Abertay Research Collections >
School of Science, Engineering & Technology >
Science Engineering & Technology Collection >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10373/1105

View Statistics
Title: Influence of pH and high pressure on the thermal inactivation kinetics of horseradish peroxidase
Authors: Lemos, Adília
Oliveira, Jorge C.
Hendrickx, Marc E.
Affiliation: University of Abertay Dundee. School of Contemporary Sciences
Keywords: Enzyme barostability
Enzyme inactivation
Kinetic modeling
Protein denaturation
Issue Date: 1999
Publisher: Taylor & Francis
Type: Journal Article
Refereed: peer-reviewed
Rights: Published version © Taylor & Francis, available from www.tandfonline.com
Citation: Lemos, M.A., Oliveira, J.C. and Hendrickx, M.E. 1999. Influence of pH and high pressure on the thermal inactivation kinetics of horseradish peroxidase. Food Biotechnology. 13(1): pp.13-32. Available from DOI: http://dx.doi.org/10.1080/08905439609549959
Abstract: The inactivation kinetics of horseradish peroxidase were determined at several values of pH (3, 4, 7, 9 and 10), temperature (40 to 70 °C) and pressure (7, 8 and 9 kbar). The data were obtained by taking samples from the moment that pressure inside the hydrostatic high pressure vessels reached the value specified, and therefore relate to isothermal and isobaric conditions. The inactivation kinetics were non‐log linear and could be individually well described by the conventional two‐fraction model, but the overall consistency of the kinetic parameters of this model was poor and the model was clearly not robust. Inversely, the kinetic model based on the Weibull probability distribution function yielded good individual fits and also a good overall consistency of the kinetic parameters. The whole set of 327 data points could be well described by an overall model considering that the shape parameter (ß) varied with pressure but not with temperature and that the rate parameter (1/α) varied with temperature according to an Arrhenius law, with a pressure‐independent activation energy, and varied exponentially with pressure. The activation energy and the pressure‐sensitivity parameter did not vary with pH up to pH 9. The results suggested a discontinuity of the kinetic behaviour at pH 10, with a different inactivation mechanism prevailing.
URI: http://hdl.handle.net/10373/1105
ISSN: 0890-5436
Appears in Collections:Science Engineering & Technology Collection

Files in This Item:

There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.


Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback