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Please use this identifier to cite or link to this item: http://hdl.handle.net/10773/7765
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dc.contributor.authorSaraiva, J.pt
dc.contributor.authorDe Cordt, S.pt
dc.contributor.authorHendrickx, M.pt
dc.contributor.authorOliveira, J.pt
dc.contributor.authorTobback, P.pt
dc.date.accessioned2012-04-04T15:52:40Z-
dc.date.available2012-04-04T15:52:40Z-
dc.date.issued1993-
dc.identifier.isbn978-0444893727-
dc.identifier.urihttp://hdl.handle.net/10773/7765-
dc.description.abstractThe thermal inactivation characteristics of dehydrated a-amylase in solid state at various moisture contents was studied at temperatures between 135 and 150°C. The inactivation kinetics show a first order decay. The enzyme was found to be more thermostable than in aqueous solution. The z-value dependency with moisture content has shown some fluctuactions, having an absolut minimum of 19°C at 23.9% moisture.pt
dc.language.isoengpt
dc.publisherElsevier Science Publisherspt
dc.relationJNICTpt
dc.rightsopenAccesspor
dc.subjectInactivationpt
dc.subjecta-amylasept
dc.subjectBacillus amyloliquefacienspt
dc.subjectmoisture contentspt
dc.titleInactivation of alpha-amylase from Bacillus amyloliquefaciens at low moisture contentspt
dc.typeconferenceObjectpt
dc.peerreviewedyespt
ua.publicationstatuspublishedpt
ua.event.date22-25 Novembro, 1992pt
ua.event.typeconferencept
degois.publication.firstPage459pt
degois.publication.lastPage466pt
degois.publication.locationMaastricht, The Netherlandspt
degois.publication.titleStability and stabilization of enzymes: proceedings of an international symposium held in Maastricht-
degois.publication.titleStability and Stabilization of Enzymes-
Appears in Collections:QOPNA - Comunicações

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