Hyaluronic acid-degrading enzymes derived from microorganisms are polysaccharide lyases, so they are often called HA lyases (HAase) (EC 4.2.2.1). This type of enzyme cleaves the β-1,4 glycosidic bond between GlcNAc and GlcUA residues in HA chain through a β-elimination reaction to create an unsaturated double bond between the C4 and C5 of the uronic acid, which has a specific absorption at 232 nm and therefore can be conveniently used for analysis and detection of oligosaccharide products. HAase has been found in a variety of bacteria, such as Proteus, Bacteroides fragilis, Streptococcus, Staphylococcus, Peptostreptococcus, Propionibacterium, Streptomyces, Clostridium, and Vibrio, etc. Most HAases have chondroitin/chondroitin sulfate-degrading activity, and thus are often classified into CSase AC. Many HAases initially behave as endonucleases when degrading substrates, randomly binding and cutting HA/CS chains, and then behave as exonucleases. Therefore, unsaturated disaccharides are often observed quick accumulation but the proportion of large-sized oligosaccharides is always very low during substrate degradation. In our products, in order to avoid confusion, we classify HAases with both HA- and CS-degrading activities into CSase AC. We can provide a variety of HAases with different specific activities and substrate-structure selectivity according to customers’ needs. Here, HAase refers to the HA-specific degrading enzyme from Streptomyces hyalurolyticus, etc., which can be used as a specific tool for HA detection in biological samples and purity analysis of HA preparations.

 Products: