Barley oxalate oxidase immobilized on zirconia-coated alkylamine glass using glutaraldehyde.
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.
Department of Bio-Sciences, Maharshi Dayanand University, Rohtak, India.
C S
CS
Pundir
N K
NK
Kuchhal
Satyapal
D000588:Amines; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000302:isolation & purification; D005976:Glutaral; D001467:Hordeum / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D010088:Oxidoreductases / Q000302:isolation & purification*; D010944:Plants / Q000201:enzymology*; D015040:Zirconium
D000588:Amines; D004800:Enzymes, Immobilized; D015040:Zirconium; D010088:Oxidoreductases; C020598:oxalate oxidase; C028541:zirconium oxide; D005976:Glutaral