Characterisation of thermostable trypsin and determination of trypsin isozymes from intestine of Nile tilapia (Oreochromis niloticus L.)

Article ID	Journal	Published Year	Pages	File Type
10539605	Food Chemistry	2012	9 Pages	PDF

Abstract

âº Trypsin from Nile tilapia was purified showing a molecular weight of 22.39Â kDa. âº The purified trypsin active in high pH (6.0-11.0) and temperature (55-60Â Â°C). âº The purified enzyme was dramatically increased in the presence of detergents. âº The Km and Kcat of the purified trypsin for BAPNA were 0.16Â mM and 23.81Â Sâ1. âº At least 6 isoforms of trypsin was found in different ages.

Keywords

BAPNA PMSF SDS Vmax kcat/Km DTT BSA Kcat bovine serum albumin Thermostable enzyme EDTA Ethylenediaminetetraacetic acid sodium dodecyl sulphate-polyacrylamide gel electrophoresis SDS-PAGE Catalytic efficiency Tame Enzyme purification Nile tilapia catalytic constant maximum velocity Michaelis–Menten constant dithiothreitol sodium dodecyl sulphate Enzyme kinetics phenylmethylsulfonyl fluoride

Related Topics

Physical Sciences and Engineering Chemistry Analytical Chemistry

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Characterisation of thermostable trypsin and determination of trypsin isozymes from intestine of Nile tilapia (Oreochromis niloticus L.)

Authors

Sasimanas Unajak, Piyachat Meesawat, Atchara Paemanee, Nontawith Areechon, Arunee Engkagul, Uthaiwan Kovitvadhi, Satit Kovitvadhi, Krisna Rungruangsak-Torrissen, Kiattawee Choowongkomon,