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|Title: ||Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution|
|Authors: ||Lemos, Adília|
Oliveira, Jorge C.
Saraiva, Jorge A.
|Affiliation: ||University of Abertay Dundee. School of Contemporary Sciences|
|Keywords: ||Enzyme inactivation|
Protein thermal denaturation
|Issue Date: ||2000|
|Publisher: ||Academic Press|
|Type: ||Journal Article|
|Rights: ||Published version © Academic Press, available from doi:10.1006/fstl.2000.0694|
|Citation: ||Lemos, M. A., Oliveira, J. C. and Saraiva, J. A. 2000. Influence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution. Lebensmittel-Wissenschaft und-Technologie. 33(5): pp.362-368. Available from DOI: http://dx.doi.org/doi:10.1006/fstl.2000.0694|
|Abstract: ||The thermal inactivation of horseradish peroxidase in aqueous solution was studied in the pH range of 3.0 to 12.5, at temperatures ranging from 40 °C to 95 °C. The data were well fitted by a double exponential model. The enzyme showed highest stability around neutral pH and the stability was particularly decreased above pH 11. The z value of the less labile fraction at pH 11.5 to 12.5 (temperatures from 40 to 65 °C) and of the more labile fraction at pH 3–4 (temperatures from 65 to 85 °C) were close to 10 °C, making these systems suitable as time-temperature integrators for assessing microbial lethality in thermal processing of low-acid foods, particularly if they can be stabilized further without affecting their low z-value.|
|Appears in Collections:||Science Engineering & Technology Collection|
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