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The study constructed a model of temperature fluctuation (TF, -20 °C âˆ¼ -10 °C) during frozen status to build a link between the tilapia fillets muscle of ice crystal morphology, moisture distribution, protein oxidation index and the edible quality. When TF treatment more than 3 times, the brightness, color and hardness of frozen tilapia fillets decreased significantly, and the cooking loss and thawing loss increased significantly. The free and unconjugated water in frozen fish fillets exceeded 97 % and did not change much after 9 times TF. The K and TVB-N values were within the safety standards (K < 60 %, TVB-N < 30 mg N/100 g). The ice crystals in the tissues were significantly increased. Protein carbonyls and Ca2+-ATPase were significantly reduced, and secondary structures were irregular. Network correlation analysis showed that ice crystal morphology was significantly correlated with the color, texture and protein oxidation index of frozen tilapia fillets. The results would provide theoretical approach for the transportation and sales of tilapia industrial enterprises.

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This study aimed to investigate the effect of oxidation on fish gelatin and its emulsifying properties. Fish gelatin was oxidized with varying concentrations of H2O2 (0-30 mM). Increased concentrations of the oxidant led to a decrease in amino acids in the gelatin, including glycine, lysine, and arginine. Additionally, the relative content of ordered secondary structure and triple helix fractions decreased. Zeta potential decreased, while particle size, surface hydrophobicity, and water contact angle increased. Regarding emulsifying behavior, oxidation promoted the adsorption of gelatin to the oil-water interface and reduced interfacial tension. With increased degrees of oxidation, the zeta potential and size of the emulsion droplets decreased. The oxidized gelatin exhibited better emulsifying activity but worse emulsifying stability. Based on these results, a mechanism for how oxidation affects the emulsifying properties of gelatin was proposed: the increase in gelatin's hydrophobicity and the decrease in triple helix structure induced by oxidation reduced the interfacial tension at the oil-water interface. This promoted protein adsorption at the oil-water interface, allowing the formation of smaller oil droplets and enhancing gelatin's emulsifying activity. However, the decrease in electrostatic repulsion between emulsion droplets and the decrease in solution viscosity increased the flocculation and aggregation of oil droplets, ultimately weakening the emulsifying stability of gelatin.

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This study explored the intrinsic relationship between the quality traits and protein-related property changes during the solar drying of shrimps (Penaeus vannamei). During drying, the shrimp exhibited a gradual decline in L*a*b* values and a notable increase in the hardness and chewiness. Proteins were degraded and oxidized. Especially, the trichloroacetic acid-soluble peptide and carbonyl contents increased, whereas the total sulfhydryl content decreased. The proportions of different types of intramolecular bonds were significantly changed. The ionic and hydrogen bonds greatly decreased to 10.72% and 9.05% and the hydrophobic and disulfide bonds notably increased to 19.38% and 28.19%, indicating the changes in the spatial structure of the protein and its denaturation during the drying process. The Pearson's correlation analysis showed that protein degradation and denaturation greatly affected the textural properties and protein oxidation caused color changes. The result of this work provides a theoretical support for improving the quality of shrimp products.

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In the brewing process, methionine is a decisive amino acid for (off-)flavor formation. A significant part of methionine is oxidized to methionine sulfoxide (MetSO) in malt. We hypothesized that MetSO and MetSO2 are metabolized to volatile compounds during yeast fermentation and examined whether the yeast Saccharomyces cerevisiae is able to catabolize l-MetSO and l-MetSO2 in free and dipeptide-bound forms. We also investigated the stability of l-methionine sulfoximine and S-methylmethionine. Cell viability in the presence of the test compounds was at least 90%. Both free and peptide-bound test substances were metabolized by Saccharomyces cerevisiae. l-MetSO was degraded most rapidly as the free amino acid, while l-MetSO2 was degraded most rapidly bound in dipeptides. We observed a different degradation behavior of the (R) and (S) diastereoisomers for l-MetSO and l-methionine sulfoximine. Furthermore, we detected methionol as the only metabolite of MetSO. Methionol sulfoxide was not formed. MetSO2 was not converted to methionol or methionol sulfone but to the respective α-hydroxy acid. We conclude that the reduction of MetSO to methionine proceeds faster than transamination. The occurrence of MetSO or MetSO2 in brewing malt will not lead to the formation of hitherto unknown volatile metabolites of the Ehrlich pathway.

