Thermal inactivation at high temperatures and regeneration of green asparagus peroxidase

Abstract

A spectrophotometric method was developed for determining the peroxidase activity of green asparagus in small samples. The optimum conditions for the analysis in the cuvette were 45 mM of H2O2, 36 mM of guaiacol, and pH 7. The method can be used to determine enzyme activity at up to two decimal reductions. A study was performed of the regeneration and inactivation kinetics of the enzyme when heated between 90 and 125°C. Regenerated asparagus peroxidase reached its maximum activity after being stored 6 days at 25°C. The regenerated enzyme followed first-order inactivation kinetics, showing an E(a) = 13.62 kcal/mol and k(100°C) = 2.07 min-1.