Pinelliae Rhizoma (PR), a traditional herbal medicine and dietary supplement, is valued for its cough relief and anti-inflammatory effects. However, it can cause significant throat irritation. And unfortunately, current processing techniques can lead to a considerable loss of active constituents in PR. This study employed microwave irradiation to process PR and elucidated the mechanisms underlying its attenuation of PR's irritation. The results demonstrated that microwave irradiation significantly enhanced the processing efficiency, reducing the traditional processing cycle from 5 to 15 days to just 10 min, while preserving active ingredients and mitigating irritation. Subsequent analysis of the irritant components found that microwave treatment significantly reduced the raphides content, altering their morphology. Concurrently, the secondary structure of lectin proteins underwent significant changes, including an increase in β-sheets, a decrease in β-turns and random coils content, and the formation of insoluble aggregates. In conclusion, microwave irradiation is an effective method for reducing the irritation of PR, with the mechanism attributed to the physical destruction of raphides and alterations in the hydrophobicity of lectin proteins. This study provides a novel approach and method for the processing and development of Araceae herbs, as well as food products such as yam, konjac, and pineapple.

Aquatic collagen, a natural macromolecule protein with excellent biocompatibility, has attracted attention in the field of medical materials. Compared to mammalian collagen, aquatic collagen offers unique advantages, including the absence of zoonotic disease risks and religious concerns. In this study, salmon skin collagen nanofiber membrane (GS) was prepared by electrostatic spinning. Then, skin collagen was combined with silk sericin (SS) and sodium hyaluronate (HA) to fabricate composite collagen nanofiber membrane (GF) using electrostatic spinning technology. GF membranes were further cross-linked (GFL) for use in a mouse wound healing model. The physicochemical properties and biocompatibility of GS, GF, and GFL were evaluated. FTIR analysis revealed that GFL exhibited a more stable secondary structure compared to GS and GF. DSC and TGA results indicated that GFL had the highest thermal stability, followed by GF. Cytotoxicity tests confirmed that GS, GF, and GFL were non-cytotoxic, with GF showing the highest cell viability rate of 175.23 ± 1.77%. In the wound healing model, GFL group achieved nearly complete healing by day 14 (98 ± 0.1%), compared to 76.04 ± 0.01% in the blank group. Measurement of TGF-β1 and VEGF levels in the healing tissue on day 14 indicated that the GFL group had progressed to the late stage of healing, whereas the blank group remained in the early stage. These results suggest that GFL holds significant potential as a medical biomaterial for wound healing applications.

In this study, pathways and mechanisms of action of a new type of Pleurotus eryngii polysaccharide (PEP) with known structural characteristics and probiotic properties in the intestine were investigated. An in vitro cell model was used to investigate the protective effects of complexes formed between PEPs and their related products with mucin against gut barrier damage. Dextran sulfate sodium salt-induced colitis was used to determine the characteristics of the interaction between PEPs and intestinal mucus (IMs) at different consumption times. Finally, the protective effect of PEPs against intestinal barrier damage was investigated, as mediated by IMs. The result showed that complexes of PEP-related products and mucin improved damage to the intestinal barrier. PEPs exhibited differential functional activities at different stages. In normal and colitis mice, the interactions between IMs and PEPs showed different characteristics. From the transport and absorption standpoint, the role of PEPs in driving intestinal health was also clarified in this study.

A vast sum of fish waste is being annually discarded by marine fishing industries imposing serious environmental pollution concerns. However, these aquatic discarded matters are captivating sources of collagen, a fibrous protein with eminent social and economic relevance. Collagen is conventionally recovered using outdated complex processes requiring many reagents, multiple steps, and extended periods. Hereupon, the current project is the first work on the isolation of Seabass fish scales (FSC) type-I collagen, with preserved secondary and triple helical structures of the native collagen, developing a simple, green, cost-effective, and eco-friendly methodology, utilizing sustainable natural deep eutectic solvents (NADES)-assisted ultrasonication (US) technical route. The operational conditions were optimized based on the one-factor-at-a-time modeling to maximize the yield with no alteration of collagen integrity. Recorded data confirmed type-I collagen with preserved triple helix integrity and thermal stability, improved bio-functionalities, in vitro fibril formation, and functional performances. Finally, the in vitro hemolysis and cytotoxicity tests confirmed the extracted collagens biocompatibility, demonstrating the feasibility of Seabass FSC waste and a NADES-coupled US brief process (20 min) to establish a more sustainable eco-friendly pathway to isolate high-quality type I-collagen, as an attempt to rise industries awareness about wastes valorization within the scheme of circular economy.

