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Substrate specificity of alpha-galactosidase from Aspergillus niger 5-16
1Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Abstract:
This paper describes the specificity of Aspergillus niger 5-16 alpha-galactosidase toward various oligosaccharides having terminal galactose or stub galactose or both on the oligosaccharide. The galactosidase rapidly hydrolyzed p-nitrophenyl-alpha-D-galactopyranoside, but hardly liberated galactose from melibiose, manninotriose, 6(3)-alpha-D-galactosylmannotriose, etc. On the other hand, the enzyme tore off the stub galactoses attached to the inner mannoses of the main-chain of galactomannooligosaccharides, but not the terminal galactoses attached to the non-reducing-end mannoses of the main-chain. Thus, the substrate specificity of A. niger 5-16 alpha-galactosidase is quite different from that of Mortierella vinacea alpha-galactosidase.