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To clarify the nutritional mechanisms of quercetin mitigation in the digestive and absorptive functions in rats fed protein-oxidized soybean meal, 48 three-week-old male SD rats were randomly allocated into a 2 × 2 factorial design with two soybean meal types (fresh soybean meal or protein-oxidized soybean meal) and two quercetin levels (0 or 400 mg/kg) for a 28-day feeding trial. The protein-oxidized soybean meal treatment decreased (p < 0.05) the relative weights of the pancreas, stomach, and cecum, duodenal villus height, pancreatic and jejunal lipase activities, apparent ileal digestibility of amino acids, and apparent total tract digestibility of dry matter, crude protein, and ether extract. The supplementation of quercetin in the protein-oxidized soybean meal diet reversed (p < 0.05) the decreases in the duodenal length, ileal villus height, lipase activity, apparent ileal digestibility of amino acids, and apparent total tract digestibility of dry matter, crude protein, and ether extract. Transcriptomics revealed that the "alanine transport" and "lipid digestion and absorption" pathways were downregulated by the protein-oxidized soybean meal compared with fresh soybean meal, while the "basic amino acid transmembrane transporter activity" and "lipid digestion and absorption" pathways were upregulated by the quercetin supplementation. Microbiomics revealed that the protein-oxidized soybean meal increased the protein-degrading and inflammation-triggering bacteria in the cecum, while the relative abundances of beneficial bacteria were elevated by the quercetin supplementation.

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Fried oyster is a popular aquatic food product in East Asia, but nutrient loss during thermal processing become a significant concern. The goal of this research was to examine the impact of distinct frying techniques, including deep frying (DF), air frying (AF), and vacuum frying (VF), on the nutritional, textural and flavor characteristics of oysters. The VF method demonstrated superior retention of beneficial properties and flavor, and reduced protein and lipid oxidation compared to the DF and AF methods. Furthermore, proteomic analysis of oysters was attempted to explain the molecular mechanisms governing the influence of key differential proteins. 20 major differential proteins, including actin-2 protein, tryptophan 2,3-dioxygenase and 1-alph, involved in oyster protein oxidation were identified, annotated and analyzed to elucidate their influence mechanisms. This research provides a deeper understanding of intricate interactions between frying techniques and oyster biochemistry, which offers valuable implications for enhancing food quality in seafood industry.

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Advanced glycation end products (AGEs) are complex and heterogeneous compounds closely associated with various chronic diseases. The changes in Nε-carboxymethyllysine (CML), Nε-carboxyethyllysine (CEL), Nε-(5-hydro-5-methyl-4-imidazolon-2-yl)-ornithine (MG-H1), and fluorescent AGEs (F-AGEs) in fried shrimp during frying (170 °C, 0-210 s) were described by kinetic models. Besides,the correlations between AGEs contents and physicochemical indicators were analyzed to reveal their intrinsic relationship. Results showed that the changes of four AGEs contents followed the zero-order kinetic, and their rate constants were ranked as kCML < kCEL ≈ kMG-H1 < kF-AGEs. Oil content and lipid oxidation were critical factors that affected the AGEs levels of the surface layer. Protein content and Maillard reaction were major factors in enhancing the CML and CEL levels of the interior layer. Furthermore, the impact of temperature on the generation of CML and CEL was greater than that of MG-H1 and F-AGEs.

