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- Title
Cloning, Expression and Characterization of a Novel Fibrinolytic Serine Metalloproteinase from Bacillus velezensis SW5.
- Authors
Ning, Y. C.; Yang, H. N.; Li, N.; Liu, Y.; Wang, C. Y.; Zhang, X.; Liu, L. L.; Weng, P. F.; Wu, Z. F.
- Abstract
A novel fibrinolytic serine metalloproteinase gene (aprx-sw5) from Bacillus velezensis SW5 was heterologously expressed in Escherichia coli Trans(DE3). Sequence analysis indicated that the open reading frame of aprx-sw5 had 1329 bp, encoding a protein of 442 amino acid residues. In silico analysis described 3D structure of AprX-SW5 for the fist time. The recombinant AprX-SW5 was purified with the molecular weight of 47 kDa. The optimum pH and temperature were 8.0 and 60°C, respectively. The enzyme was significantly activated by Mn2+, almost completely inhibited by PMSF and EDTA, but tolerant to non-ionic surfactants, such as 1% Tween 40, 1% Tween 60 and 1% Tween 80. The enzyme activity was greatly affected by DDT and SDS at the final concentrations of 5 mM. AprX-SW5 retained 81, 48, and 30% relative enzyme activities after incubation with 0.5, 1.0, and 2.0 M NaCl at 4°C for 12 h, respectively. The specific activity of 952 U/mg was evaluated for purified enzyme using fibrin as the substrate. This study indicated that AprX-SW5 may be a potential candidate for use in thrombolytic therapy.
- Publication
Applied Biochemistry & Microbiology, 2021, Vol 57, Issue 1, p48
- ISSN
0003-6838
- Publication type
Article
- DOI
10.1134/S0003683821010154