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CROSS‐LINKING OF ACTOMYOSIN BY CRUDE TILAPIA (OREOCHROMIS NILOTICUS) TRANSGLUTAMINASE
Author(s) -
WORRATAO ANULAK,
YONGSAWATDIGUL JIRAWAT
Publication year - 2003
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2003.tb00265.x
Subject(s) - tilapia , oreochromis , dithiothreitol , tissue transglutaminase , chemistry , food science , enzyme , substrate (aquarium) , biochemistry , solubility , aquaculture of tilapia , myosin , fish <actinopterygii> , fishery , biology , ecology , organic chemistry
Tilapia muscle (Oreochromis niloticus) contained the highest transglutaminase (TGase) activity of 60.8 units/g, while striped snake‐head fish (Channa striatus) contained the lowest TGase activity of 2.7 units/g. Optimal temperature and pH of crude tilapia TGase were 50C and 7–7.5, respectively. Crude tilapia TGase had high thermal stability at 6 and 25C for 2 h. TGase activity towards actomyosin was highest at 0.4 M NaCl, but its activity towards monodansylcadaverine (MDC) decreased as NaCl increased. Dithiothreitol (DTT) had no effect on TGase activity regardless of substrate. Solubility and ε‐amino group content of actomyosin were highest at 0.4 and 0.3–0.4 M NaCl, respectively. At optimum conditions, crude tilapia TGase displayed high activity for myosin cross‐linking.