Acid-induced aggregation of actomyosin from silver carp (Hypophthalmichthys molitrix) |
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Authors: | Yanshun Xu Wenshui Xia Qixing JiangShengqi Rao |
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Affiliation: | State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu 214122, China |
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Abstract: | Acid-induced denaturation and aggregation properties of silver carp actomyosin added with d-gluconic acid-δ-lactone (GDL) during incubation at chilled temperature (4 °C) were studied. Actomyosin underwent aggregation with decreasing pH, as evidenced by increased turbidity and decreased protein solubility in 0.6 M NaCl solution. Ca2+-ATPase activity decreased continually with increasing incubation time in the presence of GDL, accompanied by an initial increase in surface reactive sulphydryl (SH) content, indicating the conformation changes of actomyosin during acidification. Protein solubility in selected solvents and electrophoresis analysis showed that the major myofibrillar proteins, particularly, myosin heavy chain and actin were involved in the formation of protein aggregates mainly through noncovalent bonds including hydrophobic interactions and hydrogen bonds during acidification. The slight decrease in total SH content during acidification suggested that disulphide bonds were also involved in acid-induced aggregation of silver carp actomyosin to a lesser extent. |
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Keywords: | Silver carp Actomyosin Acid-induced gelation Aggregation Interaction |
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