Title of article
Covalent immobilization of invertase on microporous pHEMA–GMA membrane
Author/Authors
Danisman، نويسنده , , Tarik and Tan، نويسنده , , Sema and Kacar، نويسنده , , Yasemin and Ergene، نويسنده , , Aysun، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2004
Pages
6
From page
461
To page
466
Abstract
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 °C 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.
Keywords
pHEMA–GMA membrane , Enzyme immobilization , Invertase , Covalent bonding , epoxy groups
Journal title
Food Chemistry
Serial Year
2004
Journal title
Food Chemistry
Record number
1950936
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