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KMID : 1094720110160020352
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Biotechnology and Bioprocess Engineering
2011 Volume.16 No. 2 p.352 ~ p.359
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Cloning and overexpression of aprE3-17 encoding the major fibrinolytic protease of Bacillus licheniformis CH 3-17
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Jo Hyeon-Deok
Kwon Gun-Hee
Park Jae-Yong
Cha Jae-Ho
Song Young-Sun
Kim Jeong-Hwan
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Abstract
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Bacillus licheniformis (B. licheniformis) CH3-17, an isolate from cheonggukjang, a traditional Korean fermented soyfood, secretes several fibrinolytic enzymes into the culture medium, showing strong fibrinolytic activity. A gene homologous to aprE of Bacillus subtilis (B. subtilis), aprE3-17, was cloned by PCR. DNA sequencing showed that aprE3-17 encodes a prepro-type serine protease consisting of 382 amino acids. The mature enzyme was 27 kDa in size. The aprE3-17 gene was overexpressed in B. subtilis WB600 using pHY300PLK, an Escherichia coli (E. coli)-Bacillus shuttle vector, and the 27 kDa enzyme was purified from the culture supernatant. The optimum pH for activity was 6.0. Purified enzyme quickly degraded the Aα and Bβ chains of fibrinogen but could not degrade the γ-chain.
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KEYWORD
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fibrinolytic enzyme, bacilli, gene expression, Bacillus licheniformis, fermented soyfood
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