Dityrosine Content Research Articles

Mechanism of Toona sinensis seed polyphenols inhibiting oxidation and modifying physicochemical and gel properties of pork myofibrillar protein under oxidation system

This research aimed to elucidate how Toona sinensis seed polyphenols (TSSs) inhibited pork myofibrillar protein (MP) oxidation and modified physicochemical and gel properties in the Fenton oxidation system. Our result displayed that TSSs had a lower carbonyl (from 1.38 to 0.59 nmol/mg) and dityrosine contents (from 47.22 to 25.07), and higher free amino content (from 386.99 to 485.00 nmol/mg), followed by ellagic acid (EA) and quercetin-3-O-rhamnoside (QC). Meanwhile, the incorporation of phenolic compounds changed secondary and tertiary structure of proteins and then increased solubility and absolute value of zeta potential, as well as decreased turbidity and average particle size. Molecular docking indicated that MP interacted with EA primarily via hydrogen bonds and hydrophobic interaction, and with QC mostly through hydrogen bonds and electrostatic interaction. Otherwise, the incorporation of EA promoted MP gel to form a honeycomb-like microstructure after oxidation. Therefore, TSSs, EA, and QC could significantly inhibit MP oxidation as well as modify its physicochemical properties, but only EA enhanced its gel properties after oxidation. The results could be useful to improve the comprehensive utilization of plant by-products and provide theoretical references for the role of TSSs in the improvement of meat products.

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.

The effect of polysaccharide type on dielectric barrier discharge (DBD) plasma glycosylation of sodium caseinate-part I: Physicochemical, structural and thermal properties

This study aimed to investigate the impact of polysaccharide type on the physicochemical, structural, and thermal properties of dielectric barrier discharge (DBD) plasma glycosylated sodium caseinate (SC). The polysaccharides Quince seed gum (QSG), carboxymethyl cellulose (CMC), and maltodextrin (MD) were mixed with SC and treated with DBD plasma at 18 kV for 10 min. The grafting degree, electrophoresis pattern, FTIR, XRD, carbonyl, sulfhydryl, and di-tyrosine content, FE-SEM, color, and thermal properties of SC and its polysaccharide mixtures before and after plasma treatment were analyzed. Results showed that the SC-QSG conjugate had the highest glycation degree and color change after plasma treatment. The SC-CMC and SC-QSG conjugates exhibited disappearance of distinct SC bands in electrophoresis pattern compared to SC. Also, significant changes in functional group and crystallinity were occurred in SC-CMC conjugate. Plasma treatment caused oxidation of SC, but the presence of polysaccharides offered protection against oxidation. The microstructure of SC was altered by mixing with polysaccharides and exposure to plasma. Also, the mixtures indicated higher thermal stability after plasma treatment. Results confirmed that the generation of protein-polysaccharide conjugates through DBD plasma technique was depended on with SC-MD conjugate unable to form through this method.

Role of ultrasonic freezing­treated pork dumpling filling during frozen storage: Insights from protein oxidation, aggregation, and functional properties

The effects of air freezing (AF), immersion freezing (IF), and ultrasonic freezing (UF) on the oxidation, aggregation, and functional properties of myofibrillar protein (MP) in pork dumpling filling during frozen storage were investigated. The findings demonstrated that, compared to AF and IF treatments, UF treatment had higher total and reactive sulfhydryl content, solubility, and absolute zeta potential. Conversely, it exhibited lower values in carbonyl content, dityrosine content, turbidity, and particle size within the same storage time (p < 0.05). SDS-PAGE revealed that UF treatment delayed the oxidation and excessive aggregation of MP during frozen storage. Moreover, samples treated with UF at 180 days (d) displayed similar functional and qualitative characteristics to those treated with IF at 90 d or AF at 60 d, as per the hierarchical cluster analysis findings. In conclusion, UF effectively delayed the oxidation, aggregation, and loss of functional properties of MP in pork dumpling filling during frozen storage.