Marine collagen is gaining more attraction than terrestrial collagen because it is free of zoonotic disease and religious constrain. In this study, we aimed to investigate and compare the physicochemical properties and functional characteristics of acid-soluble collagen (ASC-MF) and pepsin-soluble collagen (PSC-MF) extracted from scales of Megalonibea fusca. ASC-MF and PSC-MF were evaluated in terms of yield, collagen type, amino acid composition, thermal stability, microstructure, cytotoxicity, and other physicochemical parameters. ASC-MF and PSC-MF depicted 1.72 ± 0.2% and 11.72 ± 0.3% of dry weight yields, respectively, and were identified as type I collagen with an intact triple-helical structure by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), spectroscopic analysis, and electron microscopy. Additionally, compared with many temperate and tropical species, ASC-MF and PSC-MF showed higher thermal stability, with the maximum transition temperature (Tmax) of 53.50°C (ASC-MF) and 43.16°C (PSC-MF). CCK-8 assay showed that ASC-MF and PSC-MF have no cytotoxicity in vitro. The determination of blood clotting index values showed that both ASC-MF and PSC-MF had good hemostatic ability. In summary, these findings show that PSC-MF isolated from the scales of M. fusca may be a feasible alternative to terrestrial collagen sources in food and biomedical applications.

Triboelectric nanogenerators (TENGs) combine contact electrification and electrostatic induction effects to convert waste mechanical energy into electrical energy. As conventional devices contribute to electronic waste, TENGs based on ecofriendly and biocompatible materials have been developed for various energy applications. Owing to the abundance, accessibility, low cost, and biodegradability of biowaste (BW), recycling these materials has gained considerable attention as a green approach for fabricating TENGs. This review provides a detailed overview of BW materials, processing techniques for BW-based TENGs (BW-TENGs), and potential applications of BW-TENGs in emerging bioelectronics. In particular, recent progress in material design, fabrication methods, and biomechanical and environmental energy-harvesting performance is discussed. This review is aimed at promoting the continued development of BW-TENGs and their adoption for sustainable energy-harvesting applications in the field of bioelectronics.

Tilapia, a widely farmed aquaculture fish, produces substantial waste, including viscera that contain extracellular matrix (ECM) utilized as a biomaterial for tissue regeneration applications. Extracting ECM from viscera requires a specific decellularization method, as no standardized protocol exists. This study performed three decellularization methods: sonication, orbital shaking at room temperature, and agitation at 4°C, using SDS and TX100 at concentrations of 0.1% and 0.3%. The effectiveness of each method was assessed through H&E staining, dsDNA quantification, and SEM imaging to verify cellular content removal and ECM structure preservation. Additional analyses, including ATR-FTIR, SDS-PAGE, protein quantification, HPLC, and detergent residue tests, were performed to examine functional groups, collagen composition, protein content, amino acid profiles, and detergent residues in the decellularized samples. The results of H&E staining showed a significant reduction in cellular components in all samples, which was confirmed through DNA quantification. Sonication with 0.3% SDS achieved the highest DNA removal rate (96.5 ± 1.1%), while SEM images revealed that agitation at 4°C with 0.3% TX100 better preserved ECM structure. Collagen was present in all samples, as confirmed by ATR-FTIR analysis, which revealed pronounced spectral peaks in the amide I, II, III, A, and B regions. Samples treated with agitation at 4°C using 0.1% SDS exhibited the highest protein content (875 ± 15 µg/mg), whereas those treated with TX100 had lower detergent residue. Overall, the decellularization methods effectively reduced DNA content while preserving ECM structure and components, highlighting the potential of tilapia viscera as bioscaffolds and offering insights into utilizing fish waste for high-value products.

