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Article: Raman spectroscopic study of rice globulin

TitleRaman spectroscopic study of rice globulin
Authors
KeywordsProtein conformation
Raman spectroscopy
Rice globulin
Issue Date2006
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jcs
Citation
Journal Of Cereal Science, 2006, v. 43 n. 1, p. 85-93 How to Cite?
AbstractThe conformation of rice globulin was studied by Fourier-transform Raman spectroscopy as influenced by different buffer environments and heat treatments. The Raman spectrum of the native protein showed a predominance of α-helical structures as indicated by major amide I and III bands at 1657 and 1270 cm-1, respectively. Highly acidic and alkaline pH conditions induced band shifts and intensity changes in amide I, amide III, and C-H (bending and stretching) vibrations, indicating protein denaturation. Addition of dithiothreitol and β-mercaptoethanol led to changes in S-S stretching vibration, whereas ethylene glycol and urea caused marked changes in tryptophan, tyrosine Fermi doublet and C-H band intensities. Heating at 100°C resulted in progressive denaturation as indicated by band shifts and intensity changes of major spectral regions. Our results revealed that hydrophobic interactions and disulfide bonds play a major role in stabilizing the conformation and in thermal aggregation of rice globulin. © 2005 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68382
ISSN
2015 Impact Factor: 2.402
2015 SCImago Journal Rankings: 1.265
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorEllepola, SWen_HK
dc.contributor.authorChoi, SMen_HK
dc.contributor.authorPhillips, DLen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:04:07Z-
dc.date.available2010-09-06T06:04:07Z-
dc.date.issued2006en_HK
dc.identifier.citationJournal Of Cereal Science, 2006, v. 43 n. 1, p. 85-93en_HK
dc.identifier.issn0733-5210en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68382-
dc.description.abstractThe conformation of rice globulin was studied by Fourier-transform Raman spectroscopy as influenced by different buffer environments and heat treatments. The Raman spectrum of the native protein showed a predominance of α-helical structures as indicated by major amide I and III bands at 1657 and 1270 cm-1, respectively. Highly acidic and alkaline pH conditions induced band shifts and intensity changes in amide I, amide III, and C-H (bending and stretching) vibrations, indicating protein denaturation. Addition of dithiothreitol and β-mercaptoethanol led to changes in S-S stretching vibration, whereas ethylene glycol and urea caused marked changes in tryptophan, tyrosine Fermi doublet and C-H band intensities. Heating at 100°C resulted in progressive denaturation as indicated by band shifts and intensity changes of major spectral regions. Our results revealed that hydrophobic interactions and disulfide bonds play a major role in stabilizing the conformation and in thermal aggregation of rice globulin. © 2005 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/jcsen_HK
dc.relation.ispartofJournal of Cereal Scienceen_HK
dc.subjectProtein conformationen_HK
dc.subjectRaman spectroscopyen_HK
dc.subjectRice globulinen_HK
dc.titleRaman spectroscopic study of rice globulinen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0733-5210&volume=43&spage=85&epage=93&date=2006&atitle=Raman+spectroscopic+study+of+rice+globulinen_HK
dc.identifier.emailPhillips, DL: phillips@hku.hken_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityPhillips, DL=rp00770en_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jcs.2005.06.006en_HK
dc.identifier.scopuseid_2-s2.0-28444463272en_HK
dc.identifier.hkuros115292en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-28444463272&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume43en_HK
dc.identifier.issue1en_HK
dc.identifier.spage85en_HK
dc.identifier.epage93en_HK
dc.identifier.isiWOS:000234629900010-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridEllepola, SW=9843111000en_HK
dc.identifier.scopusauthoridChoi, SM=8873744400en_HK
dc.identifier.scopusauthoridPhillips, DL=7404519365en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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