Characterization of beta-galactosidase from a special strain of Aspergillus oryzae.
beta-Galactosidase [EC 3.2.1.23] was isolated from a partially purified preparation obtained from cultured cells of a special strain of Aspergillus oryzae, RT 102 (FERM-P1680). The enzyme preparation gave a single protein band on polyacrylamide gel electrophoresis and was free from alpha-galactosidase, alpha- and beta-mannosidase, alpha- and beta-N-acetylhexosaminidase, and protease activities. The beta-galactosidase was capable of acting on aryl beta-galactosides, lactose, and lactosides. It also hydrolyzed beta-galactosyl linkages in urinary glycoasparagines and asialo alpha1-acid glycoprotein. The enzyme was rather stable in aqueous solution, retaining full activity at 4 degrees for at least several months. At pH 4.5, the optimum pH for the enzyme activity, and 37 degrees, full activity was maintained for several days.
D001216:Asparagine / Q000652:urine; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D005696:Galactosidases / Q000302:isolation & purification / Q000378:metabolism*; D006020:Glycopeptides / Q000378:metabolism / Q000652:urine; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007785:Lactose / Q000378:metabolism
D006020:Glycopeptides; D001216:Asparagine; D005696:Galactosidases; D007785:Lactose