Transglycosylation activity of endoglycoceramidase from Corynebacterium sp

Endoglycoceramidase (EGCase) catalyzes the hydrolysis of the linkage between oligosaccharides and ceramides of various glycosphingolipids (GSLs). We found that the EGCase from Corynebacterium sp. had transglycosylation activity. Digesting GSLs with the enzyme in the presence of a suitable acceptor gave a mixture of hydrolytic and transglycosylic products. When GM1 was used as the substrate (donor), 1-hexanol was found to be the best acceptor of transglycosylation activity. Hexyl-II 3NeuAcGgOse4 produced was confirmed by fast-atom bombardment-mass spectrometry analysis and exoglycosidase digestion. The enzyme also transferred oligosaccharides of various GSLs to 1-hexanol.