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J. Biochem, 1982, Vol. 91, No. 6 1971-1979
© 1982 Japanese Biochemical Society

research-article

Purification and Characterization of 1,2-{alpha}-Mannosidase of Aspergillus oryzae

Kozo YAMAMOTO, Jun HITOMI, Kanae KOBATAKE and Haruki YAMAGUCHI1

Department of Agricultural Chemistry, College of Agriculture, University of Osaka Prefecture Sakai, Osaka 591

1,2-{alpha}-Mannosidase was purified approximately 1,400-fold from an enzyme product of Aspergillus oryzae. The enzyme showed a single band in disc gel electropho-resis and the molecular weight was estimated to be about 49,000 daltons by gel exclusion chromatography. The substrate specificity of the enzyme was examined with mannooligosaccharides, yeast mannan, glycopeptides, and a glycoprotein. The {alpha}-(1->2)-linking mannose residues located at the nonreducing-ends of the substrates were selectively removed by the enzyme, whereas p-nitrophenyl {alpha}-D-mannopyrano-side was completely stable to the enzyme. {alpha}-(1->2)-Linking mannose residues in intact bovine pancreatic ribonuclease B were also removed completely with the enzyme. The enzyme showed an optimum pH in the range of pH 4.9 to 5.3 and had a Km value of 0.57 idm with 1,2-{alpha}-mannobiose. The present {alpha}-mannosidase was quite stable, and the activity was inhibited by D-mannono-{gamma}-lactone and by heavy metal ions, including zinc ions.

1To whom requests for reprints should be addressed.


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