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  • Title: Beta-galactosidase of Penicillium chrysogenum: production, purification, and characterization of the enzyme.
    Author: Nagy Z, Kiss T, Szentirmai A, Biró S.
    Journal: Protein Expr Purif; 2001 Feb; 21(1):24-9. PubMed ID: 11162383.
    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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