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 Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength
Please use this identifier to cite or link to this item http://hdl.handle.net/10773/7732

title: Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength
authors: Saraiva, Jorge
Oliveira, Jorge C.
Lemos, Adília
Hendrickx, Marc
keywords: Enzyme inactivation
Kinetic models
issue date: 1996
publisher: Wiley-Blackwell
abstract: 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.
URI: http://hdl.handle.net/10773/7732
ISSN: 1365-2621
publisher version/DOI: http://dx.doi.org/10.1046/j.1365-2621.1996.00342.x
source: International Journal of Food Science and Technology
appears in collectionsQOPNA - Artigos

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