The physical adsorption of a model enzyme, acid phosphatase from potato, on the commercial 13X zeolite was investigated. The highest reached enzyme recovery was 51% at 20°C and 0.01 mg/mL of enzyme in the solution. The formation of multilayers of protein on the support was demonstrated. The immobilization of protein on exchanged forms of the zeolite (replacing Na with Li and K) is less effective. The rate of substrate hydrolysis is controlled by surface kinetics and both interphase and intraphase mass transfer resistances can be neglected. Substrate affinity remains unchanged while operational half-life of the immobilized enzyme significantly increases (up to 1200 min in comparison with 60 min for the free enzyme at 30° c).

Synthetic zeolites as carrier for enzyme immobilization in laboratory-scale fixed bed columns

CANTARELLA M;GALLIFUOCO, ALBERTO
1994-01-01

Abstract

The physical adsorption of a model enzyme, acid phosphatase from potato, on the commercial 13X zeolite was investigated. The highest reached enzyme recovery was 51% at 20°C and 0.01 mg/mL of enzyme in the solution. The formation of multilayers of protein on the support was demonstrated. The immobilization of protein on exchanged forms of the zeolite (replacing Na with Li and K) is less effective. The rate of substrate hydrolysis is controlled by surface kinetics and both interphase and intraphase mass transfer resistances can be neglected. Substrate affinity remains unchanged while operational half-life of the immobilized enzyme significantly increases (up to 1200 min in comparison with 60 min for the free enzyme at 30° c).
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11697/26821
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