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J. Microbiol. Biotechnol. 2010; 20(2): 370-374

Published online February 28, 2010 https://doi.org/10.4014/jmb.0906.06029

Copyright © The Korean Society for Microbiology and Biotechnology.

Cloning of aprE86-1 Gene Encoding 27 kDa Mature Fibrinolytic Enzyme from Bacillus amyloliquefaciens CH86-1

Ae Ran Lee 1, Gyoung Min Kim 1, Gun-Hee Kwon 2, Kang Wook Lee 1, Jae-Yong Park 2, Jiyeon Chun 3, Jaeho Cha 4, Young-Sun Song 5 and Jeong Hwan Kim 1, 2*

1Division of Applied Life Science (BK21) Graduate School, Gyeongsang National University Jinju 660-701, Korea, 2Institute of Agriculture and Life Science, Gyeongsang National University Jinju 660-701, Korea, 3Department of Food Science and Technology, Sunchon National University Sunchon 540-742, Korea, 4Department of Microbiology, Pusan National University, Busan 609-735, Korea, 5School of Food and Life Science, Inje University, Gimhae 621-749, Korea

Received: June 17, 2009; Accepted: September 17, 2009

Abstract

A gene, encoding the major secreted fibrinolytic protein of Bacillus amyloliquefaciens CH86-1, was cloned from the genomic DNA. DNA sequencing showed that the gene, aprE86-1, could direct the synthesis of a mature protein of 275 amino acids long after processing. When aprE86-1 was introduced into B. subtilis, 27 kDa mature protein was produced as expected. The fibrinolytic activity of B. subtilis transformant (TF) was higher than that of B. amyloliquefaciens CH86-1, showing the possibility of increasing fibrinolytic activities of Bacillus strains through genetic engineering.

Keywords: Bacillus amyloliquefaciens, fibrinolytic enzymes, gene expression