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Proteolytic degradation of myofibrillar components by carp cathepsin L
Author(s) -
Ogata Hidehiro,
Aranishi Futoshi,
Hara Kenji,
Osatomi Kiyoshi,
Ishihara Tadashi
Publication year - 1998
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(199804)76:4<499::aid-jsfa980>3.0.co;2-w
Subject(s) - myofibril , carp , cathepsin , chemistry , biochemistry , cathepsin l , myosin , fish fillet , enzyme , biology , fish <actinopterygii> , fishery
Carp cathepsin L, which is the best candidate to produce textural change in the arai ‐treated carp fillet, exhibited maximum hydrolytic activity for Z‐Phe‐Arg‐MCA and soluble casein at pH 5·0–5·5. The proteolytic action of the enzyme was evaluated by complete degradation of various carp myofibrils at pH 5·0 over 30 min and by potent degradation of the same proteins at pH 5·5–6·0 over 20 h. All myofibrillar components were partially degraded by the enzyme at pH 6·5–7·0, but varying amounts of them remained undegraded after 20 h. These findings indicate that carp cathepsin L degrades not only carp myofibrillar components but also their resultant products between pH 5·0 and 7·0 and that it markedly acts on myosin heavy chain, α‐actinin and troponin‐T and ‐I. Carp cathepsin L likely contributes to postmortem muscle tenderisation of carp fillet over an extensive pH range during storage. © 1998 SCI.