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Infuence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution

2000Journal article Restricted access
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dc.contributor.authorLemos, Maria Adília
dc.contributor.authorOliveira, Jorge C.
dc.contributor.authorSaraiva, Jorge A.
dc.date.accessioned2011-10-20T16:47:55Z
dc.date.available2011-10-20T16:47:55Z
dc.date.issued2000
dc.description.abstractThe 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 3C to 95 3C. The data were well xtted 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 3C) and of the more labile fraction at pH 3}4 (temperatures from 65 to 85 3C) were close to 10 3C, 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 awecting their low z-value.por
dc.identifier.citationLEMOS, Maria Adília; OLIVEIRA, Jorge C.; SARAIVA Jorge A. - Infuence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solution. ISSN 0023-6438. Vol. 33 (2000), p. 362-368por
dc.identifier.urihttp://hdl.handle.net/10400.14/6540
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversiondoi:10.1006/fstl.2000.0694por
dc.subjectEnzyme inactivationpor
dc.subjectkinetic modellingpor
dc.subjectProtein thermal denaturationpor
dc.titleInfuence of pH on the thermal inactivation kinetics of horseradish peroxidase in aqueous solutionpor
dc.typejournal article
dspace.entity.typePublication
person.familyNameOliveira
person.givenNameJorge
person.identifier.orcid0000-0002-0680-6174
person.identifier.ridC-2642-2008
person.identifier.scopus-author-id7202452289
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublication5227bcfa-cb99-407e-a2ef-3f4eb86d4243
relation.isAuthorOfPublication.latestForDiscovery5227bcfa-cb99-407e-a2ef-3f4eb86d4243

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