Immobilization of Amaranthus leaf oxalate oxidase on arylamine glass

A membrane bound oxalate oxidase (OXO) partially purified from leaves of Am aranthus spinosus has been immobilized on arylamine glass beads through dia zotization with a conjugation yield of 5.0 mg protein/g support and 53.5% r etention of initial activity. There was no change in the optimum pH (3.5), the temperature for maximum activity (40 degrees C) and time for linearity (4 min), but the energy of activation and Km for oxalate were increased, wh ile Vmax and thermal stability of the enzyme were decreased after immobiliz ation. The immobilized enzyme lost only 10% of its initial activity after i ts regular use for a period of three months, when stored in distilled water at 4 degrees C. Cl- had no effect on immobilized enzyme.