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Please use this identifier to cite or link to this item: http://hdl.handle.net/10373/1106

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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
Affiliation: University of Abertay Dundee. School of Contemporary Sciences
Keywords: Enzyme inactivation
Kinetic models
Issue Date: May-1996
Publisher: Wiley-Blackwell
Type: Journal Article
Refereed: peer-reviewed
Rights: Published version (c)Wiley-Blackwell, available from http://dx.doi.org/10.1046/j.1365-2621.1996.00342.x. The definitive version is available at www3.interscience.wiley.com
Citation: Saraiva, J., et al. 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): pp.223-231. Available from http://dx.doi.org/10.1046/j.1365-2621.1996.00342.x
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/10373/1106
ISSN: 0950-5423
Appears in Collections:Science Engineering & Technology Collection

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