Glycosidases induced in Aspergillus tamarii. Mycelial alpha-D-galactosidases

Biochem J. 1984 May 1;219(3):849-55. doi: 10.1042/bj2190849.


Two alpha-D-galactosidases (alpha-D-galactoside galactohydrolase, EC produced by Aspergillus tamarii were purified from the mycelial extract by a procedure including chromatography on hydroxyapatite, DEAE-cellulose and ECTEOLA-cellulose. Each of these enzymes showed a single protein band corresponding to the alpha-D-galactosidase activity when examined by polyacrylamide-gel electrophoresis. They catalysed the hydrolysis of o-nitrophenyl alpha-D-galactoside, melibiose, raffinose and stachyose, but did not attack the galactomannans. Their Mr values were respectively 265000 +/- 5000 and 254000 +/- 5000 by the method of Hedrick & Smith [(1968) Arch. Biochem. Biophys. 126, 155-164]. Polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate in each case showed a single protein band, with Mr 88000 and 77500 respectively. The purified enzymes contained carbohydrate, consisting of N-acetylglucosamine, mannose, glucose and galactose in the estimated molar proportions of 1:9:5:8 in alpha-galactosidase I.

MeSH terms

  • Aspergillus / enzymology*
  • Cations / pharmacology
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme Induction
  • Galactosidases / biosynthesis*
  • Hexoses / analysis
  • Hydrogen-Ion Concentration
  • Molecular Weight
  • Substrate Specificity
  • alpha-Galactosidase / biosynthesis*
  • alpha-Galactosidase / isolation & purification


  • Cations
  • Hexoses
  • Galactosidases
  • alpha-Galactosidase