This study investigated the effects of octenyl succinic anhydride-modified starch (OSA starch) at different concentrations (0, 0.5, 1.0, 1.5, and 2.0 g/100 mL) on the emulsion properties and volatile flavor compounds of snakehead fish soup. The results showed that the oil droplets in the fish soup became smaller and more uniformly distributed as the addition level of OSA starch increased. Confocal laser scanning microscopy (CLSM) revealed that the average diameter of oil droplets decreased from 5.98 μm in the control group to 4.24 μm at an OSA starch concentration of 2.0 g/100 mL. The addition of OSA starch reduced the adsorption of proteins at the oil-water interface, leading to a gradual decrease in the absolute value of the emulsion’s zeta potential, while the contact angle of the emulsion increased. Electronic nose (E-nose) analysis indicated that the response values of sensors W1C and W2S, which are sensitive to aromatic compounds and alcohols, respectively, increased with higher OSA starch concentration, peaking at 1.0 g/100 mL before declining. Gas chromatography-mass spectrometry (GC-MS) analysis revealed that the relative contents of volatile compounds such as nonanal, (E)-2-heptenal, and trans-2-octenal were significantly higher in the OSA starch-treated groups than those in the control group, while the content of 1-octen-3-ol generally elevated. In conclusion, increasing the OSA starch concentration progressively reduced the oil droplet size in the fish soup emulsion, thereby promoting the release of volatile flavor compounds.

Water-holding capacity is an important quality attribute of fresh meat. It is closely related to eating quality attributes such as tenderness, juiciness and color. Water-holding capacity also affects the mass of meat when marketed. Therefore, water-holding capacity has a focus of attention in the meat industry. This paper reviews the fundamental theory of the water-holding capacity of meat and its recent developments. A brief introduction is given to the microstructure of muscle and water distribution in muscle. The roles of electrostatic forces, osmotic pressure, and capillary forces in the water-holding capacity of meat are summarized, and the methods used for water-holding measurement are reviewed. Finally, the latest research progress on the water-holding mechanism in meat is discussed with a focus on net charge and microstructure. This comprehensive review will provide a theoretical basis for meat research and production.

The purpose of this study was to explore the effect of freeze treatment on the binding characteristics of fillets to flavor substances in fish soup with pickled mustard greens. The study focused on the effects of freeze-thaw treatment and freeze storage on the physicochemical properties of snakehead myofibrillar protein and its binding characteristics to hexanal, octanal, linalool and myrcene. The results showed that after 7 days of storage, the solubility of myofibrillar protein decreased by about 26% in the freeze-thaw group. Compared with the freeze storage group, the oxidation degree and tertiary structural changes of myofibrillar protein were higher and more soluble aggregates were formed in the freeze-thaw group. The solubility of myofibrillar protein decreased by about 33% in the freeze storage group, which showed a more significant decrease compared to the freeze-thaw treatment (P < 0.05), resulting in more insoluble aggregates. The major force for the aggregation of myofibrillar proteins after freezing was non-covalent bonding. Molecular docking results indicated that linalool, hexanal and octanal could bind to myofibrillar proteins through hydrophobic interactions and hydrogen bonds, while the major driving force for the binding of myrcene to myofibrillar proteins was hydrophobic interaction. Freeze treatment reduced the binding capacity of hexanal and octanal to sulfhydryl groups in myofibrillar proteins through hydrogen bonds, improved the surface hydrophobicity of myofibrillar proteins, but increased the binding ability of myrcene and linalool to myofibrillar proteins. Freeze-thaw treatment increased the binding capacity of myofibrillar proteins to myrcene compared with freeze storage treatment. The results of this research provide a theoretical basis and reference for flavor control of frozen prepared fish soup with pickled mustard greens.