Abstract
β-galactosidase enzyme was isolated from Aspergillus niger, and immobilized in sodiumalginate gel. The maximum activity of the free enzyme was obtained at 65oC, pH 3.5 and its notaffected by immobilization. The free enzyme had pH stability range from 3.5 to 6.5 and it wasincreased by immobilization process especially at acid pH values. The free enzyme retained90.28, 85.09, 45.49, and 19.2 % of its initial activity after incubation at 30, 40, 50, and 60oC, for60 min respectively. Thermal stability was enhanced by immobilization process. The kineticparameters for soluble and immobilized enzyme were also determined, and immobilization ledto decrease in Km value (5.12 mM for free form to 1.48 mM for immobilized form), indicatingdecreased affinity by the enzyme for its substrate. Vmax was also decreased by immobilizationprocess, and it was reached from 86.66 μmol ONP.min-1 for free enzyme to .38.02 μMONP.min-1 for immobilized form.
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