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Frozen surimi sol incline to protein oxidation, but the quality control strategies based on oxidation remain limited. Hence, the antioxidant and cryoprotective effects of γ-polyglutamic acid (γ-PGA) on freeze-thawed salt-dissolved myofibrillar protein (MP) sol were investigated. Results showed that γ-PGA could effectively regulate protein oxidation of MP sol during freeze-thawing with lower carbonyl contents and less oxidative cross-linking. Meanwhile, γ-PGA primely maintained sol protein structures, showing reduction of 15.28% of salt soluble protein contents at γ-PGA addition of 0.04% under unoxidized condition. Additionally, compared to the control group without oxidation treatment, cooking loss of heat-induced gel with 0.04% γ-PGA decreased by 47.19%, while gel strength obviously increased by 57.22% respectively. Overall, moderate γ-PGA addition (0.04%) could inhibit protein oxidation of sol, further improving frozen stability of sol through hydrogen bonds and hydrophobic interaction, but excessive γ-PGA was adverse to sol quality due to severe cross-linking between γ-PGA and MP.

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This study investigated the effects of sodium pyrophosphate (SPP) and catechin (C) on the in vitro enzymatic digestion of oxidatively damaged myofibrillar protein (MP) gel. The results indicated that SPP increased the ß-sheet content and the gastric digestibility of the MP gel, while C hindered the transition from α-helix to ß-sheet structure, leading to decreased digestibility. Notably, neither compound significantly affected intestinal digestibility. Furthermore, SPP and C significantly enhanced the antioxidant activity of MP gel digestion products. Notably, their synergistic hydrolysis products, simulating both gastric and gastrointestinal stages, chelated 91.4 % and 89.1 % of Fe2+ and scavenged 59.4 % and 77.6 % of hydroxyl radicals, respectively. Moreover, the final digestion products of the MP gel treated with SPP and C exhibited the highest content of negatively charged amino acids and absolute Zeta potential values. Overall, this study demonstrated that incorporating SPP and C could positively impact the digestion of oxidatively damaged MP gels.

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Objective: This study investigated the protein oxidation of soybean meal (SBM) stored in a warehouse and the effects of SBM on growth performance, antioxidant status, digestive performance, intestinal morphology, and breast muscle quality of broilers. Methods: In total, 160 one-day-old Arbor Acres Plus broilers (half male and half female) were randomly divided into two groups with ten replicates of eight birds each: The control group was served with a basal diet including SBM stored at -20 °C (FSBM), and the experimental group was served with a basal diet including SBM stored in a warehouse at room temperature for 45 days (RSBM). Results: Compared with FSBM, the protein carbonyl level in RSBM was increased, the free and total thiol levels and in vitro digestibility of protein were decreased. The RSBM decreased the serum glutathione (GSH) level and the hepatic total superoxide dismutase (T-SOD) activity at days 21 and 42 when compared with FSBM. Further, RSBM reduced the duodenal T-SOD activity, jejunal catalase (CAT), and T-SOD activities at day 21, and decreased the duodenal CAT and T-SOD activities, jejunal T-SOD activity, and ileal GSH level and T-SOD activity at days 21 and 42 when compared with FSBM. Besides, the trypsin activity and the ratio of villus height (VH) to crypt depth (CD) in small intestines of broilers at days 21 and 42 were reduced when fed with a RSBM-contained diet. Compared with FSBM, the 24-h drip loss, shear force, and 24- and 48-h cooking loss of breast muscle were increased of RSBM group, the opposite result was observed for muscle lightness at 48 h. Conclusion: Room temperature storage for 45 days led a protein oxidation and decreased in vitro digestibility in SBM, and fed RSBM impaired growth performance, antioxidant status, and meat quality, reduced trypsin activity, and affected the small intestine morphologyin broilers.

