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.
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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