Title of article :
Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1
Author/Authors :
Jung، نويسنده , , Yeo-Jin and Lee، نويسنده , , Jung-Kee and Sung، نويسنده , , Chang-Geun and Oh، نويسنده , , Tae Kwang and Kim، نويسنده , , Hyung Kwoun، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2003
Pages :
7
From page :
223
To page :
229
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 274 s−1 but a very low Km value of 0.037 mM for PNPC (C6), therefore, it showed a 14-fold increase in kcat/Km value.
Keywords :
Alicyclobacillus acidocaldarius , Detergent-induced activation , Bacillus megaterium , esterase
Journal title :
Journal of Molecular Catalysis B Enzymatic
Serial Year :
2003
Journal title :
Journal of Molecular Catalysis B Enzymatic
Record number :
1709926
Link To Document :
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