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http://hdl.handle.net/10773/6948
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lemos, Maria Adı́lia | pt |
dc.contributor.author | Oliveira, Jorge C. | pt |
dc.contributor.author | Saraiva, Jorge A. | pt |
dc.date.accessioned | 2012-02-27T18:57:40Z | - |
dc.date.issued | 2000 | - |
dc.identifier.issn | 0023-6438 | pt |
dc.identifier.uri | http://hdl.handle.net/10773/6948 | - |
dc.description.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. | pt |
dc.language.iso | eng | pt |
dc.publisher | Elsevier | pt |
dc.relation | programme AAIR, project AIR1-CT92-0746 | pt |
dc.rights | restrictedAccess | por |
dc.subject | enzyme inactivation | pt |
dc.subject | kinetic modelling | pt |
dc.subject | protein thermal denaturation | pt |
dc.title | Influence of pH on the Thermal Inactivation Kinetics of Horseradish Peroxidase in Aqueous Solution | pt |
dc.type | article | pt |
dc.peerreviewed | yes | pt |
ua.distribution | international | pt |
degois.publication.firstPage | 362 | pt |
degois.publication.issue | 5 | pt |
degois.publication.issue | 5 | |
degois.publication.lastPage | 368 | pt |
degois.publication.title | Food Science and Technology | pt |
degois.publication.volume | 33 | pt |
dc.date.embargo | 10000-01-01 | - |
dc.identifier.doi | 10.1006/fstl.2000.0694 | * |
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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