Proteomic Analysis of Mechanisms Responsible for the Waterless Preservation of Fenneropenaeus chinensis Based on Cold-Forced Hibernation

Abstract

ABSTRACTIn this study, the comparative proteomic approach was used to identify the proteins that were changed significantly during the waterless preservation of Chinese white shrimp (Fenneropenaeus chinensis). Approximately 380–430 protein spots were observed in the two-dimensional protein electrophoresis (2-DE) gels. Among them, 14 altered proteins from hemolymph were excised and subjected to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis. Eleven protein spots were successfully identified—including hemocyanin, hemolymph clottable protein, myosin light chain, and sarcoplasmic calcium-binding protein. It could be speculated that the combined action of decreased hemocyanin, increased hemolymph clottable protein, and myosin light chain forced Chinese white shrimp into a temporary state of hibernation under cold temperature and could keep the hibernated shrimps alive during the waterless preservation. Moreover, increased expression of sarcoplasmic calcium-binding protein ensured that hibernated shrimps could be aroused at warm temperature. On the basis of these findings, it is believed that a protein-protein networking mechanism of hemocyanin, hemolymph clottable protein, myosin, and sarcoplasmic calcium-binding protein could interpret the cold-forced hibernation and warm-arousal of Chinese white shrimp.