Isolation and properties of α-Galactosidase from Aspergillus Awamori.
Biokhimiya, 56 (3), pp. 447 - 457, (1991)
The α-galactosidase from Asp. awamori var. XIOO/D27 was studied. Yeast galactomannan, raffinose, melibiose, galactose and lactose were tested as enzyme secretion inducers. The enzyme isolated with a 60% yield and purified 416-fold was found to be a glycoprotein of 91—93 kDa; it contains about 25% of the sugar portion consisting of alkaline labile O-carbohydrate chains. Data from amino acid analysis performed before and after reductive β-elimination suggest that the enzyme bears about 30 sugar chains bound equally to the serine and threonine moieties. α-Galactosidase has a pI of 4.7, a pH optimum at 4.5 and a temperature optimum of 55° C. The enzyme is stable: in the presence of human serum albumin it retains its activity at pH optimum over a period of 12 weeks at 37° C. The enzyme exhibits rather a broad aglycon specificity and is unable to hydrolyze B-group substances of human erythrocytes into H(0) ones.