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Article: Characterization of globulin from Phaseolus angularis (red bean)

TitleCharacterization of globulin from Phaseolus angularis (red bean)
Authors
KeywordsFunctional Property
Globulin
Phaseolus Angularis
Protein
Red Bean
Issue Date2002
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/IFS
Citation
International Journal Of Food Science And Technology, 2002, v. 37 n. 6, p. 687-695 How to Cite?
AbstractPhaseolus angularis (red bean) seeds contain about 25% protein (dry basis), almost half of which is globulin. Similar to globulins from other Phaseolus species, 7S vicilin is the major fraction of red bean globulin (RBG), with 11S legumin as a minor component. The amino acid profile of RBG met or exceeded the FAO/WHO standard. Circular dichroism measurements indicate that RBG is a protein rich in α-helical and β-turn structures. RBG exhibited higher protein solubility than Supro 610, a commercial soy protein isolate, especially at acidic pHs, with minimal solubility at around pH 5.0. Compared to Supro 610, RBG had lower water hydration capacity and comparable fat binding capacity, which might be because of its lower surface hydrophobicity. RBG had higher emulsifying activity index and emulsion stability than Supro 610, but with poorer foaming properties.
Persistent Identifierhttp://hdl.handle.net/10722/178767
ISSN
2015 Impact Factor: 1.504
2015 SCImago Journal Rankings: 0.720
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMeng, Gen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:49:37Z-
dc.date.available2012-12-19T09:49:37Z-
dc.date.issued2002en_US
dc.identifier.citationInternational Journal Of Food Science And Technology, 2002, v. 37 n. 6, p. 687-695en_US
dc.identifier.issn0950-5423en_US
dc.identifier.urihttp://hdl.handle.net/10722/178767-
dc.description.abstractPhaseolus angularis (red bean) seeds contain about 25% protein (dry basis), almost half of which is globulin. Similar to globulins from other Phaseolus species, 7S vicilin is the major fraction of red bean globulin (RBG), with 11S legumin as a minor component. The amino acid profile of RBG met or exceeded the FAO/WHO standard. Circular dichroism measurements indicate that RBG is a protein rich in α-helical and β-turn structures. RBG exhibited higher protein solubility than Supro 610, a commercial soy protein isolate, especially at acidic pHs, with minimal solubility at around pH 5.0. Compared to Supro 610, RBG had lower water hydration capacity and comparable fat binding capacity, which might be because of its lower surface hydrophobicity. RBG had higher emulsifying activity index and emulsion stability than Supro 610, but with poorer foaming properties.en_US
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/IFSen_US
dc.relation.ispartofInternational Journal of Food Science and Technologyen_US
dc.subjectFunctional Propertyen_US
dc.subjectGlobulinen_US
dc.subjectPhaseolus Angularisen_US
dc.subjectProteinen_US
dc.subjectRed Beanen_US
dc.titleCharacterization of globulin from Phaseolus angularis (red bean)en_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.doi10.1046/j.1365-2621.2002.00601.xen_US
dc.identifier.scopuseid_2-s2.0-0036335312en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036335312&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume37en_US
dc.identifier.issue6en_US
dc.identifier.spage687en_US
dc.identifier.epage695en_US
dc.identifier.isiWOS:000177085800011-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridMeng, G=13405928600en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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