Fish swim bladder (FSB) is a type of traditional nutraceutical, but the lack of high-quality drying methods limits its premium market development. In order to obtain optimal-quality dried FSBs from Chinese longsnout catfish, the effects of liquid nitrogen pre-freezing (LNF) and drying on the physical properties and flavor of FSB were evaluated. Four methods were used for FSB drying, including natural air-drying (ND), hot-air-drying (HD), LNF combined with freeze-drying (LN-FD), and LNF combined with HD (LN-HD). Color, collagen content, rehydration ratio, textural properties, and flavor characteristics (by GC-IMS, E-nose, and E-tongue) were measured to clarify the differences among four dried FSBs. The results showed that ND cannot effectively remove moisture from FSB as the final product showed a stronger sourness in taste. HD led to a decrease in the collagen content and the collapse of the fiber structure in FSB. Compared to HD, LN-HD showed a higher collagen content (0.56 g/g) and a different flavor fingerprint. FSB treated by LN-FD had better physical qualities in terms of an attractive color, a high collagen content (0.79 g/g), low shrinkage, a higher rehydration ratio (2.85), and a soft texture, while also possessing richer characteristic flavors. The application of LN-FD may help the optimization of the nutrition level, rehydration ability, mouthfeel, and flavor of dried FSB.

Recently, fish consumption has been increasing; subsequently, the number of by-products has also increased. However, generated residues are frequently discarded, and an appropriate management is necessary to properly use all fish by-products. Fishery by-products are well known for their content of bioactive compounds, such as unsaturated fatty acids, amino acids, minerals, peptides, enzymes, gelatin, collagen, and chitin. Several studies have reported that fishery by-products could provide significant properties, including antioxidant, antihypertensive, antimicrobial, anti-inflammatory, and antiobesity. Consequently, fish discards are of considerable interest to different industrial sectors, including food, nutraceuticals, medical, and pharmacology. In the food industry, the interest in using fishery by-products is focused on hydrolysates as food additives, collagen and gelatin as protein sources, chitin and chitosan to form edible films to protect food during storage, and oils as a source of Omega-3 and useful as antioxidants. Although different studies reported good results with the use of these by-products, identifying new applications in the food sector, as well as industrial applications, remains necessary.

Animal-derived biomaterials have been extensively employed in clinical practice owing to their compositional and structural similarities with those of human tissues and organs, exhibiting good mechanical properties and biocompatibility, and extensive sources. However, there is an associated risk of infection with pathogenic microorganisms after the implantation of tissues from pigs, cattle, and other mammals in humans. Therefore, researchers have begun to explore the development of non-mammalian regenerative biomaterials. Among these is the swim bladder, a fish-derived biomaterial that is rapidly used in various fields of biomedicine because of its high collagen, elastin, and polysaccharide content. However, relevant reviews on the biomedical applications of swim bladders as effective biomaterials are lacking. Therefore, based on our previous research and in-depth understanding of this field, this review describes the structures and compositions, properties, and modifications of the swim bladder, with their direct (including soft tissue repair, dural repair, cardiovascular repair, and edible and pharmaceutical fish maw) and indirect applications (including extracted collagen peptides with smaller molecular weights, and collagen or gelatin with higher molecular weights used for hydrogels, and biological adhesives or glues) in the field of biomedicine in recent years. This review provides insights into the use of swim bladders as source of biomaterial; hence, it can aid biomedicine scholars by providing directions for advancements in this field.

This study compared collagens from cold-water and warm-water fish for their structural, rheological, and functional properties, and explored their potential applications, aiming to realize the high-value utilization of marine biological resources. To this end, chum salmon skin collagen (CSSC) and Nile tilapia skin collagen (NTSC) were both successfully extracted. Collagens from the two species had different primary and secondary structures, with NTSC having a higher molecular weight, imino acid content, and α-helices and β-turns content. The denaturation temperatures were 12.01 °C for CSSC and 31.31 °C for NTSC. CSSC was dominated by viscous behavior and its structure varied with temperature, while NTSC was dominated by elastic behavior and its structure remained stable with temperature. Both collagens had good oil holding capacity, foaming capacity, and emulsifying activity, but NTSC had better water holding capacity and foaming and emulsifying stability. Their different properties make CSSC more suitable for the preservation of frozen and chilled foods and the production of sparkling beverages, and give NTSC greater potential in biofunctional materials and solid food processing.

