The thermal inactivation of horseradish peroxidase was studied in sodium phosphate buffer solutions and in pure water at pH 7 in the temperature range of 70–95°C. The sodium phosphate ions concentration affected both the thermostability and the kinetic patterns and had a stabilizing effect. The gradual change observed at low concentrations made a series-type mechanism theoretically more coherent with the experimental observations than the conventionally applied two-fraction model. In water the kinetics is apparently First order at high temperatures, while the results obtained at 25°C support the occurrence of a series-type inactivation mechanism. The pH and enzyme concentration also affect the inactivation proFile, supporting the conclusion that the thermal inactivation is not a monomolecular process with respect to protein concentration.
|Number of pages||9|
|Journal||International Journal of Food Science and Technology|
|Publication status||Published - May 1996|
Saraiva, J. A., Oliveira, J. C., Lemos, M. A., & Hendrickx, M. E. (1996). Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength. International Journal of Food Science and Technology, 31(3), 223–231. https://doi.org/10.1046/j.1365-2621.1996.00342.x