Studies on horseradish peroxidase immobilized onto arylamine and alkylamine glass

Peroxidase from horseradish has been immobilized onto zirconia coated aryla mine and alkylamine glass through the process of diazotization and glutaral dehyde coupling, respectively. Arylamine glass bound enzyme retained 77% of the initial activity with a conjugation yield of 18 mg g(-1) support, whil e alkylamine glass bound enzyme retained 38% of the initial activity with a conjugation yield of 16 mg g(-1) support. The immobilized enzyme showed an increase in optimum pH, temperature for maximum activity, energy of activa tion (Ea), and thermal stability but decrease in time for linearity and Km for H2O2 Vmax value of arylamine conjugated enzyme decreased but Vmax of al kylamine conjugated enzyme was unaltered compared to free enzyme. Both aryl amine and alkylamine bound enzyme showed higher stability in cold compared to that of free enzyme. The application of glass bound peroxidase in discre te analysis of serum urate is demonstrated.