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 Ea = 13.62 kcal/mol and k100°C = 2.07 min−1.

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The effect of heating on ascorbic acid in green asparagus during a simulated retort operation was investigated. The asparagus was heated in trays of ethylene-vinyl alcohol copolymer for selected time intervals at four temperatures ranging from 110 to 125 degrees C. It was found that the rate of degradation followed first-order kinetics. Kinetic parameters were obtained by using two least squares methods. The activation energy and z value were 35 kcal/mol and 20 degrees C, respectively.

An unsteady-state method was developed for estimating texture degradation during heating-cooling of green asparagus spears. The method used a mathematical model of heat transmission for time-temperature history estimation, and a nonlinear regression of texture measurements of asparagus spears to estimate kinetic parameters. The specific heat, conductivity and convective coefficient of green asparagus were determined experimentally and used in the mathematical model for temperature estimation. Values obtained were Ea = 76.19Ϯ0.13 kJ/mol and k 1158°C = 0.00528Ϯ0.00005 s -1 . Good agreement was found between predicted and observed texture values. The method was compared with the classical steadystate method. The mathematical model and kinetic parameters estimated could be used to design and evaluate thermal processes for green asparagus.

The inactivation kinetics of horseradish peroxidase (HRP) heated in capillary tubes in the range 110 to 135°C was studied. Its regeneration kinetics when stored at 4 and 25°C was also considered. As the severity of the treatment increased, the absolute value of the regeneration decreased. The storage temperature of the enzyme did not affect the percentage of maximum activity regenerable, although when this temperature was raised from 4 to 25°C the speed of regeneration increased. Kinetics of HRP inactivation determined after heating and after regeneration were compared. Both forms of the enzyme showed similar behavior with first-order inactivation kinetics, with Ea = 19.5 ± 1.0 kcal/mol and k120°C = 3.7 ± 0.2 min−1, and Ea = 18.8 ± 1.2 kcal/mol and k120°C = 3.7 ± 0.2 min−1, respectively.