Matrix metalloproteinases(MMPs)play essential roles in the metabolism of collagens;however,information regarding MMPs in aquatic animals is limited.To elucidate the specific role of MMPs in shrimp muscle degradation,p...Matrix metalloproteinases(MMPs)play essential roles in the metabolism of collagens;however,information regarding MMPs in aquatic animals is limited.To elucidate the specific role of MMPs in shrimp muscle degradation,proteinases with gelati-nolytic activity were identified in the hepatopancreas of Litopenaeus vannamei(Lv).The gelatinolytic activity was suppressed by metalloproteinase inhibitors EDTA and EGTA to some degree,suggesting the existence of metalloproteinases.Then the catalytic do-main of LvMMP-2(LvMMP-2c)was cloned and expressed heterologously in the Pichia pastoris expression system.rLvMMP-2c(re-combinant LvMMP-2c)demonstrated optimal gelatinolytic activity at pH 8.0 and 50℃,and its activity could be enhanced by Ca^(2+)and Ba^(2+).Type I collagen and myofibrillar proteins from shrimp were effectively hydrolyzed by rLvMMP-2c not only at 37℃,but also at 4℃,indicating its involvement in the postmortem tenderization of shrimp muscle.Our present study provided new informa-tion to elucidate the role of metalloproteinase underlying shrimp meat softening during cold storage,and suggested new strategies to prevent shrimp quality decrement during cold storage.展开更多
基金supported by the National Key R&D Program of China(No.2018YFD0901004)the National Natural Science Foundation of China(No.31772049)the Agricultural Guidance Program of Fujian Province(No.2024N0057).
文摘Matrix metalloproteinases(MMPs)play essential roles in the metabolism of collagens;however,information regarding MMPs in aquatic animals is limited.To elucidate the specific role of MMPs in shrimp muscle degradation,proteinases with gelati-nolytic activity were identified in the hepatopancreas of Litopenaeus vannamei(Lv).The gelatinolytic activity was suppressed by metalloproteinase inhibitors EDTA and EGTA to some degree,suggesting the existence of metalloproteinases.Then the catalytic do-main of LvMMP-2(LvMMP-2c)was cloned and expressed heterologously in the Pichia pastoris expression system.rLvMMP-2c(re-combinant LvMMP-2c)demonstrated optimal gelatinolytic activity at pH 8.0 and 50℃,and its activity could be enhanced by Ca^(2+)and Ba^(2+).Type I collagen and myofibrillar proteins from shrimp were effectively hydrolyzed by rLvMMP-2c not only at 37℃,but also at 4℃,indicating its involvement in the postmortem tenderization of shrimp muscle.Our present study provided new informa-tion to elucidate the role of metalloproteinase underlying shrimp meat softening during cold storage,and suggested new strategies to prevent shrimp quality decrement during cold storage.