Inhibitive effect of trehalose and sodium pyrophosphate on oxidation and structural changes of myofibrillar proteins in silver carp surimi during frozen storage

This work investigated the cryoprotective effect of trehalose (TH) and sodium pyrophosphate (SPP) alone and in combination on myofibrillar protein (MP) oxidation and structural changes in silver carp surimi during 90 days of frozen storage (-20 °C). TH combined with SPP was significantly more effective than single TH or SPP in preventing MP oxidation (P < 0.05), showing a higher SH content (6.05 nmol/mg protein), and a lower carbonyl (4.24 nmol/mg protein) and dityrosine content (1280 A.U.). SDS-PAGE results indicated that TH combined with SPP did not differ significantly from TH and SPP in inhibiting protein degradation but was more effective in inhibiting protein crosslinking. Moreover, all cryoprotectants could stabilise the secondary and tertiary structures and inhibit unfolded and aggregation of MP, with the combination of TH and SPP being the best. It's worth noting that TH combined with SPP had a synergistic effect on inhibiting the decrease in α-helix content and gel-forming ability, and the increase in surface hydrophobicity. Overall, TH combined with SPP could significantly inhibited MP oxidation and structural changes in surimi during frozen storage and improve the gel-forming ability, which was significantly better than single TH or SPP.

Incorporating ε-polylysine hydrochloride, tea polyphenols, nisin, and ascorbic acid into edible coating solutions: Effect on oxidation and structure of marinated egg proteins

Egg processing products lose their attraction due to protein oxidation and degradation, while the edible coating incorporating antioxidant and antimicrobial agents can address this deficit. In this work, chitosan (CS) in combination with ε-polylysine hydrochloride, tea polyphenols, nisin, and vitamin C (CS–NH-TC) was applied as a novel edible coating material for preserving marinated eggs for 20 days and its effects on egg quality, and protein oxidation and structure were determined. The CS–NH–TC coating exhibited the highest antioxidant and antibacterial activities among all coatings. Compared to uncoated marinated eggs (Sulfhydryl: 12.02 μmol/g, dityrosine: 6251.8, protein hydrophobicity: 3691, turbidity: 0.13 mg/mL, particle size: 342.13 nm), CS- and CS–NH–TC-coated eggs exhibited improved protein stability, as evidenced by a higher sulfhydryl (22.20 and 30.92 μmol/g) and lower dityrosine content (4722 and 4216), protein hydrophobicity (2891.72 and 865.75), turbidity (0.06 and 0.03 mg/mL), and particle size (292.06 and 256.57 nm). Additionally, edible coatings, especially CS–NH–TC coatings, were positively correlated with smaller intermolecular force changes in marinated eggs, corresponding to suppressed protein oxidation and conformational changes. Furthermore, CS–NH–TC-coated samples showed more stable protein secondary structures and less disorderly and aggregated protein microstructure, and better color, texture, and sensory scores. Our study could provide a theoretical basis for stabilizing the protein structure of egg processing products.

The Protection of Quinoa Protein on the Quality of Pork Patties during Freeze-Thaw Cycles: Physicochemical Properties, Sensory Quality and Protein Oxidative.

The present study investigated the impact of quinoa protein (QP) on the physicochemical properties, sensory quality, and oxidative stability of myofibrillar protein (MP) in pork patties during five freeze-thaw (F-T) cycles. It was observed that repeated F-T cycles resulted in a deterioration of pork patty quality; however, the incorporation of QP effectively mitigated these changes. Throughout the F-T cycles, the sensory quality of the QP-treated group consistently surpassed that of the control group. After five F-T cycles, the thiobarbituric acid reactive substance (TBARS) content in the control group was measured at 0.423 mg/kg, whereas it significantly decreased to 0.347 mg/kg in the QP-treated group (p < 0.05). Furthermore, QP inclusion led to a decrease in pH and an increase in water-holding capacity (WHC) within pork patties. Following five F-T cycles, Ca2+-ATPase activity exhibited a significant increase of 11.10% in the QP-treated group compared to controls (p < 0.05). Additionally, supplementation with QP resulted in elevated total sulfhydryl content and reduced carbonyl content, Schiff base content, and dityrosine content within myofibrillar proteins (MPs), indicating its inhibitory effect on MP oxidation. In particular, after five F-T cycles, total sulfhydryl content reached 58.66 nmol/mL for the QP-treated group significantly higher than that observed for controls at 43.65 nmol/mL (p < 0.05). While carbonyl content increased from 2.37 nmol/mL to 4.63 nmol/mL between the first and fifth F-T cycle for controls; it only rose from 2.15 nmol/mL to 3.47 nmol/mL in the QP-treated group. The endogenous fluorescence levels were significantly higher (p < 0.05) in the QP-treated group compared to controls. In conclusion, the addition of QP enhanced the quality of pork patties and effectively inhibited the oxidative denaturation of MP during F-T cycles.

