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Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1 |
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| Authors: | Yeo-Jin Jung Jung-Kee Lee Chang-Geun Sung Tae Kwang Oh Hyung Kwoun Kim |
| Affiliation: | a Division of Biosciences and Technology, The Catholic University of Korea, 43-1 Yokkok 2-dong, Wonmi-gu, Bucheon, Gyeonggido 420-743, South Korea b Laboratory of Microbial Genomics, Korea Research Institute of Bioscience and Biotechnology, P.O. Box 115, Yusong, Daejon 305-600, South Korea c Department of Food Science Technology, Chungnam National University, 220 Kung-Dong, Yusong, Daejon 305-764, South Korea |
| 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: | Esterase Bacillus megaterium Alicyclobacillus acidocaldarius Detergent-induced activation |
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