Heparinase I can degrade heparin and heparan sulfate, making it a powerful tool for heparin structural research, clinical diagnosis, and industrial quality control.

Heparinase I selectively cleaves the linkages between glucosamine and O-sulfated iduronic acid in heparin and heparan sulfate (relative activity approximately 3:1), with the main products being disaccharides. This enzyme can also cleave the pentasaccharide binding site of antithrombin III within heparin molecules.

Heparinase I, derived from Bacteroides fragilis, is widely utilized in heparinase I applications, including as a raw material for diagnostic reagents in thromboelastography heparin cups.