Collect. Czech. Chem. Commun. 1988, 53, 3214-3219

Immobilization of mold beta-galactosidase

Milena Kmínková, Alexandra Prošková and Jiří Kučera

Research Institute of Food Technology, 150 38 Prague 5


We immobilized beta-galactosidase (EC from the mold Aspergillus oryzae by various methods on the derivatives of bead cellulose manufactured by Czechoslovak industry. The activity, specific activity and operational stability of the immobilized enzyme were determined. The best results were obtained with the mold enzyme which had been immobilized by ionic adsorption to DEAHP bead cellulose (Ostsorb DEAHP); its activity was 275 U/g and its operational stability at 40 °C was 30·6 days. The pH-optimum of this enzyme is 4·3 and the optimum temperature determined from the linearized Arrhenius plot is 65 °C. Beta-galactosidase of Kluyveromyces fragilis was also immobilized on the same supports and its properties determined for comparison. The immobilized enzyme from the yeast Kluyveromyces fragilis showed a higher activity in all experiments yet its operational stability was 5 to 14 times lower in the individual cases.