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Myofibril‐Bound Serine Proteinase (MBP) and its Degradation of Myofibrillar Proteins
Author(s) -
Cao M.J.,
Hara K.,
Osatomi K.,
Tachibana K.,
Izumi T.,
Ishihara T.
Publication year - 1999
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1999.tb15102.x
Subject(s) - myofibril , tropomyosin , myosin , chemistry , proteolysis , protein degradation , biochemistry , serine , actin , enzyme
Proteolysis of a myofibril‐bound serine proteinase (MBP) from carp Cyprinus carpio on myofibrillar proteins and their gel formation ability were investigated. MBP readily decomposed myosin heavy chain as indicated by SDS‐PAGE. In the preparation of kamaboko, the gel formation ability was diminished by addition of MBP. The optimum degradation temperatures of MBP to myosin heavy chain in myofibril and kamaboko gel were 55°C and 60°C, respectively. The degradation effects of MBP on actin, α‐actinin and tropomyosin were studied by the immunoblotting method. Because of its myofibril‐bound and myofibrillar protein degradation characteristics, MBP was regarded as the proteinase most probably involved in the modori effect.