Abstract
Oligosaccharidase activity of a neutral β-N-acetylglucosaminidase from carp blood was examined. The enzyme hydrolyzed the trisaccharides (GlcNAcβ1-4GlcNAcβ1-4GlcNAc and GlcNAcβ1-4GlcUAβ1-3GlcNAc) derived from chitin and hyaluronic acid, but did not hydrolyze the trisaccharide (GalNAcβ1-4GlcUAβ1-3GalNAc) derived from chondroitin. The C-4 configuration of thenon-reducing terminal N-acetylhexosamine in substrates is an important determinant of the specificity of the enzyme, while the subterminal sugar and position of β-linkage are not strictly required by the enzyme.
