Thermal stability of horseradish peroxidase enzymatic papers

摘要

The thermal stability, functionality and selectivity of bioactive enzyme papers was investigated. Horseradish peroxidase enzyme (HRP) was adsorbed from solution onto paper and dried. The HRP enzyme paper was aged at 23℃ and 90℃ for various period and exposed to DAB, the enzyme substrate. The reactivity of the HRP enzymatic paper was followed by measuring the intensity of the colorimetric sample. HRP enzymatic paper retains its functionality and selectivity. Immobilization on paper was found to increase the thermal stability of HRP compared to the enzyme in solution. Thermal degradation of HRP enzymatic paper was found not to follow the expected first order reaction with respect to enzyme concentration, but rather to form a two-step process.