Cloning, Expression, and Characterization of a Highly Stable Heparinase I from Bacteroides xylanisolvens.

ABSTRACT: Heparinase I (Hep I), which specifically degrades heparin to oligosaccharide or unsaturated disaccharide, has an important role in the production of low molecular weight heparin (LMWH). However, low productivity and stability of heparinase I hinders its applications. Here, a novel heparinase I (BxHep-I) was cloned from Bacteroides xylanisolvens and overexpressed in soluble form in Escherichia coli. The expression conditions of BxHep-I were optimized for an activity of 7144 U/L. BxHep-I had a specific activity of 57.6 U/mg at the optimal temperature and pH of 30 °C and pH 7.5, with the K_m and V_max of 0.79 mg/mL and 124.58 U/mg, respectively. BxHep-I catalytic activity could be enhanced by Ca²⁺ and Mg²⁺, while strongly i

SUBMITTER: Pei JL 

PROVIDER: S-EPMC10097318 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature