Abstract
Composition and some properties of muscle from two species of bigeye snapper, P. tayenus and P. mcracanthus, were investigated. Both species had a similar composition with the same myofibrillar protein content. However, muscle proteins from P. tayenus had higher them1 stability than those from P. macracanthus, as indicated by the higher enthalm for transitions as well as the lower inactivation rate constant (KD). Upon 15 days of iced storage, natural actomyosin Cd'-ATPase and M$'-~'-ATPase aciivities decreased, whereas M&+-EGTA-ATPase activity increased, suggesting the denaturation of myosin, actomyosin andtroponin/tropomyosin complexes, respectively. Increased surface hydrophobicity and decreased suljhydryl groups indicated the denatumtion possibly occurred via hydrophobic interaction and disulfi& formation. Heading and eviscerating offish retarded the denaturation and physicochemical changes of proteins during iced storage. The results indicated that a rapid and proper post harvest handling was of importance to maintain the muscle quality of bigeye snapper.
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