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http://hdl.handle.net/10773/6948
Title: | Influence of pH on the Thermal Inactivation Kinetics of Horseradish Peroxidase in Aqueous Solution |
Author: | Lemos, Maria Adı́lia Oliveira, Jorge C. Saraiva, Jorge A. |
Keywords: | enzyme inactivation kinetic modelling protein thermal denaturation |
Issue Date: | 2000 |
Publisher: | Elsevier |
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. |
Peer review: | yes |
URI: | http://hdl.handle.net/10773/6948 |
DOI: | 10.1006/fstl.2000.0694 |
ISSN: | 0023-6438 |
Appears in Collections: | QOPNA - Artigos |
Files in This Item:
File | Description | Size | Format | |
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P6_LWT_peroxidase pH.pdf | 203.99 kB | Adobe PDF |
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