrostatic repulsion and spatial conformation altered the molecular interaction. In the intestine, the decreasing β-sheets, hydrophobic force and disulfide bonds were conducive to the adsorption of bile salts and lipase/colipase. Hence, ultrasonic treatments simultaneously enhanced emulsion stability and lipid digestion.

Changes in properties of myofibrillar protein and myofibrillar protein gel from freshwater fish after low-temperature and high-pressure collaborative treatment

This study investigated the effects of low-temperature and high-pressure collaborative and conventional air freezing (CAF) on myofibrillar protein (MP) characteristics from grass carp. Turbidity, solubility, and particle size analysis showed that the pressure shift freezing (PSF) treatment could inhibit the formation of large MP aggregates to a certain extent during freezing. Chemical interaction studies unveiled that PSF treatment not only mitigates damage to the inherent structure of MP during freezing but also enhances its crosslinking ability. Microstructure analysis revealed a densely woven fibrous protein network structure within the MP gel in the PSF group. MP gel with fiber shape network structure in the PSF group exhibited stronger water-holding capacity and mechanical properties compared to the CAF group having an incomplete protein network structure. This suggests that the combined application of low-temperature and high-pressure treatment holds promising potential for utilization in the surimi gel processing industry and aquatic products processing.Industrial relevance: The quality and safety of food are closely related to the commodity value of food. Combined low-temperature and high-pressure treatment can enhance the commodity value of low-value freshwater fish products and has potential in surimi gel new product development. This study provides theoretical guidance for high-pressure and low-temperature collaborative processing and industrial production of related aquatic products.

Effect of low-frequency alternating magnetic fields on the physicochemical, conformational and rheological properties of myofibrillar protein after iterative freeze-thaw cycles

In this work, the effects of low-frequency alternating magnetic fields (LF-AMF) on the physicochemical, conformational, and functional characteristics of myofibrillar protein (MP) after iterative freeze-thaw (FT) cycles were explored. With the increasing LF-AMF treatment time, the solubility, active sulfhydryl groups, surface hydrophobicity, emulsifiability, and emulsion stability of MP after five FT cycles evidently elevated and then declined, and the peak value was obtained at 3 h. Conversely, the moderate LF-AMF treatment time can significantly reduce the average particle size, carbonyl content, and endogenous fluorescence intensity of MP. The rheology results showed that various LF-AMF treatment times would elevate the G' value of MP after iterative FT cycles. The FTIR spectroscopy results suggested that LF-AMF influenced the secondary structure of MP after multiple FT cycles, resulting in a depression in α-helix content and an increment in β-folding proportion. Moreover, LF-AMF treatment induced the gradually lighter and wider myosin heavy chain bands of MP, implying that LF-AMF accelerated the degradation of macromolecular aggregates. Therefore, the LF-AMF treatment efficaciously ameliorates the structural and functional deterioration of MP after iterative FT cycles and could be used as a potential quality-improving technology in the frozen meat industry.

Low-frequency alternating magnetic field and CaCl2 influence the physicochemical, conformational and gel characteristics of low-salt myofibrillar protein

In this study, the improvement mechanism of low-frequency alternating magnetic field (LF-AMF, 5 mT, 3 h) combined with calcium chloride (CaCl2, 0–100 mM) on the gel characteristics of low-salt myofibrillar protein (MP) was investigated. LF-AMF combined with 80 mM CaCl2 treatment increased solubility (32.71%), surface hydrophobicity (40.86 μg), active sulfhydryl content (22.57%), water-holding capacity (7.15%). Besides, the combined treatment decreased turbidity, particle size and intrinsic fluorescence strength of MP. Fourier transform infrared spectroscopy (FT-IR) results indicated that the combined treatment altered the secondary structure of MP by increasing β-sheet and β-turn, and reducing α-helix and random coil. The combined treatment also induced a high G' value and shortened T2 relaxation time for forming a homogeneous and compact gel structure. These results revealed that LF-AMF combined CaCl2 treatment could as a potential approach for modifying the gel characteristics of low-salt MP.

