文献类型： 外文期刊

作者： Ning, Y. C. ¹ ; Yang, H. N. ¹ ; Li, N. ¹ ; Liu, Y. ¹ ; Wang, C. Y. ¹ ; Zhang, X. ¹ ; Liu, L. L. ¹ ; Weng, P. F. ¹ ; Wu, Z. F ¹ ;

作者机构： 1.Ningbo Univ, Coll Food & Pharmaceut Sci, Lab Food Biotechnol, Ningbo 315211, Zhejiang, Peoples R China

2.Henan Univ Anim Husb & Econ, Sch Food & Bioengn, Lab Food Biotechnol, Zhengzhou 450046, Henan, Peoples R China

3.Fujian Acad Agr Sci, Inst Qual Stand & Testing Technol Agroprod, Fuzhou 350003, Fujian, Peoples R China

关键词： Bacillus velezensis; fibrinolytic serine metalloproteinase; gene expression

期刊名称：APPLIED BIOCHEMISTRY AND MICROBIOLOGY （ 影响因子：0.886； 五年影响因子：0.956 ）

ISSN： 0003-6838

年卷期： 2021 年 57 卷 1 期

页码：

收录情况： SCI

摘要： 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 degrees 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 degrees 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.