Purification and Biochemical Characterization of a 17 kDa Fibrinolytic Enzyme from Schizophyllum commune

In Suk Park; Jeong Uck Park; Min Jeong Seo; Min Jeong Kim; Hye Hyeon Lee; Sung Ryeal Kim; Byoung Won Kang; Yung Hyun Choi; Woo Hong Joo; Yong Kee Jeong

doi:10.1007/s12275-010-0384-3

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Purification and Biochemical Characterization of a 17 kDa Fibrinolytic Enzyme from Schizophyllum commune: In Suk Park ¹, Jeong Uck Park ², Min Jeong Seo ³, Min Jeong Kim ¹, Hye Hyeon Lee ¹, Sung Ryeal Kim ¹, Byoung Won Kang ², Yung Hyun Choi ⁴, Woo Hong Joo ⁵, Yong Kee Jeong ^1,2,3; Journal of Microbiology 2010;48(6):836-841.
DOI: https://doi.org/10.1007/s12275-010-0384-3
Published online: January 9, 2011

¹Department of Biotechnology, Dong-A University, Busan 604-714, Republic of Korea, ²Medi-Farm Industrialization Research Center, Dong-A University, Busan 604-714, Republic of Korea, ³Department of Medical Bioscience, Dong-A University, Busan 604-714, Republic of Korea, ⁴Department of Biochemistry, College of Oriental Medicine, Dong-Eui University, Busan 614-050, Republic of Korea, ⁵Department of Biology, Changwon National University, Kyungnam 641-713, Republic of Korea

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

Received: 27 September 2010 • Accepted: 26 October 2010

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Abstract

A fibrinolytic enzyme of the mushroom, Schizophyllum commune was purified with chromatographic methods, including a DEAE-Sephadex A-50 ion-exchange column and gel filtrations with Sephadex G-75 and Sephadex G-50 columns. The analysis of fibrin-zymography and SDS-PAGE showed that the enzyme was a monomeric subunit that was estimated to be approximately 17 kDa in size. The fibrinolytic activity of the enzyme in plasminogen-rich and plasminogen-free fibrin plates was 1.25 and 0.44 U/ml, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as HYNIXNSWSSFID, which was highly distinguished from known fibrinolytic enzymes. The relative activity of the purified enzyme with an addition of 5 mM EDTA, Phosphoramidon, and Bestatin was about 76, 64, and 52%, respectively, indicating that it is a metalloprotease. The optimum temperature for the purified enzyme was approximately 45°C, and over 87% of the enzymatic activity was maintained as a stable state in a pH range from 4.0 to 6.0. Therefore, our results suggest that the potential thrombolytic agent from S. commune is a unique type of fibrinolytic enzyme.

Keywords: fibrinolytic enzyme;fibrin-zymography;N-terminal amino acid sequence;mushroom;S. commune

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Purification and Biochemical Characterization of a 17 kDa Fibrinolytic Enzyme from Schizophyllum commune

J. Microbiol. 2010;48(6):836-841. Published online January 9, 2011

DOI: https://doi.org/10.1007/s12275-010-0384-3

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