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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus / chemistry
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Bacillus / enzymology*
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Bacillus / genetics
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Bacillus subtilis / genetics
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Bacillus subtilis / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics*
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Bacterial Proteins / metabolism
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Cloning, Molecular*
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Gene Expression*
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Kinetics
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Molecular Sequence Data
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Sequence Alignment
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Serine Endopeptidases / chemistry
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Serine Endopeptidases / genetics*
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Serine Endopeptidases / metabolism
Substances
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Bacterial Proteins
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Serine Endopeptidases
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bacillopeptidase F