Textural dynamic crisping mechanism of crisp grass carp: Oxidative stress, apoptosis, collagen filling, and cross‐linking

AbstractFeeding faba beans to freshwater fish could crisp its muscle texture to avoid softening. However, the dynamic crisping mechanism was unclear. Herein, a 120‐day feeding trial was conducted to systemically investigate the textural crisping mechanism of crisp grass carp (CGC) via molecular‐level, gene/protein expression analysis. In the early crisping stage (0–30 days), the total antioxidant capacity significantly decreased (by 16.79%), TUNEL staining and qRT‐PCR results revealed that apoptosis occurred, which was induced by oxidative stress validating by proteomics. Meanwhile, the content of dityrosine and hydroxylysyl pyridinoline rose, thereby substantially increasing the hardness and chewiness of CGC by 37.51% and 40.84%, respectively. With further crisping (30–90 days), Masson staining exhibited collagen gradually filling the gap between myofibrils, the content and cross‐linking degree of collagen further increased, finally elevating the hardness and chewiness of CGC. This study laid a theoretical foundation for producing and supplying aquatic raw materials with different texture characteristics.

Effects of Edible Organic Acid Soaking on Color, Protein Physicochemical, and Digestion Characteristics of Ready-to-Eat Shrimp upon Processing and Sterilization

Soft-packed ready-to-eat (RTE) shrimp has gradually become popular with consumers due to its portability and deliciousness. However, the browning caused by high-temperature sterilization is a non-negligible disadvantage affecting sensory quality. RTE shrimp is processed through “boiling + vacuum soft packing + high temperature and pressure sterilization”. Ultraviolet-visible (UV) spectroscopy with CIELAB color measurement showed that phytic acid (PA) + lactic acid (LA), PA + citric acid (CA), and PA + LA + CA soaking before cooking alleviated browning, as well as UVabsorbance and the browning index (BI). Meanwhile, UV spectroscopy and fluorescence spectroscopy showed that organic acid soaking reduced the content of carbonyl, dityrosine, disulfide bonds, surface hydrophobicity, and protein solubility, but promoted the content of free sulfhydryl and protein aggregation. However, in vitro digestion simulations showed that organic acid soaking unexpectedly inhibited the degree of hydrolysis and protein digestibility. This study provides the basis for the application of organic acids as color protectors for RTE aquatic muscle product.

Protein oxidation/aggregation during ultrasound thawing at different powers impair the gel properties of common carp (Cyprinus carpio) myofibrillar protein

The influences of ultrasound thawing (UT) at different power (0, 100, 300, and 500 W) on the oxidation, aggregation, and gel properties of common carp (Cyprinus carpio) myofibrillar protein were evaluated in the present study. The free amino content, carbonyl content, dityrosine content, and TBARS value of UT-300 were significantly lower than those of other thawing groups (P < 0.05), suggesting that appropriate ultrasound power (300 W) thawing inhibited the oxidation of myofibrillar protein and fat. However, excessive power (500 W) UT enhanced the oxidation of fish protein. UT-300 had the smallest surface hydrophobicity, particle size, and turbidity values, indicating that UT-300 reduced protein aggregation caused by thawing. At the same time, UT-300 protein gel had a higher gel strength and water-holding capacity than other thawing treatments, which were characterized by fine and uniform gel networks. Water distribution analysis also proved that UT-300 inhibited the loss of bound water, free water, and immobilized water, as well as the increase in fluidity caused by thawing. In conclusion, proper power (300 W) UT was beneficial in inhibiting the degradation of gel properties caused by protein oxidation and aggregation during thawing.

