Hep/HS-degrading enzymes (Hepases) from microorganisms are polysaccharide lyases that cleave the a-1,4 glycosidic bond between GlcNAc and GlcUA/IdoUA in Hep/HS through a b-elimination mechanism, and an unsaturated double bond with specific absorption at 232 nm is generated at the C4 and C5 of the uronic acid. The introduction of this double bond is beneficial to the analysis and detection of enzymatic products. HEPases have been identified in various Hep/HS-degrading bacteria, such as Flavobacterium heparinum, Bacteroides thetaiotaomicron, Bacteroides stercoris, Sphingomonas, Bacillus, Pseudomonas aeruginosa, etc. Based no substrate selectivity, HEPases can be divided into three categories: HEPase I, which selectively degrades the highly sulfated regions in Hep and HS, HEPase III, which selectively degrades the low sulfated regions in HS and Hep, and HEPase II, which can simultaneously degrade both Hep and HS. The above three types of HEPases are all endolyases, and recently a family of Hep/HS exolyases (exoHEPases) was discovered for the first time. As important tools, HEPases are widely used in the structural and functional studies of Hep/HS, the production of low molecular weight heparin, and the quality testing and consistency evaluation of heparin-related drugs. We can provide customers with various known types of HEPases according to their needs from basic studies to large-scale applications.

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