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This study investigated the effects of ethanol, 1,2-propanediol, and glycerol on the structure and aggregation behavior of silver carp (Hypophthalmichthys molitrix) myosin. All alcohols induced extensive alteration in the tertiary structure of myosin. Both ethanol and 1,2-propanediol further promoted an increase in the content of β-sheets in myosin and induced myosin aggregation. While glycerol had almost no impact on the secondary structure of myosin. Molecular dynamics simulations revealed that increasing the concentration of ethanol and 1,2-propanediol affected the overall structural changes in the myosin heavy chain (MHC), while glycerol exerted a more pronounced effect on the MHC tail when compared to the MHC head. Disruption of the hydration layers induced by ethanol and 1,2-propanediol contributed to local structural changes in myosin. Glycerol at a concentration of 20% induced the formation of a larger hydration layer around the MHC tail, which facilitated the stabilization of the protein structure., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier Ltd.)

Muscle protein stability during freeze-thaw (F-T) cycles was investigated with tilapia cultured in recirculating aquaculture systems (RAS) and traditional aquaculture in ponds (TAP). This study found that fatty acids (eg., palmitic acid) were enriched in TAP, while antioxidants (eg., glutathione) were enriched in RAS. Generally, proteins in the RAS group exhibited greater stability against denaturation during the F-T cycle, suggested by a less decrease in haem protein content (77% in RAS and 86% in TAP) and a less increase in surface hydrophobicity of sarcoplasmic protein (63% in RAS and 101% in TAP). There was no significant difference in oxidative stability of myofibrillar protein between the two groups. This study provides a theoretical guide for the quality control of tilapia cultured in RAS during frozen storage., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

To improve nutritional health, a low-salt (0.5 %) silver carp (Hypophthalmichthys molitrix) surimi gel with α-tocopherol, soybean oil, and glyceryl monostearate oleogel was fabricated and evaluated for textural qualities, lipid oxidation, and in-vitro digestion analysis. Based on the texture profile analysis, gel strength, water holding capacity (WHC), rheological, protein secondary structure, and microstructural examination, 5 % oleogel addition to low-salt surimi exhibited similar physicochemical properties to regular-salt surimi gels. By crosslinking myosin and filling protein network voids, the oleogel increased surimi gel density. Increasing oleogel content improved the physicochemical qualities of heat-induced surimi, causing protein aggregation during digestion and reducing digestibility. The presence of oleogel altered protein secondary structure, reducing α-helix content and increasing β-sheet and other structures, enhancing WHC and gel strength of low salt surimi. Adding oleogel improved the antioxidant activity of digestive solutions. This study will help understand myosin-oleogel interaction and the development of sustainable and nutritious surimi-based foods., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The reduction of the salt content of foods is of interest for health reasons. The present study showed that low-salt surimi gels could be produced using a combination of l-arginine (Arg) and transglutaminase (TGase) under microwave (MW) irradiation. The low-salt surimi gels produced by MW had similar physicochemical properties as regular-salt surimi gels produced by conventional two-stage water bath heating. Compared to low-salt surimi gels containing TGase alone, Arg increased the water holding capacity and gel strength (P < 0.05) and promoted the formation of a more homogeneous and compact three-dimensional gel network. As a result, there was a significant increase in the proportion of immobilized water and decrease in the proportion of free water (P < 0.05). The nature of the binding sites between Arg and myosin heavy chain was predicted using the molecular docking simulations analysis. These results may be useful for the development of low-salt surimi products., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

In this study, glutamic acid and zein were utilized to prepare colloidal nanoparticles as stabilizers for Pickering emulsions. The effect of the ratio of glutamic acid to zein on the stability, zeta potential, particle size, morphology, and structure of colloidal nanoparticles was studied. The results showed that zein and glutamic acid combined in the form of noncovalent bonds, which changed the characteristics of the zein. In addition, colloidal particles aggregation was induced by glutamic acid, which altered the distribution of droplets in the emulsion, and increased the adsorption of proteins on the surface of the oil droplets, as reflected by the analysis of the size, microstructure, rheological behaviours, and driving force of the Pickering emulsion. Hydrophobic interactions and electrostatic interactions were the main driving forces for the formation of colloidal particles, which was determined by driving force analysis and the change of the zeta potential., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

The effects of l-arginine (Arg)-assisted ultrasonic treatment on the molecular and interfacial characteristics of myosin and emulsifying properties of the emulsion were evaluated to ascertain the underlying mechanism in improving the emulsion stability. Ultrasonication induced the exposure of residues of native myosin, which was increased by the addition of Arg (40 mM). Furthermore, in terms of emulsions containing Arg, the higher the ultrasonication intensity was, the greater the increase in adsorbed protein (from 15.43 ± 0.28% to 50.49 ± 1.65%) and π value, and the decrease in droplet sizes (from 4098 nm to 2324 nm) (P < 0.05). Moreover, the increase in the ordered structures of interfacial myosin induced by Arg and ultrasonication favoured the formation of a protein gelation network. In summary, Arg-assisted ultrasonic treatment improved the stability of the emulsion by inducing the exposure of native myosin and facilitating the formation of ordered structures of interfacial myosin., (Copyright © 2020 Elsevier Ltd. All rights reserved.)