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

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Title
Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1
Author(s)
Yeo Jin Jung; Jung-Kee Lee; C G Sung; Tae Kwang Oh; Hyung Kwoun Kim
Bibliographic Citation
Journal of Molecular Catalysis B: Enzymatic, vol. 26, no. 3, pp. 223-229
Publication Year
2003
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.
Keyword
Alicyclobacillus acidocaldariusBacillus megateriumDetergent-induced activationEsterase
ISSN
1381-1177
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.molcatb.2003.06.006
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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