Biochemical Analysis of a Fibrinolytic Enzyme Purified from Bacillus subtilis Strain A1

Won Sik Yeo; Min Jeong Seo; Min Jeong Kim; Hye Hyeon Lee; Byoung Won Kang; Jeong Uck Park; Yung Hyun Choi; Yong Kee Jeong

doi:10.1007/s12275-011-1165-3

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Research Support, Non-U.S. Gov't
Biochemical Analysis of a Fibrinolytic Enzyme Purified from Bacillus subtilis Strain A1: Won Sik Yeo ¹, Min Jeong Seo ², Min Jeong Kim ¹, Hye Hyeon Lee ¹, Byoung Won Kang ², Jeong Uck Park ², Yung Hyun Choi ³, Yong Kee Jeong ^1,2; Journal of Microbiology 2011;49(3):376-380.
DOI: https://doi.org/10.1007/s12275-011-1165-3
Published online: June 30, 2011

¹Department of Biotechnology, Dong-A University, Busan 604-714, Republic of Korea, ²Medi-Farm Industrialization Research Center, Busan 604-714, Republic of Korea, ³Department of Biochemistry, College of Oriental Medicine, Dong-Eui University, Busan 614-050, Republic of Korea

Corresponding author: Yong Kee Jeong , Tel: +82-51-200-7557,

Received: 31 March 2011 • Accepted: 8 June 2011

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Abstract

A fibrinolytic enzyme from Bacillus subtilis strain A1 was purified by chromatographic methods, including DEAE Sephadex A-50 column chromatography and Sephadex G-50 column gel filtration. The purified enzyme consisted of a monomeric subunit and was estimated to be approximately 28 kDa in size by SDS-PAGE. The specific activity of the fibrinolytic enzyme was 1632-fold higher than that of the crude enzyme extract. The fibrinolytic activity of the purified enzyme was approximately 0.62 and 1.33 U/ml in plasminogen-free and plasminogen-rich fibrin plates, respectively. Protease inhibitors PMSF, DIFP, chymostatin, and TPCK reduced the fibrinolytic activity of the enzyme to 13.7, 35.7, 15.7, and 23.3%, respectively. This result suggests that the enzyme purified from B. subtilis strain A1 was a chymotrypsin-like serine protease. In addition, the optimum temperature and pH range of the fibrinolytic enzyme were 50°C and 6.0-10.0, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as Q-T-G-G-S-I-I-D-P-I-N-G-Y-N, which was highly distinguished from other known fibrinolytic enzymes. Thus, these results suggest a fibrinolytic enzyme as a novel thrombolytic agent from B. subtilis strain A1.

Keywords: amidolytic activity;Bacillus subtilis strain A1;fibrinolytic enzyme;plasminogen activator;N-terminal amino acid sequence

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Biochemical Analysis of a Fibrinolytic Enzyme Purified from Bacillus subtilis Strain A1

J. Microbiol. 2011;49(3):376-380. Published online June 30, 2011

DOI: https://doi.org/10.1007/s12275-011-1165-3

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