No abstract

Proteolytic activity in muscle from two species of bigeye snapper (Priacanthus macracanthus and Priacanthus tayenus) was studied. Autolysis of mince and washed mince at 50 and 60 • C was compared. Higher degradation of myosin heavy chain was observed in both mince and washed mince from P macracanthus than in those from P tayenus, especially when the incubation time was increased. Autolysis of washed mince from both species was inhibited by soybean trypsin inhibitor, suggesting that myofibril-associated proteases were serine proteases. When sarcoplasmic proteolytic activity in P macracanthus muscle was studied, two activity peaks with an optimum temperature of 60 • C were observed at pH 6.5 and 8.5. The activities of both peaks were mostly inhibited by soybean trypsin inhibitor, suggesting that the major protease was a serine protease. Major sarcoplasmic proteolytic activity in P macracanthus muscle was found at M r 62 000 on sodium dodecyl sulphate substrate gel. For P tayenus sarcoplasmic proteolytic activity, two activity peaks with an optimum temperature of 60 • C were found at pH 5.0 and 8.5. The pH 5.0 peak activity was effectively inhibited by pepstatin A, while the pH 8.5 peak activity was inhibited by several inhibitors. The results indicated that various sarcoplasmic proteases were present in P tayenus muscle. The two species contained different sarcoplasmic proteases in terms of composition and activity level. P macracanthus muscle generally had higher sarcoplasmic proteolytic activities than P tayenus muscle.

No abstract

Composition and some properties of muscle from two species of bigeye snapper, P. tayenus and P. macracanthus, were investigated. Both species had a similar composition with the same myofibrillar protein content. However, muscle proteins from P. tayenus had higher thermal stability than those from P. macracanthus, as indicated by the higher enthalpy for transitions as well as the lower inactivation rate constant (KD). Upon 15 days of iced storage, natural actomyosin Ca2*‐ATP ase and Mg2+‐Ca2+‐ATPase activities decreased, whereas Mg2+‐EGTA‐ATPase activity increased, suggesting the denaturation of myosin, actomyosin and troponin/tropomyosin complexes, respectively. Increased surface hydrophobicity and decreased sulfhydryl groups indicated the denaturation possibly occurred via hydrophobic interaction and disulfide 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.

Effects of some additives on the inhibition of trimethylamine-N-oxide demethylase (TMAOase) from lizardfish (Saurida tumbil) muscle were investigated. Sodium citrate and pyrophosphate could inhibit TMAOase activity in a concentration-dependent manner, most likely because of their chelating property. Sodium alginate was the hydrocolloid possessing the inhibitory activity towards TMAOase (P < 0.05). During the storage of lizardfish mince at )20°C for 24 weeks, the addition of 0.5% sodium alginate and 0.3% pyrophosphate in combination with 4% sucrose and 4% sorbitol as the cryoprotectants resulted in the retarded increase in TMAOase activities with the coincidental lowered formation of dimethylamine and formaldehyde (FA), compared with the control (without additives) (P < 0.05). The loss in solubility of muscle proteins was also impeded with the addition of those compounds, suggesting their role in the inhibition of TMAOase as well as the retardation of protein denaturation induced by FA.