Beta-galactosidase of Penicillium chrysogenum: production, purification, and characterization of the enzyme.
Intracellular beta-galactosidase from Penicillium chrysogenum NCAIM 00237 was purified by procedures including precipitation with ammonium sulfate, ion-exchange chromatography on DEAE-Sephadex, affinity chromatography, and chromatofocusing. These steps resulted a purification of 66-fold, a yield of about 8%, and a specific activity of 5.84 U mg(-1) protein. Some enzyme characteristics were determined using o-nitrophenyl-beta-d-galactopyranoside as substrate. The pH and temperature optimum of the activity were about 4.0 and 30 degrees C respectively. The K(m) and pI values were 1.81 mM and 4.6. beta-Galactosidase of P. chrysogenum is a multimeric enzyme of about 270 kDa composed of monomers with a molecular mass of 66 kDa.
Nagy
Z
Z
Faculty of Natural Sciences, Department of Microbiology and Biotechnology, Department of Biochemistry, University of Debrecen, Egyetem tér 1, H-4010 Debrecen, Hungary.
Kiss
T
T
Szentirmai
A
A
Biró
S
S
D002846:Chromatography, Affinity / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D010408:Penicillium chrysogenum / Q000201:enzymology*; D013816:Thermodynamics; D014462:Ultrafiltration; D001616:beta-Galactosidase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
D001616:beta-Galactosidase