Purification and characterization of transglutaminase from Tropical tilapia (Oreochromis niloticus)

被引:48
作者
Worratao, A [1 ]
Yongsawatdigul, J [1 ]
机构
[1] Suranaree Univ Technol, Sch Food Technol, Inst Agr Technol, Nakhon Ratchasima 30000, Thailand
关键词
transglutaminase; tilapia (Oreochromis niloticus); purification;
D O I
10.1016/j.foodchem.2004.09.044
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Transglutaminase (TGase) from Tropical tilapia (Oreochromis niloticus) was purified to electrophoretic homogeneity using successive chromatographies of DEAE-Sephacel, Sephacryl S-4 HR and HiTrap Heparin with a yield and purification-fold of 12.9% and 69.8, respectively. The molecular weight (MW) of the purified tilapia TGase was estimated to be 85 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The isoelectric point (pI) of tilapia TGase was 6.53. Optimal temperature and optimal pH of tilapia TGase were 37-50 degrees C and 7.5, respectively. Optimal concentrations of CaCl2 and dithiothreitol (DTT) were at 1.25 and 5 mM, respectively. The activity of TGase towards monodansylcadaverine (MDC) decreased as the NaCl concentration increased. Chelating agents, ethylenediaminetetra acetic acid (EDTA) and ethylene glycol-O,O'-bis(2-aminoethyl)N,N,N',N'-tetraacetic acid (EGTA), inhibited TGase activity. Tilapia TGase was strongly inactivated by p-chloromercuribenzoic acid (PCMB), N-ethylmaleimide (NEM), iodoacetamide (IAA), Cu2+, and Zn2+, suggesting a thiol group at the active site. (c) 2005 Elsevier Ltd. All rights reserved.
引用
收藏
页码:651 / 658
页数:8
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