Immobilization of Amaranthus leaf oxalate oxidase on alkylamine glass

A membrane bound oxalate oxidase from leaves of Amaranthus spionsus has bee n partially purified and immobilized on alkylamine glass with a yield of 9. 2 mg protein/g support. The enzyme retained 99.4% of initial activity of fr ee enzyme after immobilization. There was no change in the optimum pH (3.5) and V-max but the temperature for maximum activity was slightly decreased (35 degrees C) and energy of activation (E-a) and K-m for oxalate were incr eased after immobilization. The immobilized enzyme preparation was stable f or 6 months, when stored in distilled water at 4 degrees C. Presence of Cl- did not affect the activity of immobilized enzyme.