Degradation of myofibrillar proteins in the belly muscle of the threadfin bream is caused by the possible leaking of soluble serine proteinase from the viscera during storage.
Degradation of myofibrillar proteins in the belly muscle of the threadfin bream is caused by the possible leaking of soluble serine proteinase from the viscera during storage.
复制标题
鳊鱼腹部肌肉中肌原纤维蛋白的降解是由于储存过程中可溶性丝氨酸蛋白酶可能从内脏泄漏而引起的。
DOI:
10.1007/s12562-019-01398-w
复制
发表时间:
2020
影响因子:
1.9
通讯作者:
Kiyoshi Osatomi
中科院分区:
文献类型:
--
作者:
4)Jin-Yang Liu;Asami Yoshida;Yi-Li Gao;Kazuya Shirota;Yasuhiko Shiina;Kiyoshi Osatomi
The present work aims to clarify the mechanism of gel weakening (modoriphenomenon) onsurimi-based products and provide information on how to prevent it from happening in threadfin bream. We investigated the distribution of endogenous proteinases in the normal and belly muscles and their effects on the quality of thesurimigel. There was severe degradation of myofibrillar proteins in the belly muscle during heating at 50 °C, which was not found in the normal muscle. Thesurimigel prepared from the belly muscle also showed a low gel strength as compared to that of the normal muscle. The myofibrillar proteins in the belly muscle were found to be degraded by a sarcoplasmic serine proteinase (SSP). The SSP activity was detected in the belly muscle and hepatopancreas but not in the normal muscle, while the SSP mRNA was detected only in the hepatopancreas. It is suggested that SSP in the hepatopancreas leaks to the belly muscle during post-harvest storage and is responsible for themodoriphenomenon. These results imply that high-qualitysurimigel of the threadfin bream can be produced by preventing protease leakage to the muscle during post-harvest storage.