Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus
2001
Benjakul, S. | Visessanguan, W. | Ishizaki, S. | Tanaka, M.
Natural actomyosin (NAM) of P. tayenus exhibited higher turbidity and storage modulus (G') upon heating, compared to that of P. macracanthus, suggesting the higher protein aggregation and rigidity. At temperature above 35 degrees C, P. tayenus NAM had higher surface hydrophobicity and disulfide bond formation than P. macracanthus NAM. The alpha-helix content of NAM from both fish species decreased as the temperature increased, indicating changes in structural conformation during heating. NAM gel from P. tayenus rendered more three-dimensional network than that from P. macracanthus. These results indicated that P. tayenus NAM possessed superior gelling characteristic to P. macracanthus NAM due to the higher aggregation of protein caused by both hydrophobic interaction and disulfide bond.
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