File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Study of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry

TitleStudy of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometry
Authors
Issue Date1988
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 1988, v. 36 n. 1, p. 155-160 How to Cite?
AbstractThermal denaturation of dilute (<0.05%) oat globulin solutions at high ionic strength was studied by ultraviolet (UV) and fluorescence spectrophotometry. Ultraviolet spectra show a significant red shift of absorption maximum when the protein was heated at 110°C. Second-derivative and difference-derivative spectra suggest exposure of tryptophan and tyrosine residues in the heated samples. Fluorescence emission spectra show a significant blue shift, indicating protein unfolding. When 1% oat globulin was heat aggregated and fractionated into soluble and insoluble fractions, UV and fluorescence spectra indicate no marked protein unfolding in the soluble fraction but extensive denaturation in the insoluble aggregates. The soluble fraction had significantly higher surface hydrophobicity than the soluble fraction and the unheated protein.
Persistent Identifierhttp://hdl.handle.net/10722/178361
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorHarwalkar, VRen_US
dc.date.accessioned2012-12-19T09:47:16Z-
dc.date.available2012-12-19T09:47:16Z-
dc.date.issued1988en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 1988, v. 36 n. 1, p. 155-160en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178361-
dc.description.abstractThermal denaturation of dilute (<0.05%) oat globulin solutions at high ionic strength was studied by ultraviolet (UV) and fluorescence spectrophotometry. Ultraviolet spectra show a significant red shift of absorption maximum when the protein was heated at 110°C. Second-derivative and difference-derivative spectra suggest exposure of tryptophan and tyrosine residues in the heated samples. Fluorescence emission spectra show a significant blue shift, indicating protein unfolding. When 1% oat globulin was heat aggregated and fractionated into soluble and insoluble fractions, UV and fluorescence spectra indicate no marked protein unfolding in the soluble fraction but extensive denaturation in the insoluble aggregates. The soluble fraction had significantly higher surface hydrophobicity than the soluble fraction and the unheated protein.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_US
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_US
dc.titleStudy of thermal denaturation of oat globulin by ultraviolet and fluorescence spectrophotometryen_US
dc.typeArticleen_US
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_US
dc.identifier.authorityMa, CY=rp00759en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0000079360en_US
dc.identifier.volume36en_US
dc.identifier.issue1en_US
dc.identifier.spage155en_US
dc.identifier.epage160en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats