Abstract
The relative activity and thermal stability of native and covalently immobilized glucose oxidase (GOD) onto polyamide-6 (PA-6) membrane was studied at temperatures of 28, 45 and 60 °C for 10 h and in the presence of organic solvents (methylol, ethyleneglycol, glycerol) with concentrations 10%, 30% and 60%. It was proven that immobilized GOD had better stability than the native one in all the three organic solvents. At 28 °C, the strongest activating and stabilizing effect on the free GOD was observed with 10% methylol and on the immobilized GOD with 10% and 30% methylol. The addition of certain concentrations of ethyleneglycol and glycerol to the enzyme at higher temperatures was found to stabilize the enzyme molecule. At temperatures of 45 and 60 °C, the strongest stabilizing effect on both forms of the enzyme was exerted by glycerol (optimal stabilizing concentration of 10%). It was concluded that the most stable form of the enzyme was GOD covalently immobilized onto PA-6 membrane in the presence of 10% solution of glycerol.
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