IMMOBILIZATION OF OXALATE DECARBOXYLASE TO EUPERGIT AND PROPERTIES OF THE IMMOBILIZED ENZYME |
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Authors: | Rihui Lin Ruchun Wu Xinlin Huang Tao Xie |
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Affiliation: | 1. Key Laboratory of Chemical and Biological Transforming, College of Chemistry and Ecology Engineering , Guangxi University for Nationalities , Nanning, China linrihui_0@yahoo.com.cn;3. Key Laboratory of Chemical and Biological Transforming, College of Chemistry and Ecology Engineering , Guangxi University for Nationalities , Nanning, China |
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Abstract: | Oxalate decarboxylase, an oxalate degradation enzyme used for medical diagnosis and decreasing the oxalate level in the food or paper industry, was covalently immobilized to Eupergit C. Different immobilization parameters, including ratio of enzyme to support, ammonia sulfate concentration, pH, and incubation time, were optimized. Under the condition of enzyme/support ratio at 1:20, pH 9, with 1.5 mol/L (NH4)2SO4, room temperature, and shaking at 30 rpm for 24 hr, activity recovery of immobilized Oxdc reached 90% with an apparent specific activity of 0.44 U/mg support. The enzymatic properties of immobilized Oxdc were investigated and compared with those of the soluble enzyme. Both shared a similar profile of optimum conditions; the optimum pH and temperature for soluble and immobilized Oxdc were 3.5 and 50°C, respectively. The immobilized enzyme was more stable at lower pH and higher temperatures. The kinetic parameters for soluble and immobilized enzyme were also determined. |
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Keywords: | enzyme properties Eupergit C immobilization oxalate decarboxylase |
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