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Light exposure during manufacturing, storage, and administration can lead to the photodegradation of therapeutic proteins. This photodegradation can be promoted by pharmaceutical buffers or impurities. Our laboratory has previously demonstrated that citrate-Fe(III) complexes generate the •CO2- radical anion when photoirradiated under near UV (λ = 320-400 nm) and visible light (λ = 400-800 nm) [Subelzu, N.; Schöneich, C. Mol. Pharmaceutics 2020, 17 (11), 4163-4179; Zhang, Y. Mol. Pharmaceutics 2022, 19 (11), 4026-4042]. Here, we evaluated the impact of citrate-Fe(III) on the photostability and degradation mechanisms of disulfide-containing proteins (bovine serum albumin (BSA) and NISTmAb) under pharmaceutically relevant conditions. We monitored and localized competitive disulfide reduction and protein oxidation by high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) analysis depending on the reaction conditions. These competitive pathways were affected by multiple factors, including light dose, Fe(III) concentration, protein concentration, the presence of oxygen, and light intensity.

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This work investigated the effects of five thawing methods (air thawing (AT), water thawing (WT), plasma-activated water thawing (PT), ultrasound-assisted water thawing (UWT) and ultrasound-assisted plasma-activated water thawing (UPT)) on thawing rate, quality characteristics, lipid and protein oxidation of porcine longissimus dorsi using fresh sample as control. The thawing time of UPT samples was significantly reduced by 81.15% compared to AT treatment (P < 0.05). The thawing loss of UPT samples was 1.55% significantly lower than AT samples (4.51%) (P < 0.05). In addition, UPT samples had the least cooking loss and centrifugal loss. UPT treatment reduced the conversion of bound and immobilized water to free water and resulted in more uniform water distribution. UPT treatment significantly decreased the thiobarbituric acid reactive substances (TBARS) value and carbonyl content and increased the total sulfhydryl content of the samples (P < 0.05). In conclusion, UPT treatment increased the thawing rate and retarded the lipid and protein oxidation, resulting in better maintenance of quality characteristics of porcine longissimus dorsi than other thawing methods.

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Both rice bran (RB) rancidity and dephenolization could affect the structural characteristics and phenolics composition of rice bran protein (RBP), thereby affecting RBP digestibility. The synergistic effects of RB rancidity and dephenolization on RBP digestibility were investigated. Excessive RB rancidity (RB stored for 10 d) and non-dephenolization reduced RBP digestibility, while moderate RB rancidity (RB stored for 1 d) combined with dephenolization improved RBP digestibility to a maximum of 74.19%. Dephenolization reduced the antioxidant capacities of RBP digestive products. The digestibility of non-dephenolized RBP (NDRBP) was significantly (P < 0.05) related with its carbonyl content, surface hydrophobicity, and ζ-potential. The digestibility of dephenolized RBP (DRBP) was significantly related with its ß-sheet structure content, surface hydrophobicity, ζ-potential, and average particle size. Overall, moderate RB rancidity combined with dephenolization enhanced RBP digestibility by reducing the non-competitive inhibition of endogenous phenolics on protease and regulating the spatial structural characteristics of RBP.

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The human tumor suppressor p16INK4a is a small monomeric protein that can form amyloid structures. Formation of p16INK4a amyloid fibrils is induced by oxidation which creates an intermolecular disulfide bond. The conversion into amyloid is associated with a change from an all α-helical structure into ß-sheet fibrils. Currently, structural insights into p16INK4a amyloid fibrils are lacking. Here, we investigate the amyloid-forming regions of this tumor suppressor using isotope-labeling limited-digestion mass spectrometry analysis. We discover two key regions that likely form the structured core of the amyloid. Further investigations using thioflavin-T fluorescence assays, electron microscopy, and solution nuclear magnetic resonance spectroscopy of shorter peptide regions confirm the self-assembly of the identified sequences that include methionine and leucine repeat regions. This work describes a simple approach for studying protein motifs involved in the conversion of monomeric species into aggregated fibril structures. It provides insight into the polypeptide sequence underlying the core structure of amyloid p16INK4a formed after a unique oxidation-driven structural transition.

