Purification and Some Properties of β-Galactosidase from Penicillium multicolor

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β-Galactosidase of a strain of Penicillium multicolor was purified to homogeneity from culture broth. The enzyme was most active at pH 4.0 and at 60°C, and was stable in the pH range 3.5 to 7.5 and below 45°C. Only β-D-galactosides could be substrates. The activity to ONPG was highest among the galactosides tested and about 2-times higher than that to lactose. The apparent Km values were 0.6 and 8.9mM for ONPG and lactose, respectively. Hg2+ and Cu2+ inhibited the activity while the other metal ions tested had no effect. p-Aminophenyl β-D-thiogalactopyranoside inhibited the activity competitively. The molecular weight of the enzyme was estimated to be 1.26×105 and 1.3×105 by sedimentation equilibrium and SDS-polyacrylamide gel electrophoresis, respectively. Leucine and glycine were the N- and C-terminal residues, respectively.
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