Mitsutomi M, Kidoh H, Tomita H, Watanabe T
Department of Applied Biological Sciences, Faculty of Agriculture, Saga University, Japan.
Biosci Biotechnol Biochem. 1995 Mar;59(3):529-31. doi: 10.1271/bbb.59.529.
Both chitinase A1 and D from Bacillus circulans WL-12 specifically hydrolyzed the N-acetyl-beta-D-glucosaminidic bonds in 50% N-acetylated chitosan molecules to produce hetero-oligosaccharides with GlcNAc at the reducing end residues, together with GlcNAc and (GlcNAc)2. GlcN-GlcNAc and GlcN-GlcNAc-GlcNAc were produced as major hydrolysis products with chitinase A1 and D, respectively, but GlcN-GlcNAc was not detected in the digest of 50% N-acetylated chitosan with chitinase D.
来自环状芽孢杆菌WL-12的几丁质酶A1和D均能特异性水解50% N-乙酰化壳聚糖分子中的N-乙酰-β-D-葡糖胺糖苷键,生成还原端残基带有GlcNAc的杂寡糖,以及GlcNAc和(GlcNAc)2。几丁质酶A1和D分别以GlcN-GlcNAc和GlcN-GlcNAc-GlcNAc作为主要水解产物,但在用几丁质酶D消化50% N-乙酰化壳聚糖时未检测到GlcN-GlcNAc。