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This study examined the effects of replacing alkaline phosphate (AP) with bamboo fiber (BF), isolated pea protein (PP), and mushroom powder (MP) on the nutritional, technological, oxidative, and sensory characteristics of low-sodium mortadellas. Results indicated that this reformulation maintained the nutritional quality of the products. Natural substitutes were more effective than AP in reducing water and fat exudation. This led to decreased texture profile analysis (TPA) values such as hardness, cohesiveness, gumminess, and chewiness. The reformulation reduced the L* values and increased the b* values, leading to color modifications rated from noticeable to appreciable according to the National Bureau of Standards (NBS) index. Despite minor changes in oxidative stability indicated by increased values in TBARS (from 0.19 to 0.33 mg MDA/kg), carbonyls (from 2.1 to 4.4 nmol carbonyl/mg protein), and the volatile compound profile, the sensory profile revealed a beneficial increase in salty taste, especially due to the inclusion of MP, which was enhanced by the synergy with BF and PP. In summary, the results confirmed the potential of natural alternatives to replace chemical additives in meat products. Incorporating natural antioxidants into future formulations could address the minor oxidation issues observed and enhance the applicability of this reformulation strategy.

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The oxidative phase of the pentose phosphate pathway (PPP) involving the enzymes glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconolactonase (6PGL), and 6-phosphogluconate dehydrogenase (6PGDH), is critical to NADPH generation within cells, with these enzymes catalyzing the conversion of glucose-6-phosphate (G6P) into ribulose-5-phosphate (Ribu5-P). We have previously studied peroxyl radical (ROO•) mediated oxidative inactivation of E. coli G6PDH, 6PGL, and 6PGDH. However, these data were obtained from experiments where each enzyme was independently exposed to ROO•, a condition not reflecting biological reality. In this work we investigated how NADPH production is modulated when these enzymes are jointly exposed to ROO•. Enzyme mixtures (1:1:1 ratio) were exposed to ROO• produced from thermolysis of 100 mM 2,2'-azobis(2-methylpropionamidine) dihydrochloride (AAPH). NADPH was quantified at 340 nm, and protein oxidation analyzed by liquid chromatography with mass spectrometric detection (LC-MS). The data obtained were rationalized using a mathematical model. The mixture of non-oxidized enzymes, G6P and NADP+ generated ∼175 µM NADPH. Computational simulations showed a constant decrease of G6P associated with NADPH formation, consistent with experimental data. When the enzyme mixture was exposed to AAPH (3 h, 37 °C), lower levels of NADPH were detected (∼100 µM) which also fitted with computational simulations. LC-MS analyses indicated modifications at Tyr, Trp, and Met residues but at lower concentrations than detected for the isolated enzymes. Quantification of NADPH generation showed that the pathway activity was not altered during the initial stages of the oxidations, consistent with a buffering role of G6PDH towards inactivation of the oxidative phase of the pathway.

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Clusterin is a secreted glycoprotein that participates in multiple physiological processes through its chaperon function. In Alzheimer's disease, the brain functions under an increased oxidative stress condition that causes an elevation of protein oxidation, resulting in enhanced pathology. Accordingly, it is important to determine the type of human brain cells that are mostly prone to methionine oxidation in Alzheimer's disease and specifically monitoring the methionine-oxidation levels of clusterin in human and mice brains and its effect on clusterin's function. We analyzed the level of methionine sulfoxide (MetO)-clusterin in these brains, using a combination of immunoprecipitation and Western-blott analyses. Also, we determine the effect of methionine oxidation on clusterin ability to bind beta-amyloid, in vitro, using calorimetric assay. Our results show that human neurons and astrocytes of Alzheimer's disease brains are mostly affected by methionine oxidation. Moreover, MetO-clusterin levels are elevated in postmortem Alzheimer's disease human and mouse brains in comparison to controls. Finally, oxidation of methionine residues of purified clusterin reduced its binding efficiency to beta-amyloid. In conclusion, we suggest that methionine oxidation of brain-clusterin is enhanced in Alzheimer's disease and that this oxidation compromises its chaperon function, leading to exacerbation of beta-amyloid's toxicity in Alzheimer's disease.