Oxidative behaviour, aggregation and structural properties of silver carp myofibrillar proteins with different molecular states subjected to freeze–thaw process

SummarySilver carp myofibrillar proteins (MP) with different moleculars states were constructed by the addition of NaCl and fracture degree of muscle fibres. Results showed that salt‐dissolved MP (P+) under unfrozen and oxidised state showed higher oxidation degree with higher carbonyl (3.42 nmol mg−1) and dityrosine contents (25.98 a.u.) (P &lt; 0.05) compared with saltless‐polymeric MP (P) and salt‐induced swelling MP (F+) due to addition of salt and broken muscle fibres. After oxidative and freeze–thaw process, P+ group also exhibited more cross‐linking as evidenced by turbidity (0.73), solubility (64.96%) and SDS‐PAGE, but unordered aggregates in P group increased probably due to severe frozen denaturation. Moreover, F+ group of salt‐induced swelling MP from intact muscle fibres suffered less structural damages with higher fluorescence intensity (668.41 a.u.) and higher α‐helix contents (15.56%). Overall, Fish‐ Hua of salt‐dissolved MP had a higher oxidation level and NaCl contributed to improve freeze–thaw stability of MP during freeze–thaw process.

Changes in the structure and hydration properties of high-temperature peanut protein induced by cold plasma oxidation

To improve the hydration properties of high-temperature pressed peanut protein isolate (HPPI), we investigated the effect of cold plasma (CP) oxidation on functional and structural properties. Compared to HPPI, the hydrated molecules number and the surface contact angle were significantly decreased at 70 W, from 77.2 × 109 to 17.7 × 109 and from 85.74° to 57.81°, respectively. The reduction of the sulfhydryl content and the increase of the disulfide bond and di-tyrosine content indicated that the structural transformation was affected by the oxidation effect. In terms of structural changes, a stretched tertiary structure, ordered secondary structure, and rough apparent structure were observed after CP treatment. Additionally, the enhancement of surface free energy and group content such as -COOH, -CO and -OH on the surface of HPPI contributed to the formation of hydrated crystal structures. In general, the oxidation effect of CP effectively improved the hydration properties of HPPI and broaden its application field.

Influence of atmospheric pressure plasma jet on the structural, functional and digestive properties of chickpea protein isolate

Chickpea protein (CPI) is a promising dietary protein and potential substitute for soy protein in food product development due to its high protein content and low allergenicity. However, CPI possesses denser tertiary and quaternary structures and contains certain amount of anti-nutritional factors, both of which constrain its functional properties and digestibility. The objective of this study was to assess the effectiveness of atmospheric pressure plasma jets (APPJ) as a non-thermal method for enhancing the functional characteristics and digestibility of CPI. In this study, the reactive oxygen and nitrogen species generated by the APPJ treatment led to protein oxidation and increased carbonyl and di-tyrosine contents. At the same time, the secondary, tertiary and microstructural structures of CPI were changed. The solubility, water holding capacity, fat absorption capacity, emulsifying capacity and foaming capacity of CPI were significantly improved after 30 s APPJ treatment, and a higher storage modulus in rheology was observed. Additionally, it was observed that the in vitro protein digestibility (IVPD) of APPJ-treated CPI increased significantly from 44.85 ± 0.6 % to 50.2 ± 0.59 % following in vitro simulated gastric and intestinal digestion, marking a noteworthy improvement of 11.93 %. These findings indicate that APPJ processing can enhance the functional and digestive properties of CPI through structural modification and expand its potential applications within the food industry.

Quinoa protein Pickering emulsion improves the freeze-thaw stability of myofibrillar protein gel: Maintaining protein composition, structure, conformation and digestibility and slowing down protein oxidation

In this work, the effects of quinoa protein Pickering emulsion (QPPE) on protein oxidation, structure and gastrointestinal digestion property of myofibrillar protein gels (MPGs) after freeze-thaw (F-T) cycles are revealed. SDS-PAGE results indicated that 5.0 %–10.0 % QPPE addition slowed down the protein degradation. Meanwhile, 5.0 %–7.5 % QPPE maintained the stability of the protein secondary and tertiary structure of MPGs after F-T cycles. The sulfhydryl group, disulfide bond and dityrosine content increased with QPPE supplementation. The conformations of disulfide bond changed from g-g-t and t-g-t to g-g-g after F-T cycles, and 5.0 %–7.5 % QPPE stabilized the changes of t-g-t conformation. Furthermore, the increase of dityrosine content after F-T cycles was significantly reduced with 7.5 % QPPE addition, indicating its effect to slow down protein oxidation of MPGs. In addition, MPGs with 5.0 % and 7.5 % QPPE showed noticeably higher zeta potential values than other groups, indicating the enhanced electrostatic repulsion and weakened aggregation caused by F-T damage. This work showed that 7.5 % QPPE improved the F-T stability of MPGs and reduced the protein denaturation and oxidation caused by F-T treatments, exerting no side effect on the digestion property of MPGs. QPPE can be used as a green and effective antifreeze in meat industry.

