[Purification and properties of beta-galactosidase from fungus, Curvularia inaequalis].
Highly purfied beta-galactosidase from fungus Curvularia inaequalis cultural fluid with a specific activity of 50 units per mg of protein was obtained by 2-fold purification of the enzyme, using chromatography on DEAE-cellulose and on hydroxylapatite. The enzyme was found to hydrolyze o-nitrophenyl-beta-D-galactopyranoside (pH optimum of 3.7--4.5) and lactose (pH optimum 3.9--5.3). The isoelectric point was observed at pH 4.4 the temperature optimum was 60 degrees C. The molecular weight (115 000--126 000) and the amino acid composition of the enzyme were determined. Km values for o-nitrophenyl-beta-D-galactopyranoside and lactose were 0.55-10(-3) M and 4.5-10(-3) M respectively. Disc-electrophoresis in polyacrylamide gel revealed a single band with a specific activity. The homogeneity of the enzyme was found in ultracentrifuge.
D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000032:analysis / Q000302:isolation & purification*; D006868:Hydrolysis; D007785:Lactose / Q000302:isolation & purification; D003904:Mitosporic Fungi / Q000201:enzymology*; D008970:Molecular Weight; D009598:Nitrophenylgalactosides / Q000302:isolation & purification
D009598:Nitrophenylgalactosides; D005696:Galactosidases; D007785:Lactose
Ochistka i svoĭstva beta-galaktozidazy iz griba Curvularia inaequalis.