Preliminary communication

https://doi.org/10.17113/ftb.53.02.15.3874

Purification and Characterisation of a Fibrinolytic Enzyme from Rhizopus micro sporus var. tuberosus

Shuli Zhang ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China
Yingdong Wang ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China
Nan Zhang ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China
Zhe Sun ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China
Yan Shi ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China
Xingnan Cao ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China
Haikuan Wang ; Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Ministry of Education, Tianjin , PR China

Abstract

Extracellular fibrinolytic enzyme from Rhizopus microsporus var. tuberosus was purified and characterised. The microorganism was isolated in a distillery from daqu, a fermentative agent used in the production of Chinese liquor and vinegar at diff erent temperatures. The fibrinolytic enzyme was partially purifi ed by ammonium sulphate precipitation, dialysis, DEAE Sepharose® Fast Flow ion exchange chromatography and Sephadex G-75 gel filtration chromatography. The molecular mass of the fi brinolytic enzyme was estimated to be 24.5 kDa by SDS-PAGE. The purified enzyme showed optimal activity at pH=7.0 and 37 °C by fibrin plate method. It showed stronger resistance to the inhibition by trypsin and was stable at 37 °C retaining 96.1 % residual activity aft er 4 h of incubation. The fibrinolytic activity of the enzyme was enhanced by Na+, Ca2+, Mg2+ and Mn2+. Conversely, Zn2+ and Cu2+ partly inhibited enzymatic activity. Using fibrin plate method, we found that the enzyme not only degrades fibrin directly, but also activates plasminogen into plasmin to degrade fibrin. The results indicate that the pure enzyme has a potential in dissolving blood clot, and the possibility for application in the treatment of thrombosis.

Keywords

Rhizopus microsp orus var. tuberosus; fibrinolytic enzyme; purification; characterisation

Hrčak ID:

140242

URI

https://hrcak.srce.hr/140242

Publication date:

23.6.2015.

Article data in other languages: croatian

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