Complex organic acids treatment on crayfish (Procambarus clarkii): the relationship between myofibrillar protein structure and meat quality

SummaryThe effect of complex organic acids (COA) treatment at different concentrations (0%, 1%, 5%, 10% and 15%) on the myofibrillar protein (MP) structure and meat quality of crayfish (Procambarus clarkii) was investigated. The results showed that with increasing concentrations of COA treatment, the sulfhydryl content of MP decreased and dityrosine content increased. The MP secondary structure has a reduced α‐helix content and an increased β‐fold content. The MP tertiary structure unfolded, exposing hydrophobic and other amino acids to a polar environment. MP aggregation was induced in the 1% and 5% COA treatment groups and MP degradation was induced in the 10% and 15% COA treatment groups. Crayfish meat in the 5% COA treatment group showed improved textural properties due to protein aggregation. It also enhanced the colour, aroma and micromorphology of the crayfish meat.

ROS-driven structural and functional fibrinogen modifications are reverted by interleukin-6 inhibition in Giant Cell Arteritis

BackgroundCranial and extra-cranial vascular events are among the major determinants of morbidity and mortality in Giant Cell Arteritis (GCA). Vascular events seem mostly of inflammatory nature, although the precise pathogenetic mechanisms are still unclear. We investigated the role of oxidation-induced structural and functional fibrinogen modifications in GCA. The effects of the anti-IL6R tocilizumab in counteracting these mechanisms were also assessed. Materials and methodsA cross-sectional study was conducted on 65 GCA patients and 65 matched controls. Leucocyte reactive oxygen species (ROS) production, redox state, and fibrinogen structural and functional features were compared between patients and controls. In 19 patients receiving tocilizumab, pre vs post treatment variations were assessed. ResultsGCA patients displayed enhanced blood lymphocyte, monocyte and neutrophil ROS production compared to controls, with an increased plasma lipid peroxidation and a reduced total antioxidant capacity. This oxidative impairment resulted in a sustained fibrinogen oxidation (i.e. dityrosine content 320 (204–410) vs 136 (120–176) Relative Fluorescence Units (RFU), p < 0.0001), with marked alterations in fibrinogen secondary and tertiary structure [intrinsic fluorescence: 134 (101–227) vs 400 (366–433) RFU, p < 0.001]. Structural alterations paralleled a remarkable fibrinogen functional impairment, with a reduced ability to polymerize into fibrin and a lower fibrin susceptibility to plasmin-induced lysis. In patients receiving tocilizumab, a significant improvement in redox status was observed, accompanied by a significant improvement in fibrinogen structural and functional features (p < 0.001). ConclusionsAn impaired redox status accounts for structural and functional fibrinogen modifications in GCA, suggesting a potential role of tocilizumab for cardiovascular prevention in GCA.

Effects of protein and lipid oxidation on the water holding capacity of different parts of bighead carp: Eye, dorsal, belly and tail muscles

The quality of fish can change due to differences in the lipid and protein oxidation rates in different muscles. This study examined vacuum-packed eye muscle (EM), dorsal muscle (DM), belly muscle (BM), and tail muscle (TM) of bighead carp frozen for 180 days. The results reveal that EM had the highest lipid content and the lowest protein content, while DM had the lowest lipid content and the highest protein content. EM also showed the highest values of centrifugal loss and cooking loss, and the correlation analysis showed that these losses were positively correlated with dityrosine content and negatively correlated with conjugated triene content. The content of carbonyl, disulfide bond, and surface hydrophobicity of myofibrillar protein (MP) also increased with time, with DM having the highest values. The microstructure of EM was looser than other muscles. Therefore, DM had the fastest oxidation rate and EM had the lowest water holding capacity.

