Microbial-derived CS/DS chain-degrading enzymes (CSases) are polysaccharide lyases that cleave the b1,4 bond between GalNAc and GlcUA residues in CS/DS through a b-elimination reaction, and an unsaturated double bond is formed between the C4 and C5 of the uronic acid. This double bond with a specific absorption at 232 nm can be easily used for analysis and detection of oligosaccharide products. Commercial CSases include: CSase ABC from Proteus vulgaris, which can degrade CS, DS and HA, and notably, CSase ABC is a mixture of two enzymes: endolytic CSase ABCI and non-reducing end exolytic CSase ABCII; CSase ACI and B from Flavobacterium heparinum, where CSase ACI is a CS- and HA-specific endolyase, while CSase B is a DS-specific endolyase; and CSase ACII from Arthrobacter aurescens is CS- and HA-specific exolyase, which is particularly useful in enzymatic sequencing of CS oligosaccharides due to its efficiency in cleaving fluorescently labeled oligosaccharides at the reducing end. CS/DS lyases are not only important tools for studying the structure-activity relationship of CS/DS and preparing CS/DS oligosaccharides, but also has important clinical application potential in the treatment of central nervous system injury. We can provide customers with various CSases with different substrate selectivity, different substrate degradation modes and different specifications to meet the various needs, such as structural and functional studies of CS/DS, production and quality testing of GAGs, large-scale preparation of CS/DS oligosaccharides, etc.

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