Myofibrin-bound serine proteinase (MBP) and its degradation of myofibrillar proteins

Citation
Mj. Cao et al., Myofibrin-bound serine proteinase (MBP) and its degradation of myofibrillar proteins, J FOOD SCI, 64(4), 1999, pp. 644-647
Citations number
26
Categorie Soggetti
Food Science/Nutrition
Journal title
JOURNAL OF FOOD SCIENCE
ISSN journal
00221147 → ACNP
Volume
64
Issue
4
Year of publication
1999
Pages
644 - 647
Database
ISI
SICI code
0022-1147(199907/08)64:4<644:MSP(AI>2.0.ZU;2-8
Abstract
Proteolysis of a myofibril-bound serine proteinase (MBP) from carp Cyprinus carpio on myofibrillar proteins and their gel formation ability were inves tigated, 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 h eavy chain in myofibril and kamaboko gel were 55 degrees C and 60 degrees C , respectively. The degradation effects of MBP on actin, alpha-actinin and tropomyosin were studied by the immunoblotting method. Because of its myofi bril-bound and myofibrillar protein degradation characteristics, MBP was re garded as the proteinase most probably involved in the modori effect.