Effect of air frying and baking on physicochemical properties and digestive properties of scallop (Patinopecten yessoensis) adductor muscle

In this study, the effects of dry heat treatments including air frying and baking on the physicochemical and digestive properties of proteins in scallop adductor muscle (SAM) were evaluated. After heat treatments, the proteins in SAM exhibited different degrees of oxidation, aggregation and degradation. For both heat treatments, the increase of carbonyl and dityrosine contents and the decrease of free sulfhydryl groups and surface hydrophobicity of proteins in SAM were observed along with increasing heat temperature. Meanwhile, with increasing heat temperature, there was a progressive transition from α-helix to β-sheet in protein secondary structure. However, the protein solubility first increased and then decreased with increasing temperature. Among which, the solubility of 160°C-treated samples was the highest, which were 21.02% and 20.32% for air frying and baking. The protein digestive properties which reflected by the degree of hydrolysis (DH), soluble amino groups and soluble peptides showed a trend of increasing first and then decreasing with increasing temperature. After gastrointestinal digestion, the DH, soluble amino groups and soluble peptides of 160°C-treated SAMs cooking by air frying were 69.96%, 61.14% and 39.33%, respectively, which were significantly higher than all other samples including the fresh ones. Correlation analysis showed that the protein digestive indexes were positively correlated with solubility, free sulfhydryl content and surface hydrophobicity, and negatively correlated with protein carbonyl content, dityrosine content and protein aggregation degree. These results provide evidence for knowing more about the effects of dry heat treatments on physicochemical and digestive properties of aquatic muscle food.

Quality of chicken breast meat improved by dietary pterostilbene referring to up-regulated antioxidant capacity and enhanced protein structure

This research aimed to investigate the effects of dietary pterostilbene supplementation on meat quality, myofibrillar protein (MP) structure and antioxidant capacity of broiler chicken. The results showed that pterostilbene increased pH24h, redness a*24h, water-holding capacity, and decreased yellowness b*24h and shear force of chicken meat; it also raised the crude protein, non-essential amino acid and flavor amino acid content in muscle. Pterostilbene increased Ca2+-ATPase activity and the α-helical ratio in muscle MP, accompanied by decreased dityrosine content and protein particle size, suggesting that pterostilbene addition effectively improved the MP structure. These alterations caused by dietary pterostilbene might be partially associated with the enhanced total superoxide dismutase, catalase and glutathione peroxidase activities regulated by genes relating to the Nrf2 signaling pathway, as well as reduced lipid and protein oxidation. Together, pterostilbene could be used as a promising dietary supplement for enhancing the organoleptic quality and nutritional value of chicken meat.

Effects of ultra high pressure-magnetic field treatment on protein properties and quality characteristics of stored shrimp (LitopenaeusVannamei)

The preservation of ultra high pressure (UHP) and magnetic field (MF) technologies on food have been reported, but the effect of combined treatment (UHP-MF) on aquatic product quality is rarely explored. The purposes of this study were to investigate the effects of UHP-MF treatment on protein properties and quality deterioration of stored Litopenaeus Vannamei. The vacuum-packed shrimps were treated at 200 and 300 MPa for 5 min, then stored in 5 mT MF for 12 days. Results showed the hardness, springiness, chewiness, shear force, L*, a*, b*, and W of muscle were improved by UHP, whereas the texture softening, a* and b* increase, water holding capacity were inhibited during MF storage. On the 12th day, compared with CON group, the cathepsin B, D, H, L activities, TBARS, carbonyl and dityrosine content in UHP300-MF group were reduced by 46.67%, 27.26%, 43.10%, 52.00%, 41.30%, 32.86%, and 30.42%, respectively. Furthermore, UHP-MF treatment slow down the accumulation of surface hydrophobicity, myofibril fragmentation index, and trichloroacetic acid-soluble peptide content. Generally, UHP-MF treatment inhibited lipid oxidation, weakened cathepsin activities, delayed protein oxidation and degradation of stored shrimp, retarded quality deterioration and prolonged shelf life of stored shrimp.