Purification and characterization of heparinase that degrades both heparin and heparan sulfate from bacillus circulans

Abstract

A heparinase that degrades both heparin and heparan sulfate (HS) was purified to homogeneity from the cell-free extract of Bacillus circulans HpT298. The purified enzyme had a single band on SDS-polyacrylamide gel electrophoresis with an estimated molecular mass of 111,000. The enzyme showed optimal activity at pH 7.5 and 45°C, and its activity was stimulated in the presence of 5 mM CaCl2, BaCl2, or MgCl2. Analysis of substrate specificity and degraded disaccharides demonstrated that the enzyme acts on both haparin and HS, similar to heparinase II from Flavobacterium heparinum. © 2002, Taylor & Francis Group, LLC. All rights reserved.