Characterization of myosin subfragment-1 of summer and winter silver carp (Hypophthalmichthys molitrix) muscle.

UNLABELLED

Myosin subfragment-1 (S1) was prepared from myofibrils of summer and winter silver carp by chymotryptic digestion in the presence of ethylenediaminetetraacetic acid (EDTA). Two S1 heavy chain isoforms with different molecular sizes of 91 kDa and 95 kDa were detected in the fast skeletal muscle from summer and winter silver carp, respectively. ATPase inactivation assay indicated that winter S1 was about 20-fold unstable comparing to summer S1. Matrix-assisted laser desorption/ionization time-of-flight/mass spectrometry (MALDI-TOF MS) further confirmed that summer and winter myosin S1 heavy chain isoforms were homologous to myosin high-temperature type and myosin low-temperature type S1 heavy chain, respectively. Moreover, both types of myosin S1 heavy chain isoforms were identified at the intermediate stage. The results indicated that myosin was expressed in a season-specific manner; different types of myosin isomer expressed in different seasons, showing different thermostabilities.

PRACTICAL APPLICATION

Silver carp, Hypophthalmichthys molitrix, is one of the most abundant freshwater fish species in China. The structure thermal stability of myosin rod from silver carp was affected by season change. The gel-forming abilities of surimi prepared in different seasons were different. This study investigated the seasonal differences in structure thermal stability of myosin S1 which is vital for gel formation of myosin. The results of this study will aid understanding of the relationship between the structure and function of myosin, and effective production of surimi from freshwater fish species in different seasons.