Purification and characterization of recombinant nattokinase from Bacillus subtilis

Authors

  • Tran Quoc Tuan VAST
  • Le Thi Thuy Ai
  • Dinh Minh Hiep
  • Tran Cat Dong

DOI:

https://doi.org/10.15625/0866-7160/v37n1se.6094

Keywords:

Bacillus subtillis, characterization, nattokinase, purification, recombinant

Abstract

Nattokinase, a thrombosis-degradation serin protease, is obtained from Bacillus subtilis Natto. The enzyme has been clinically proven effective and safe in the treatment of thrombotic disease in humans orally. Nattokinase is produced by solid-state fermentation (SSF) of soybean by Bacillus subtilis Natto so yield and quality should be limited. In recent years, there have been initially researches recombinant nattokinase in bacterial systems (Escherichia coli, Bacillus subtilis, Lactobacillus). This study conducted purified recombinant nattokinase from Bacillus subtillis DB104 strain and surveyed some properties of nattokinase. The crude enzyme was precipitated at 70% saturation of (NH4)2SO4. The optimal pH value and temperature were 8.0 and 55oC, respectively and alkaline stability within the range of pH 6.0-10. The molecular weight of Nattokinase was approximately 27.7 kDa. The apparent Vmax and Km values were 0.306 µmol/min/ml and 6.778, respectively. The enzyme was activated with Mg2+, Zn2+, Ca2+ and obviously inhibited by Mn2+ and Hg2+.

Downloads

Download data is not yet available.

Downloads

Published

25-04-2015

How to Cite

Tuan, T. Q., Thuy Ai, L. T., Hiep, D. M., & Dong, T. C. (2015). Purification and characterization of recombinant nattokinase from Bacillus subtilis. Academia Journal of Biology, 37(1se), 75–84. https://doi.org/10.15625/0866-7160/v37n1se.6094

Issue

Section

Articles

Most read articles by the same author(s)