A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood
2009
Yoshida, A., Nagasaki Univ. (Japan) | Bae, I. | Sonoda, H. | Cao, M.J. | Tachibana, K. | Osatomi, K. | Hara, K.
Collagen degradation is known to be involved in the post mortem tenderization of fish muscle. A serine proteinase that is assumed to be related to collagen degradation after fish death was purified from the sarcoplasmic fraction of red sea bream Pagrus major by ammonium sulfate fractionation and column chromatography on Sephacryl S-300, Q Sepharose and Phenyl Sepharose CL-4B. The enzyme hydrolyzed gelatin and was obtained as a protein band of approximately 38 kDa upon sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions. The N-terminal amino acid sequence of the enzyme was determined for 32 residues. A protein that had the same N-terminal amino acid sequence as the enzyme had for ten residues was purified from the serum of red sea bream and showed the same characteristics as the enzyme. Therefore, it is suggested that the serine proteinase migrates from the blood to muscle and degrades muscle proteins after the death of the fish.
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