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Title 

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

Authors 

Hyung Kwoun KimSun Yang ParkTae Kwang Oh

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

1997

Citation 

Journal of Microbiology and Biotechnology, vol. 7, no. 1, pp. 37-42

Keywords 

Bacillus stearothermophilusThemostability

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.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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