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The influence of water activity on thermal stability of horseradish peroxidase

dc.contributor.authorHendrickx, M.
dc.contributor.authorSaraiva, J.
dc.contributor.authorLyssens, J.
dc.contributor.authorOliveira, J.
dc.contributor.authorTobback, P.
dc.date.accessioned2011-10-21T11:43:48Z
dc.date.available2011-10-21T11:43:48Z
dc.date.issued1992
dc.description.abstractThe thermal stability of horseradish peroxidase in the solid state was studied as a function of water activity, from 0.11 to 0.88. At all activities the enzyme was found to be much more stable in the solid state than in solution. Inactivation temperatures were in the range of 140–160°C. Inactivation curves show a biphasic behaviour which can be described by a model assuming two fractions (heat labile and heat stable) with independent first order inactivation kinetics. The labile fraction represents approximately 30% of the total activity. The z-value for both stable and labile fractions depends on water activity (moisture content) and has a maximum at aw= 0.76 (44.4°C and 43.8°C, respectively).por
dc.identifier.citationHENDRICKX, M. - The influence of water activity on thermal stability of horseradish peroxidase. International Journal of Food Science & Technology. ISSN 1365-2621. Vol. 27 n.º 1 (1992), p. 33-40por
dc.identifier.doi10.1111/j.1365-2621.1992.tb01175.x
dc.identifier.eid84988121020
dc.identifier.urihttp://hdl.handle.net/10400.14/6648
dc.identifier.wosA1992HL32900004
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherWileypor
dc.subjectDecimal reduction timepor
dc.subjectZ-valuepor
dc.subjectEnzyme thermal inactivationpor
dc.subjectLow moisture stabilitypor
dc.titleThe influence of water activity on thermal stability of horseradish peroxidasepor
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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