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Cold plasma treatment is an innovative technology in the food processing and preservation sectors. It is primarily employed to deactivate microorganisms and enzymes without heat and chemical additives; hence, it is often termed a "clean and green" technology. However, food quality and safety challenges may arise during cold plasma processing due to potential chemical interactions between the plasma reactive species and food components. This review aims to consolidate and discuss data on the impact of cold plasma on the chemical constituents and physical and functional properties of major food products, including dairy, meat, nuts, fruits, vegetables, and grains. We emphasize how cold plasma induces chemical modification of key food components, such as water, proteins, lipids, carbohydrates, vitamins, polyphenols, and volatile organic compounds. Additionally, we discuss changes in color, pH, and organoleptic properties induced by cold plasma treatment and their correlation with chemical modification. Current studies demonstrate that reactive oxygen and nitrogen species in cold plasma oxidize proteins, lipids, and bioactive compounds upon direct contact with the food matrix. Reductions in nutrients and bioactive compounds, including polyunsaturated fatty acids, sugars, polyphenols, and vitamins, have been observed in dairy products, vegetables, fruits, and beverages following cold plasma treatment. Furthermore, structural alterations and the generation of volatile and non-volatile oxidation products were observed, impacting the color, flavor, and texture of food products. However, the effects on dry foods, such as seeds and nuts, are comparatively less pronounced. Overall, this review highlights the drawbacks, challenges, and opportunities associated with cold plasma treatment in food processing.

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Spatiotemporal assessment of lipid and protein oxidation is key for understanding quality deterioration in emulsified food products containing polyunsaturated fatty acids. In this work, we first mechanistically validated the use of the lipid oxidation-sensitive fluorophore BODIPY 665/676 as a semi-quantitative marker for local peroxyl radical formation. Next, we assessed the impact of microfluidic and colloid mill emulsification (respectively producing mono- and polydisperse droplets) on local protein and lipid oxidation kinetics in whey protein isolate (WPI)-stabilized emulsions. We further used BODIPY 581/591 C11 and CAMPO-AFDye 647 as colocalisation markers for lipid and protein oxidation. The polydisperse emulsions showed an inverse relation between droplet size and lipid oxidation rate. Further, we observed less protein and lipid oxidation occurring in similar sized droplets in monodisperse emulsions. This observation was linked to more heterogeneous protein packing at the droplet surface during colloid mill emulsification, resulting in larger inter-droplet heterogeneity in both protein and lipid oxidation. Our findings indicate the critical roles of emulsification methods and droplet sizes in understanding and managing lipid oxidation.

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Chronic Kidney Disease (CKD) patients are at increased risk for atherosclerosis, cardiovascular disease (CVD) and progression to end stage kidney disease (ESKD). This heavy CVD risk cannot be solely at-tributed to traditional Framingham risk factors. Oxidative stress (OS), defined as the disruption of balance between prooxidants and antioxidants in favor of the former, has emerged as a novel risk factor for CVD and CKD progression. Specifically, lipid peroxidation has been identified as a trigger for endothelial dys-function, the first step towards atherogenesis and protein oxidation has been associated with CKD progres-sion. The oxidation of proteins and lipids starts early in CKD, increases gradually with disease progression and is further exacerbated in ESKD, due to dialysis related factors. In order to counteract the deleterious effects of free radicals and thereby ameliorate, or delay, CV disease and progression of CKD, exogenous administration of antioxidants has been proposed. Here, we attempt to summarize existing data from ex-perimental and clinical studies that test antioxidants for their possible beneficial effects against CVD and CKD progression such as vitamins E and C, statins, omega-3 fatty acids, trace elements, polyphenols and N-acetylcysteine.