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Title 

Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1

Authors 

Yeo Jin JungJung-Kee LeeC G SungTae Kwang OhHyung Kwoun Kim

Publisher 

Elsevier

Issue Date 

2003

Citation 

Journal of Molecular Catalysis B:Enzymatic, vol. 26, no. 3, pp. 223-229

Keywords 

alicyclobacillus acidocaldariusbacillus megateriumdetergent-induced activationesterasedetergentsenzyme activationalicyclobacillus

Abstract 

An esterase-producing Bacillus megaterium strain (20-1) was isolated from a soil sample collected in South Korea. The cloned gene showed that the esterase 20-1 composed of 310 amino acids corresponding to a molecular mass (Mr) of 34,638. Based on the Mr and the protein sequence, the esterase 20-1 belonged to the H lipase/esterase group. The optimum temperature and pH of the purified His-tagged enzyme were 20-35°C and 8.0, respectively. The esterase 20-1 showed a 'nonionic detergent-induced activation' phenomenon, which was a detergent type- and concentration-dependent process. In comparison with the native enzyme, the Tween 80-treated enzyme had relatively a similar kcat value of 274s-1 but a very low Km value of 0.037mM for PNPC (C6), therefore, it showed a 14-fold increase in kcat/Km value.

ISSN 

1381-1177

Link 

http://dx.doi.org/10.1016/j.molcatb.2003.06.006

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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