The effects of ultrasonic power (0, 150, 300, 450, and 600 W) on the extraction yield and the structure and rheological properties of pepsin-soluble collagen (PSC) from albacore skin were investigated. Compared with the conventional pepsin extraction method, ultrasonic treatment (UPSC) significantly increased the extraction yield of collagen from albacore skin, with a maximum increase of 8.56%. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that peptides of low molecular weight were produced when the ultrasonic power exceeded 300 W. Meanwhile, secondary structure, tertiary structure, and X-ray diffraction analyses showed that the original triple helix structure of collagen was intact after the ultrasonic treatment. The collagen solutions extracted under different ultrasonic powers had significant effects on the dynamic frequency sweep, but a steady shear test suggested that the collagen extracted at 150 W had the best viscosity. These results indicate that an ultrasonic power between 150 and 300 W can improve not only the extraction yield of natural collagen, but also the rheological properties of the collagen solution without compromising the triple helix structure.

Noise pollution is increasingly prevalent in aquatic ecosystems, causing detrimental effects on growth and behavior of marine fishes. The physiological responses of fish to underwater noise are poorly understood. In this study, we used RNA-sequencing (RNA-seq) to study the transcriptome of the sonic muscle in small yellow croaker (Larimichthys polyactis) after exposure to a 120 dB noise for 30 min. The behavioral experiment revealed that noise exposure resulted in accelerated tail swimming behavior at the beginning of the exposure period, followed by loss of balance at the end of experiment. Transcriptomic analysis found that most highly expressed genes in the sonic muscle, including parvalbumin, slc25a4, and troponin C were related with energy metabolism and locomotor function. Further, a total of 1261 differentially expressed genes (DEGs) were identified, including 284 up-regulated and 977 down-regulated genes in the noise exposure group compared with the control group. Gene ontology (GO) analysis indicated that the most enriched categories of DEGs included protein folding and response to unfolding protein. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis found over-represented pathways including protein processing in the endoplasmic reticulum, chaperones and folding catalysts, as well as arginine and proline metabolism. Specifically, many genes related to fatty acid and collagen metabolism were up-regulated in the noise exposure group. Taken together, our results indicate that exposure to noise stressors alters the swimming behavior of croaker, inducing endoplasmic reticulum stress, disrupting lipid metabolism, and causing collagen degradation in the sonic muscle of L. polyactis.

Collagen is an important biopolymer widely used in food, cosmetics and biomedical applications. Understanding the effect of pH on the structure and properties of collagen is beneficial for its further processing and exploitation. In this study, greenfin horse-faced filefish skin collagen (GHSC) was prepared and identified as a type I collagen. We systematically investigated the effect of pH on the structural, functional and rheological properties of GHSC. Scanning electron microscopy showed that the collagen morphology changed from an ordered stacked sheet structure to a rough silk-like structure as pH increased. Gaussian-fitted Fourier infrared spectroscopy results of the collagen revealed that it unfolded with increasing pH. Moreover, the ordered structure was reduced, and random coils became the dominant conformation. Its β-sheet and random coil contents increased from 18.43 ± 0.08 and 33.62 ± 0.17 to 19.72 ± 0.02 and 39.53 ± 1.03%, respectively, with increasing pH. α-helices and β-turns decreased from 35.00 ± 0.26 and 12.95 ± 0.01 to 29.39 ± 0.92 and 11.36 ± 0.10%, respectively. The increase in β-sheets and random coils allowed the pI-treated collagen to exhibit maximum water contact angle. The emulsification and foaming properties decreased and then increased with increasing pH in a V-shape. The increased net surface charge and β-sheets in collagen benefited its emulsification and foaming properties. The rheological results showed that the protoprotein exhibited shear-thinning properties in all pH ranges. The collagen solutions showed liquid-like behaviour in low-pH (2, 4) solutions and solid-like behaviour in high-pH (6, 7.83 and 10) solutions. Moreover, the frequency-dependent properties of the storage modulus (G') and loss modulus (G″) of the collagen solutions weakened with increasing pH. Collagen has considerable frequency-dependent properties of G' and G″ at low pH (2, 4). Thus, the importance of collagen raw material preparation for subsequent processing was emphasised, which may provide new insights into applying collagen-based materials in food, biomaterials and tissue engineering.

