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Barley oxalate oxidase immobilized on zirconia-coated alkylamine glass using glutaraldehyde.
Indian J Biochem Biophys ; 1993 Feb; 30(1): 54-7
Article in English | IMSEAR | ID: sea-26239
ABSTRACT
A method for immobilizing barley oxalate oxidase to zirconia coated alkylamine glass through the process of glutaraldehyde coupling has been described. The immobilized enzyme retained 97.2% of the specific activity, with a conjugation yield of 6.63 mg/g support and showed an increase in optimum pH. The Km value of immobilized enzyme was unaltered but Vmax was decreased compared to free enzyme. The conjugated enzyme was stable at 4 degrees C for 2 years. A number of inorganic ions and metabolic substances did not denature the immobilized enzyme. The clinical importance of this work is demonstrated.
Subject(s)
Full text: Available Index: IMSEAR (South-East Asia) Main subject: Oxidoreductases / Plants / Hordeum / Zirconium / Enzyme Stability / Glutaral / Enzymes, Immobilized / Amines / Hydrogen-Ion Concentration Language: English Journal: Indian J Biochem Biophys Year: 1993 Type: Article

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Full text: Available Index: IMSEAR (South-East Asia) Main subject: Oxidoreductases / Plants / Hordeum / Zirconium / Enzyme Stability / Glutaral / Enzymes, Immobilized / Amines / Hydrogen-Ion Concentration Language: English Journal: Indian J Biochem Biophys Year: 1993 Type: Article