Abstract
β-Galactosidase from Kluyveromyces lactis was covalently immobilized onto a mPOS–PVA, using glutaraldehyde as activating agent and its properties were evaluated. The enzymatic water insoluble derivative displayed the same optimum pH (6.5) and optimum temperature (50 °C) of the soluble enzyme. The apparent Kmapp and activation energy for both soluble and immobilized enzyme derivative were found to be not significantly different. The mPOS–PVA β-galactosidase preparation presented a higher operational and thermal stability than the soluble enzyme. This immobilized β-galactosidase also was effective in hydrolyzing lactose from milk. Hence, one can conclude that mPOS–PVA is an attractive and efficient support for β-galactosidase immobilization.
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