Cloning and expression of a bpr gene encoding bacillopeptidase F from Bacillus amyloliquefaciens CH86-1

Gun Hee Kwon; Jae Yong Park; Jong Sang Kim; Jinkyu Lim; Cheon Seok Park; Dae Young Kwon; Jeong Hwan Kim

doi:10.4014/jmb.1010.10061

Cloning and expression of a bpr gene encoding bacillopeptidase F from Bacillus amyloliquefaciens CH86-1

Gun Hee Kwon, Jae Yong Park, Jong Sang Kim, Jinkyu Lim, Cheon Seok Park, Dae Young Kwon, Jeong Hwan Kim

School of Food Science & Biotechnology

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

9 Scopus citations

Abstract

A gene encoding bacillopeptidase F, bpr86-1, was cloned from B. amyloliquefaciens CH86-1 isolated from cheonggukjang. This gene could encode a preproenzyme of 1,431 amino acids. When bpr86-1 was introduced into B. subtilis WB600 via pHY300PLK, an E. coli-Bacillus shuttle vector, the transformant showed fibrinolytic activity. During growth on LB, the fibrinolytic activity of cells increased sharply when they entered the stationary phase. The highest activity (761.4 mU/mg protein) was observed at 96 h of cultivation.

Original language	English
Pages (from-to)	515-518
Number of pages	4
Journal	Journal of Microbiology and Biotechnology
Volume	21
Issue number	5
DOIs	https://doi.org/10.4014/jmb.1010.10061
State	Published - May 2011

Keywords

Bacillopeptidase F
Bacillus amyloliquefaciens CH86-1
Bpr gene
Fibrinolytic enzymes

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10.4014/jmb.1010.10061

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title = "Cloning and expression of a bpr gene encoding bacillopeptidase F from Bacillus amyloliquefaciens CH86-1",

abstract = "A gene encoding bacillopeptidase F, bpr86-1, was cloned from B. amyloliquefaciens CH86-1 isolated from cheonggukjang. This gene could encode a preproenzyme of 1,431 amino acids. When bpr86-1 was introduced into B. subtilis WB600 via pHY300PLK, an E. coli-Bacillus shuttle vector, the transformant showed fibrinolytic activity. During growth on LB, the fibrinolytic activity of cells increased sharply when they entered the stationary phase. The highest activity (761.4 mU/mg protein) was observed at 96 h of cultivation.",

keywords = "Bacillopeptidase F, Bacillus amyloliquefaciens CH86-1, Bpr gene, Fibrinolytic enzymes",

author = "Kwon, {Gun Hee} and Park, {Jae Yong} and Kim, {Jong Sang} and Jinkyu Lim and Park, {Cheon Seok} and Kwon, {Dae Young} and Kim, {Jeong Hwan}",

year = "2011",

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T1 - Cloning and expression of a bpr gene encoding bacillopeptidase F from Bacillus amyloliquefaciens CH86-1

AU - Kwon, Gun Hee

AU - Park, Jae Yong

AU - Kim, Jong Sang

AU - Lim, Jinkyu

AU - Park, Cheon Seok

AU - Kwon, Dae Young

AU - Kim, Jeong Hwan

PY - 2011/5

Y1 - 2011/5

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AB - A gene encoding bacillopeptidase F, bpr86-1, was cloned from B. amyloliquefaciens CH86-1 isolated from cheonggukjang. This gene could encode a preproenzyme of 1,431 amino acids. When bpr86-1 was introduced into B. subtilis WB600 via pHY300PLK, an E. coli-Bacillus shuttle vector, the transformant showed fibrinolytic activity. During growth on LB, the fibrinolytic activity of cells increased sharply when they entered the stationary phase. The highest activity (761.4 mU/mg protein) was observed at 96 h of cultivation.

KW - Bacillopeptidase F

KW - Bacillus amyloliquefaciens CH86-1

KW - Bpr gene

KW - Fibrinolytic enzymes

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SN - 1017-7825

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JO - Journal of Microbiology and Biotechnology

JF - Journal of Microbiology and Biotechnology

IS - 5

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Cloning and expression of a bpr gene encoding bacillopeptidase F from Bacillus amyloliquefaciens CH86-1

Abstract

Keywords

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