Purification and partial characterization of thermostable carboxyl esterase from Bacillus stearothermophilus L1

Cited 0 time in scopus
Metadata Downloads
Title
Purification and partial characterization of thermostable carboxyl esterase from Bacillus stearothermophilus L1
Author(s)
Hyung Kwoun Kim; Sun Yang Park; Tae Kwang Oh
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 7, no. 1, pp. 37-42
Publication Year
1997
Abstract
A bacterial strain LI producing a thermostable esterase was isolated from soil taken near a hot spring and identified as Bacillus stearothermophilus by its microbiological properties. The isolated thermostable esterase was purified by ammonium sulfate fractionation, ion exchange and hydrophobic interaction chromatographies. The molecular weight of the purified enzyme was estimated to be 50,000 by SDS-PAGE. Its optimum temperature and pH for hydrolytic activity against PNP caprylate were 85°C and 9.0, respectively. The purified enzyme was stable up to 70°C and at a broad pH range of 4.0-11.5 in the presence of bovine serum albumin. The enzyme was inhibited by phenylmethylsulfonyl fluoride and diethyl p-nitrophenyl phosphate, indicating the enzyme is a serine esterase. The enzyme obeyed Michaelis-Menten kinetics in the hydrolysis of PNPEs and had maximum activity for PNP caproate (C6) among PNPEs (C2- C12) tested.
Keyword
Bacillus stearothermophilusThemostability
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.