Beta-galactosidase of Penicillium chrysogenum: production, purification, and characterization of the enzyme |
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Authors: | Nagy Z Kiss T Szentirmai A Biró S |
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Institution: | Faculty of Natural Sciences, Department of Microbiology and Biotechnology, Department of Biochemistry, University of Debrecen, Egyetem tér 1, H-4010 Debrecen, Hungary. |
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Abstract: | 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. |
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