Department of Food and Nutrition, University of Helsinki, 00014 Helsinki, Finland.
Department of Food and Nutrition, University of Helsinki, 00014 Helsinki, Finland.
Food Chem. 2022 Mar 15;372:131347. doi: 10.1016/j.foodchem.2021.131347. Epub 2021 Oct 7.
The subcellular distribution of calpain-1 and -2 and the proteolytical activity of myofibril-bound calpains in pork were investigated during 12 days cold storage. The content of sarcoplasmic calpain-1 decreased during storage while myofibril-bound calpain-1 content first increased (P < 0.05) to 17% of that of 12 h-sarcoplasmic calpain-1 on day 6 followed by a gradual decrease with subsequent storage, suggesting that calpain-1 gradually translocated from sarcoplasm to myofibrils during the initial 6 days of postmortem storage. Intact desmin decreased (P < 0.05) after incubation of myofibrils with 0.05 mM Ca, and this was more pronounced with 5 mM Ca (P < 0.05). Ca titration curves of day 6 myofibrils showed two distinct proteolytic activities becoming activated in the range 0.03 to 0.06 mM and 0.4 to 0.8 mM Ca, respectively. The results suggest that both calpain-1 and calpain-2 binds to myofibrils during storage and subsequently degrade structural proteins including desmin.
在 12 天的冷藏过程中,研究了钙蛋白酶-1 和 -2 的亚细胞分布以及肌原纤维结合钙蛋白酶在猪肉中的蛋白水解活性。贮藏过程中肌浆钙蛋白酶-1 的含量逐渐下降,而肌原纤维结合钙蛋白酶-1 的含量先增加(P<0.05),在第 6 天达到 12 小时肌浆钙蛋白酶-1 的 17%,随后随着贮藏时间的延长逐渐减少,表明钙蛋白酶-1 在死后贮藏最初 6 天内逐渐从肌浆向肌原纤维转移。用 0.05 mM Ca 孵育肌原纤维后,完整的结蛋白减少(P<0.05),用 5 mM Ca 时更为明显(P<0.05)。第 6 天肌原纤维的钙滴定曲线显示,两种不同的蛋白水解活性分别在 0.03 至 0.06 mM 和 0.4 至 0.8 mM Ca 范围内被激活。结果表明,钙蛋白酶-1 和钙蛋白酶-2 在贮藏过程中都与肌原纤维结合,随后降解包括结蛋白在内的结构蛋白。