Lutein exhibits excellent functional activity making it useful in many fields. Nevertheless, its use is limited by its physical and chemical instability. Here, collagen and Lycium barbarum L. leaf flavonoids (LBLF) were used as emulsifiers, their structures were characterized, the properties of the complexes were evaluated, and their stabilizing effects on lutein emulsions were explored. According to the results, the encapsulation rate of the complex of collagen-LBLF was (68.67 ± 1.43) % and the drug loading was (6.92 ± 0.13) %. Collagen compounded LBLF with a changed structure and morphology, resulting in improved antioxidant capacity, better foaming and emulsification, and reduced hydrophobicity. In addition, the thiobarbituric acid value of collagen-LBLF stabilized lutein emulsion (0.0012 ± 0.00011) mg/kg was significantly lower than that of collagen stabilized lutein emulsion (0.0021 ± 0.00016)  mg/kg (P < 0.05), indicating that the composite stabilized lutein emulsion obtained higher stability. LBLF contributed a high free radical scavenging effect and inhibited lutein degradation during storage. During simulated digestion, collagen-LBLF effectively stabilized the emulsion and protected lutein from destruction, made it release more slowly, and benefited the bio-accessibility of lutein during the next utilization step. Based on the present study, improved storage and digestion stabilities of lutein wereachievedby the utilization of collagen-LBLF complex, which provides a new method for the preparation and application of composite functional emulsifiers.

The objective of this study was to isolate and characterize collagen and angiotensin-I-converting enzyme (ACE)-inhibitory (ACEi) peptides from the swim bladders of monkfish (Lophius litulon). Therefore, acid-soluble collagen (ASC-M) and pepsin-soluble collagen (PSC-M) with yields of 4.27 ± 0.22% and 9.54 ± 0.51%, respectively, were extracted from monkfish swim bladders using acid and enzyme methods. The ASC-M and PSC-M contained Gly (325.2 and 314.9 residues/1000 residues, respectively) as the major amino acid, but they had low imino acid content (192.5 and 188.6 residues/1000 residues, respectively) in comparison with collagen from calf skins (CSC) (216.6 residues/1000 residues). The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns and ultraviolet (UV) absorption spectrums of ASC-M and PSC-M illustrated that they were mainly composed of type I collagen. Subsequently, three ACEi peptides were isolated from a PSC-M hydrolysate prepared via a double-enzyme system (alcalase + neutrase) and identified as SEGPK (MHP6), FDGPY (MHP7) and SPGPW (MHP9), with molecular weights of 516.5, 597.6 and 542.6 Da, respectively. SEGPK, FDGPY and SPGPW displayed remarkable anti-ACE activity, with IC50 values of 0.63, 0.94 and 0.71 mg/mL, respectively. Additionally, a molecular docking assay demonstrated that the affinities of SEGPK, FDGPY and SPGPW with ACE were -7.3, -10.9 and -9.4 kcal/mol, respectively. The remarkable ACEi activity of SEGPK, FDGPY and SPGPW was due to their connection with the active pockets and/or sites of ACE via hydrogen bonding, hydrophobic interaction and electrostatic force. Moreover, SEGPK, FDGPY and SPGPW could protect HUVECs by controlling levels of nitric oxide (NO) and endothelin-1 (ET-1). Therefore, this work provides an effective means for the preparation of collagens and novel ACEi peptides from monkfish swim bladders, and the prepared ACEi peptides, including SEGPK, FDGPY and SPGPW, could serve as natural functional components in the development of health care products to control hypertension.

The objective of this study was to evaluate the effect of ultrasound pre-treatment on the characterization from Bactrian camel skin. It was possible to produce and characterize collagen extracted from Bactrian camel skin. The results showed that the yield of collagen was higher in ultrasound pre-treatment (UPSC) (41.99%) than the pepsin-soluble collagen extraction (PSC) (26.08%). All extracts were identified as type I collagens using sodium dodecyl sulfate polyacrylamide gel electrophoresis and retained their helical structure, as confirmed through Fourier transform infrared spectroscopy. The scanning electron microscopy analysis of UPSC revealed that some physical changes were caused by sonication. UPSC had smaller particle size than PSC. The viscosity of UPSC always plays a leading role in the range of 0-10 Hz. However, the contribution of elasticity to the solution system of PSC increased in the range of 1-10 Hz. Moreover, ultrasound-treated collagen had superior solubility property at pH 1-4 and at <3% (w/v) NaCl than non-ultrasound treated collagen. Therefore, the utilization of ultrasound for the extraction of pepsin soluble collagen is a good alternative technology to expand the application at industrial level.