Cryoprotective effect of tamarind seed polysaccharide on grass carp surimi: characteristics, interactions, and mechanisms

In surimi products, the quality deterioration caused by freezing is a common problem. Therefore, the development of natural cryoprotectants is receiving increased attention. Tamarind seed polysaccharide (TSP) has been found to have a superior ice recrystallization inhibitory effect. In this work, the cryoprotective effect of TSP on grass carp surimi was investigated, including freeze-thaw stability, water distribution, texture, and microstructure. Additionally, the interaction between TSP and myofibrillar protein was analyzed. The inclusion of TSP resulted in the formation of a more regular and compact gel network through hydrogen bonding, which enhanced the binding between water molecules and myofibrillar protein. This, in turn, immobilized free water within the gel network. Furthermore, TSP prevented the texture deterioration of the surimi gel during repeated freeze-thaw cycles, particularly when 1.0% TSP was added. Moreover, the presence of TSP delayed the decline of Ca2+-ATPase activity and stabilized the secondary, tertiary, and quaternary structure of myofibrillar protein during freeze-thaw cycles. Therefore, TSP shows promise as a potential cryoprotectant for frozen surimi products, enhancing their quality and stability during frozen storage.

Structural and functional properties of protein hydrolysates from myofibrillar protein of crocodile (Crocodylus siamensis) meat

In this study, three proteases (papain, neutral protease, bromelain) were employed to hydrolyze crocodile (Crocodylus siamensis) myofibrillar protein (MP), effects of hydrolysis duration on functional and structural properties of MP hydrolysates was investigated. The findings revealed that solubility of all hydrolysates exceeded 60%, with the highest reaching 96.7%. The emulsifying activity of neutral protease hydrolysates exhibited a significant superiority over the other two hydrolysates (P < 0.05). The Fe2+ chelating and DPPH radical scavenging activity of hydrolysates ranged from 20% to 60%, and 60%–90%, respectively. Based on the experiment results, the hydrolysates of papain at 1h, neutral protease at 1h, and bromelain at 2h were used for structural analysis. Compared to MP, the secondary structure of hydrolysates showed a reduction of 9.6%, 15.2%, and 4.7% in α-helix and the increase of 42.4%, 29.6%, and 44.2% in β-fold content of papain, neutral protease and bromelain hydrolysates respectively, suggesting the transition from spiral to folding structure and the exposure of hydrophobic group, which was proved by free amino acid analysis. SEM results confirmed the alterations in MP structure. The molecular weight distributions of three hydrolysates were predominantly below 1000 Da, demonstrating that crocodile MP was effectively hydrolyzed into bioactive peptides.

Oxidation affects pH buffering capacity of myofibrillar proteins via modification of histidine residue and structure of myofibrillar proteins

The pH buffering capacity is an important functionality of muscle proteins, and muscle foods are susceptible to being oxidized during storage and processing. In order to study the effect of oxidation on the pH buffering capacity of myofibrillar proteins, myofibrils extracted from snakehead fish (Channa argus) were oxidized with H2O2. Results showed that increased oxidation led to loss of free sulfhydryl groups, formation of carbonyl groups, increased surface hydrophobicity, and aggregation of myofibrillar proteins. In addition, there was a significant reduction in the content of histidine in oxidized myofibrillar proteins. The pH buffering capacity of myofibrillar proteins significantly decreased from 3.14 ± 0.03 mM H+/(mL × ΔpH) down to 2.55 ± 0.03 mM H+/(mL × ΔpH) after oxidation with 50 mM H2O2. Both oxidized myofibrillar proteins and histidine showed a high pH buffering capacity at pH near 5.8, which is the histidine pKa value. Here, we hypothesize that oxidation-induced changes in the pH buffering capacity of myofibrillar proteins were driven by oxidative modification of histidine and structural changes of myofibrillar proteins. The significance of this study to food industry may be the awareness that protein oxidation may affect pH through changes in buffering capacity. And the use of antioxidants, especially those targeting at histidine will be promising in addressing this issue.