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

来源：

FOOD CHEMISTRY | 2005年 / 93卷 / 04期

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

页码：651 / 658

页数：8

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