The biochemical properties of collagens and gels from grass carp (Ctenopharyngodon idella) were studied to explore the feasibility of their application in biomaterials. The yields of skin collagen (SC) and swim bladder collagen (SBC) extracted from grass carp were 10.41 ± 0.67% and 6.11 ± 0.12% on a wet basis, respectively. Both collagens were characterized as type I collagen. Denaturation temperatures of SC and SBC were 37.41 ± 0.02 °C and 39.82 ± 0.06 °C, respectively. SC and SBC had high fibril formation ability in vitro, and higher values of salinity (NaCl, 0-280 mM) and pH (6-8) in formation solution were found to result in faster self-assembly of SC and SBC fibrils as well as thicker fibrils. Further tests of SC gels with regular morphology revealed that their texture properties and water content were affected by pH and NaCl concentration. The hardness, springiness, and cohesiveness of SC gels increased and the chewiness and water content decreased as pH increased from 7 to 8 and NaCl concentration increased from 140 to 280 mM. These properties suggest that collagens from grass carp may be useful in biomaterial applications in the future.

The objective of this study was to develop aquatic collagen production from fish processing by-product skin as a possible alternative to terrestrial sources. Silver carp skin collagen (SCSC) was isolated and identified as type I collagen, and LC-MS/MS analysis confirmed the SCSC as Hypophthalmichthys molitrix type I collagen, where the yield of SCSC was 40.35 ± 0.63% (dry basis weight). The thermal denaturation temperature (Td) value of SCSC was 30.37 °C, which was superior to the collagen of deep-sea fish and freshwater fish. Notably, SCSC had higher thermal stability than human placental collagen, and the rheological experiments showed that the SCSC was a shear-thinning pseudoplastic fluid. Moreover, SCSC was functionally superior to some other collagens from terrestrial sources, such as sheep, chicken cartilage, and pig skin collagen. Additionally, SCSC could provide a suitable environment for MC3T3-E1 cell growth and maintain normal cellular morphology. These results indicated that SCSC could be used for further applications in food, cosmetics, and biomedical fields.

For the mixed aqueous solution of LSL and COP, the interaction mode and mechanism have been comprehensively studied using multispectral methods including fluorescence spectrum, ultraviolet-visible adsorption spectrum (UV-Vis), and circular dichroism spectrum (CD). Then its surface activity, particle size, foaming, emulsifying, viscosity, and antibacterial properties are evaluated in detail by surface tension measurement (ST), dynamic light scattering (DLS), oscillametric method, spectrophotometer, ubbelohde viscometer and zone of inhibition separately. Compared with the single LSL or COP aqueous solution, the mixed system shows different performance optimizations in different aspects. The surface activity and foaming properties are mainly attributed to LSL, and the viscosity is attributed to COP. Fluorescence spectroscopy results show that the fluorescence distribution of COP has significant changes by the LSL addition and a static quenching mechanism is proved. The results of UV-Vis and CD spectra also show the changing conformation of COP by the LSL addition. The data of thermodynamic parameters prove that the combination of LSL and COP is a spontaneous exothermic process and is an enthalpy-driven process. The interaction mechanism between LSL and COP is very helpful for the application and development of the mixed mild biosurfactant-protein system used in the cosmetic and food industries.

This study aimed to compare ozone-microbubble-washing (OM) performed by domestic equipment with conventional water-washing (CW) regarding resultant quality attributes of muscle foods. For this purpose, muscle microstructure and lipid and protein oxidation were evaluated in pork and fish samples after OM and CW treatments. The assessment of muscle microstructure showed that OM treatment did not damage the microstructure of muscle fibers in both pork and fish samples. Thiobarbituric acid reactive substances (TBARS) values were not detected in both treatment groups, and they were substantially below the generally acceptable threshold (1 mg MDA/kg). The methylglyoxal (MGO) level of OM-treated fish samples was significantly higher than that of CW-treated fish samples. However, glyoxal (GO) and MGO levels of OM-treated pork samples were significantly lower than that of CW-treated pork samples. Similar types and sites of oxidative modification and similar numbers of modified peptides, as well as no significant difference in the concentration of total and most of the free amino acids (FAA) between treatment groups, indicated that OM treatment did not accelerate protein oxidation.