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

Yeo Jin Jung; Jung Kee Lee; Chang Geun Sung; Tae Kwang Oh; Hyung Kwoun Kim

doi:10.1016/j.molcatb.2003.06.006

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

Yeo Jin Jung
, Jung Kee Lee
, Chang Geun Sung
, Tae Kwang Oh
, Hyung Kwoun Kim

Biotechnology

Korea Research Institute of Bioscience and Biotechnology
Chungnam National University

Research output: Contribution to journal › Article › peer-review

30 Scopus citations

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 (M_r) of 34,638. Based on the M_r 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 k_cat value of 274s^-1 but a very low K_m value of 0.037mM for PNPC (C₆), therefore, it showed a 14-fold increase in k_cat/K_m value.

Original language	English
Pages (from-to)	223-229
Number of pages	7
Journal	Journal of Molecular Catalysis - B Enzymatic
Volume	26
Issue number	3-6
DOIs	https://doi.org/10.1016/j.molcatb.2003.06.006
State	Published - 1 Dec 2003

Bibliographical note

Funding Information:
This work was supported by the 21C Frontier Microbial Genomics and Applications Center Program, Ministry of Science and Technology (Grant MG02-0301-002-1-0-0), Republic of Korea.

Keywords

Alicyclobacillus acidocaldarius
Bacillus megaterium
Detergent-induced activation
Esterase

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10.1016/j.molcatb.2003.06.006

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title = "Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1",

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.",

keywords = "Alicyclobacillus acidocaldarius, Bacillus megaterium, Detergent-induced activation, Esterase",

author = "Jung, \{Yeo Jin\} and Lee, \{Jung Kee\} and Sung, \{Chang Geun\} and Oh, \{Tae Kwang\} and Kim, \{Hyung Kwoun\}",

note = "Funding Information: This work was supported by the 21C Frontier Microbial Genomics and Applications Center Program, Ministry of Science and Technology (Grant MG02-0301-002-1-0-0), Republic of Korea.",

year = "2003",

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day = "1",

doi = "10.1016/j.molcatb.2003.06.006",

language = "English",

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pages = "223--229",

journal = "Journal of Molecular Catalysis - B Enzymatic",

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T1 - Nonionic detergent-induced activation of an esterase from Bacillus megaterium 20-1

AU - Jung, Yeo Jin

AU - Lee, Jung Kee

AU - Sung, Chang Geun

AU - Oh, Tae Kwang

AU - Kim, Hyung Kwoun

N1 - Funding Information: This work was supported by the 21C Frontier Microbial Genomics and Applications Center Program, Ministry of Science and Technology (Grant MG02-0301-002-1-0-0), Republic of Korea.

PY - 2003/12/1

Y1 - 2003/12/1

N2 - 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.

AB - 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.

KW - Alicyclobacillus acidocaldarius

KW - Bacillus megaterium

KW - Detergent-induced activation

KW - Esterase

UR - https://www.scopus.com/pages/publications/0242575084

U2 - 10.1016/j.molcatb.2003.06.006

DO - 10.1016/j.molcatb.2003.06.006

M3 - Article

AN - SCOPUS:0242575084

SN - 1381-1177

VL - 26

SP - 223

EP - 229

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

IS - 3-6

ER -

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

Abstract

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Keywords

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