4.7 Article

Covalent immobilization of invertase on microporous pHEMA-GMA membrane

Journal

FOOD CHEMISTRY
Volume 85, Issue 3, Pages 461-466

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2003.07.015

Keywords

pHEMA-GMA membrane; epoxy groups; covalent bonding; enzyme immobilization; invertase

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Poly (2-hydroxyethyl methacrylate-glycidyl methacrylate) (pHEMA-GMA) membrane was prepared by UV-initiated photopolymerization. Invertase was immobilized by the condensation reaction of the epoxy groups of glycidyl methacrylate in the membrane structure with amino groups of the enzyme. The (Km) values were 22 mM and 58 mM for free and immobilized enzyme, respectively. Immobilization improved the pH stability and temperature stability of the enzyme. Thermal stability was found to increase with immobilization. The half times for the activity decay at 70 degreesC were found to be 11 and 38 min for the free and immobilized enzyme, respectively. The immobilized enzyme activity was found to be quite stable in later experiments. (C) 2003 Elsevier Ltd. All rights reserved.

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