Kinetics of adsorption of β-galactosidase on silica gel

The specific activities of tetramers and dimers [0.67 and 0.2 (muM S)/(min mg E), respectively] and the equilibrium association constant (1.4 x 10(5) M-1) for Penicillium Canescens beta-galactosidase were determined. The kinetics of adsorption of beta-galactosidase on silica gel was studied. It was shown that the association of the protein occurs through the solution. The adsorption was found to be a two-stage process: the protein is first weakly and then strongly bounded to the carrier. Three kinetic parameters of adsorption for the accepted scheme were calculated from the experimental data obtained. A kinetic analysis allowed us to calculate three rate constants for this mechanism. The beta-galactosidase enzyme (KF 3.2.1.23) from Penicillium Canescens had a complex quaternary structure. Solutions of the enzyme were equilibrium mixtures of active dimers and tetramers.