Chondroitinase AC from Arthrobacter aurescens

Chondroitinase AC is an eliminase that degrades chondroitin sulfates A and C, but not chondroitin sulfate B. The enzyme cleaves, via an elimination mechanism, sulfated and non-sulfated polysaccharide chains containing (1-4) linkages between hexosamines and glucuronic acid residues. The reaction yields oligosaccharide products, mainly disaccharides, containing unsaturated uronic acids that can be detected by UV spectroscopy at 232 nm.
The enzyme shows approximately equal activity with chondroitin sulfates A and C, while the activity observed with chondroitin sulfate B is approximately 7% of this value. This activity is most likely due to the presence of chondroitin sulfates A and C (10%) in the chondroitin sulfate B.

One unit will liberate 1.0 μmole of 2-acetamido-2-deoxy-3-O-(β-D-gluc-4-ene-pyranosyluronic acid)-4-O-sulfo-D-galactose from chondroitin sulfate A or 1.0 μmole of 2-acetamido-2-deoxy-3-O-(β-D-gluc-4-ene-pyranosyluronic acid)-6-O-sulfo-D-galactose from chondroitin sulfate C per min at pH 6.0 at 37 °C.