Food and Bioprocess Technology

, Volume 1, Issue 2, pp 187–195 | Cite as

Thermal Inactivation Kinetics of Peroxidase in Coriander Leaves

  • S. G. Rudra
  • U. S. ShivhareEmail author
  • S. Basu
  • B. C. Sarkar


Design of efficient blanching treatments requires knowledge of critical factors such as enzyme inactivation kinetic parameters and relative proportions of heat-labile and heat-resistant fractions, which is unique in each vegetable. Thermal inactivation curves for peroxidase in coriander leaves were determined in the temperature range of 70 to 100 °C and in steam. The isothermal data were statistically treated using both linear and nonlinear regression. Applicability of various enzyme inactivation models available in the literature was critically evaluated. The two-fraction first-order model was found to be the best model to describe the peroxidase inactivation kinetics in coriander leaves (R 2 > 0.97). Kinetic parameters were determined for heat-labile and heat-resistant isoenzyme fractions. The temperature dependence of the rate parameters in the present study did not follow the Arrhenius relationship.


Coriander Peroxidase Heat treatment Blanching Modeling 


α1, α2

ratio of specific activities E 1/E and E 2/E


activity fraction of the thermal labile isozyme group


specific activity of each component


enzyme activity at time t


enzyme activity for heat labile and resistant fraction


initial enzyme activity at t = 0


activity of the resistant enzyme fraction


concentration of heat labile isozyme


enzyme activity per unit volume of the ith component at time 0


concentration of heat resistant isozyme

E, E1 and E2

specific activities of enzymes and isoenzymes


homogenous native enzyme population


activation energy (kJ/mol)


reaction rate constant (min−1)

k1, k2

first-order inactivation rate coefficients (min−1)

kL, kR

rate constants for thermal inactivation of heat-labile and heat-resistant isozymes (min−1)


reaction rate constant for the heat-labile and heat-resistant isozymes with the substrate (min−1)


pre-exponential factor


number of components


ratio of C o2 to C o1


universal gas constant (8.314 J mol−1 K−1)


coefficient of correlation


standard error


absolute temperature (K)


ΔAbsorbace per minute of native enzyme


ΔAbsorbace per minute after heat treatment for time ‘t


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Copyright information

© Springer Science + Business Media, LLC 2007

Authors and Affiliations

  • S. G. Rudra
    • 1
  • U. S. Shivhare
    • 2
    Email author
  • S. Basu
    • 2
  • B. C. Sarkar
    • 3
  1. 1.Department of Food and Nutrition, Institute of Home EconomicsDelhi UniversityNew DelhiIndia
  2. 2.Department of Chemical Engineering & TechnologyPanjab UniversityChandigarhIndia
  3. 3.Department of Food TechnologySant Longowal Institute of Engineering & TechnologyLongowalIndia

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