Abstract
The kinetic properties of commercial β-galactosidase (Escherichia coli K-12) bonded to .8cm x 1.3cm Teflon stirring bars via a polyisocyanate polymer were compared to those of the soluble enzyme. Assays of immobilized β-galactosidase were performed with test tubes placed in a 37C water-jacketed container positioned on top of a stirring motor set at 80±5rpm. The Michaelis-Menten constants for soluble and immobilized β-galactosidase at pH 6.5 were 13.1mM and 22.1mM. The pH optimum for immobilized β-galactosidase shifted upward .8 pH units relative to the soluble enzyme. Activation energies for hydrolysis of lactose were 15,200 cal/mole and 12,500 cal/mole for soluble and immobilized β-galactosidase. The immobilized β-galactosidase exhibited good stability, retaining 65.6% of the original activity after intermittent use for 118 days. When not in use, the immobilized β-galactosidase was stored at 4C in .1M phosphate buffer (pH 6.5).
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