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The properties of mutant glucoamylases(GlaBs) from Aspergillus oryzae H-1 and G-4 strains with a high level of GlaB activity were compared with those of native GlaBs from parental strains. Amino acid compositions of both mutant GlaBs were different from those of native GlaBs, with a particular decrease in Ser residue of mutant GlaBs. Moreover, N-linked suger chains of native and mutant GlaBs were considered a complex or hybrid type, and not a high mannose type. Because N-linked sugar chain of each GlaB mainly consisted of galactose and N-acetylglucosamine, there was little mannose. Since a little more galactose and N-acetylglucosamine combined per mannose were found in the N-linked suger chains of mutant GlaBs than of native GlaBs, this suggested that each N-linked sugar chain length of mutant GlaBs was possibly shorter. Native GlaBs were not deglycosylated with Endoglycosidase H, while both mutant GlaBs were deglycosylated. This result suggests N-linked suger chain structures of both mutant GlaBs changed from a complex type in native GlaBs to a hybrid type. In circular dichroism spectra analysis, Tm values of GlaBs from H-1 and G-4 strains were approximately 53°C both, and thus similar to Tm of native GlaBs. Therefore, the thermostability of mutant GlaBs was shown as not being affected by mutation.

Comparison of Biochemical Properties of Wild Type Glucoamylases and Those of High Glucoamylase Mutant Strains of <i>Aspergillus oryzae</i>