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Article: Heat-induced modifications in the functional and structural properties of vicilin-rich protein isolate from kidney (Phaseolus vulgaris L.) bean

TitleHeat-induced modifications in the functional and structural properties of vicilin-rich protein isolate from kidney (Phaseolus vulgaris L.) bean
Authors
KeywordsFunctional Property
Heat Treatment
Kidney Protein Isolate
Modification
Phaseolus Vulgaris L.
Structural Conformation
Issue Date2009
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2009, v. 115 n. 3, p. 859-866 How to Cite?
AbstractHeat-induced changes in the physico-chemical (and/or functional) and structural properties of protein isolate from kidney beans (KPI) were characterised. The extent of protein denaturation, free sulphydryl contents, surface hydrophobicity, as well as structural characteristics of the proteins were evaluated. Analyses of size-exclusion chromatography combined with laser scattering showed that the heating at 95 °C led to transformation of 7S-form vicilin to its 11S-form, and even higher molar mass (MW) oligomers or polymers. Moderate heating (for 15-30 min) significantly improved protein solubility, emulsifying and foaming activities (at neutral pH), whilst extensive heating (for 60-120 min) on the contrary decreased these properties. Spectral analyses of fluorescence and/or Raman spectroscopy showed that tertiary and secondary conformations of protein in KPI were remarkably affected to a varying extent by the heating. The results suggested a close relationship between functional properties of the vicilin from kidney bean and its conformational characteristics. © 2009 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/179120
ISSN
2015 Impact Factor: 4.052
2015 SCImago Journal Rankings: 1.620
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTang, CHen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:52:07Z-
dc.date.available2012-12-19T09:52:07Z-
dc.date.issued2009en_US
dc.identifier.citationFood Chemistry, 2009, v. 115 n. 3, p. 859-866en_US
dc.identifier.issn0308-8146en_US
dc.identifier.urihttp://hdl.handle.net/10722/179120-
dc.description.abstractHeat-induced changes in the physico-chemical (and/or functional) and structural properties of protein isolate from kidney beans (KPI) were characterised. The extent of protein denaturation, free sulphydryl contents, surface hydrophobicity, as well as structural characteristics of the proteins were evaluated. Analyses of size-exclusion chromatography combined with laser scattering showed that the heating at 95 °C led to transformation of 7S-form vicilin to its 11S-form, and even higher molar mass (MW) oligomers or polymers. Moderate heating (for 15-30 min) significantly improved protein solubility, emulsifying and foaming activities (at neutral pH), whilst extensive heating (for 60-120 min) on the contrary decreased these properties. Spectral analyses of fluorescence and/or Raman spectroscopy showed that tertiary and secondary conformations of protein in KPI were remarkably affected to a varying extent by the heating. The results suggested a close relationship between functional properties of the vicilin from kidney bean and its conformational characteristics. © 2009 Elsevier Ltd. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchemen_US
dc.relation.ispartofFood Chemistryen_US
dc.subjectFunctional Propertyen_US
dc.subjectHeat Treatmenten_US
dc.subjectKidney Protein Isolateen_US
dc.subjectModificationen_US
dc.subjectPhaseolus Vulgaris L.en_US
dc.subjectStructural Conformationen_US
dc.titleHeat-induced modifications in the functional and structural properties of vicilin-rich protein isolate from kidney (Phaseolus vulgaris L.) beanen_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.doi10.1016/j.foodchem.2008.12.104en_US
dc.identifier.scopuseid_2-s2.0-62249111360en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-62249111360&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume115en_US
dc.identifier.issue3en_US
dc.identifier.spage859en_US
dc.identifier.epage866en_US
dc.identifier.isiWOS:000265348100013-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridTang, CH=35197262700en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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