Changes in sarcoplasmic proteins during the burnt meat occurrence of cultured yellowtail were investigated using SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and 2D-gel electrophoresis. The decreased proteins during burnt meat occurrence were identified as muscle glycogen phosphorylase (PYGM), phosphoglycerate kinase (PGK), creatine kinase (CK), glyceraldehydes-3-phosphate dehydrogenase (GAPDH),
L-lactate dehydrogenase (LDH) and adenylate kinase, respectively, by MALDI-QIT-TOF mass spectrometry (MALDI-QIT-TOFMS). The decreases of sarcoplasmic proteins were little suppressed by the protease inhibitors
in vitro. In contrast, some sarcoplasmic proteins such as PYGM, GAPDH and aldolase were appeared in myofibril fraction of burnt meat. These results suggested that the sarcoplasmic proteins are insolubilized and shifted to myofibrillar fraction, when the burnt meat occurs in cultured yellowtail.
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