Salt-soluble proteins were extracted from bovine longissimus thoracis muscles (BLTM). Effects of pea protein on physicochemical properties (SDS-PAGE, solubility, surface hydrophobicity, sulfhydryl group, disulfide bond content, emulsifying properties) and secondary structures of salt-soluble proteins from BLTM were studied. Additionally, the types of chemical bonds formed during the gelling of pea protein and salt-soluble proteins were explored. The SDS-PAGE results indicated that vicilin (7S), legA, and legB in pea protein were bound to actin, troponin T, and troponin C in salt-soluble proteins. When 0.08 g/mL pea protein was added, the surface hydrophobicity of salt-soluble protein increased significantly (P<0.05). Moreover, the disulfide bond content increased rapidly when more than 0.12 g/mL pea protein was added (P<0.05). As the concentration of pea protein increasing, the contents of both total sulfhydryl and surface active sulfhydryl of salt-soluble proteins decreased, while their turbidity and emulsibility increased. Furthermore, the solubility of salt-soluble proteins increased first and then decreased, with the maximal reached when 0.04 g/mL pea protein was added. Additionally, the amount of pea protein added was negatively correlated with α-helix and surface active sulfhydryl content, and it was positively correlated with β-folding, β-rotation, irregular curl, disulfide bond content, and surface hydrophobicity of salt soluble proteins. Besides, hydrophobic interaction was the most important chemical force when forming pea protein- BLTM salt soluble proteins gel network structure.
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