Abstract
In this study, β-galactosidase from Kluyveromyces lactis was immobilized onto graphite surface using glutaraldehyde as the cross-linking reagent with the specific activity yield of 17% and 25%, while the enzyme loading was 1.8 and 1.1 U/cm 2 of the graphite external surface area, respectively. The activity yield was decreased with the increase of the enzyme loading. The Michaelis–Menten kinetics parameters, K m and V m for the free enzyme were estimated to be 1.74 mM and 77.34 μmol o-nitrylphenol min −1 mg −1 enzyme, respectively. The K m value of the immobilized enzyme was found to be of five folds of the free enzyme. Lactose hydrolysis at concentrations of 5% (w/v) by the immobilized enzyme was also investigated. The degree of lactose hydrolysis was approximately 70% at 37°C over a period of 3 h. The immobilized enzyme showed a good storage and operational stability.
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