Proteolytic degradation of myofibrillar components by endogenous proteases in red sea bream muscle

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  • Yoshida Asami
    Graduate School of Fisheries Science and Environmental Studies, Nagasaki University
  • Kurihara Makoto
    Oh-e Plant, Processing Section, Maruha Nichiro Foods, Inc.
  • Ogata Hidehiro
    Graduate School of Fisheries Science and Environmental Studies, Nagasaki University LSI Medience Corporation
  • Cao Min-Jie
    College of Biological Engineering, Jimei University
  • Osatomi Kiyoshi
    Graduate School of Fisheries Science and Environmental Studies, Nagasaki University
  • Hara Kenji
    Graduate School of Fisheries Science and Environmental Studies, Nagasaki University

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  • マダイ筋肉中の内在性プロテアーゼによる筋肉構成タンパク質の分解

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Abstract

Degradation of myofibrillar proteins is one of the causes of post-mortem muscle softening of fish. In order to clarify the endogenous proteases responsible for fish muscle softening, we injected specific protease inhibitors into the duct of Cuvier of live red sea bream to suppress the endogenous protease activities under similar physiological conditions. After sacrificing the fish, we confirmed the effects of protease inhibitors on degradation of myofibrillar components by western blot analysis during storage at 25℃. Degradation of myosin heavy chain (MHC) and β-connectin were significantly suppressed by leupeptin, diisopropyl fluorophosphate (DFP) (serine protease inhibitors), and o-phenanthroline (a metalloproteinase inhibitor). Hydrolysis of α-actinin was inhibited by E-64 (a cysteine protease inhibitor). Degradation of troponin I was suppressed by leupeptin, DFP, o-phenanthroline, and E-64. The limited degradation of tropomyosin was inhibited by DFP and o-phenanthroline. Our results suggested that endogenous serine proteases and metalloproteinases were involved in degradation of most of the myofibrillar components (MHC, β-connectin, troponin I, and tropomyosin) while α-actinin was hydrolyzed only by cysteine proteases in red sea bream muscle.

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