File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Raman spectroscopic study of globulin from Phaseolus angularis (red bean)

TitleRaman spectroscopic study of globulin from Phaseolus angularis (red bean)
Authors
KeywordsProtein conformation
Raman spectroscopy
Red bean globulin
Issue Date2003
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchem
Citation
Food Chemistry, 2003, v. 81 n. 3, p. 411-420 How to Cite?
AbstractFourier-transform Raman spectroscopy was used to study the conformation of red bean globulin (RBG) in various buffered environments and on heat treatment. The Raman spectrum of 20% (w/v) freeze-dried RBG in 0.01 M phosphate buffer at pH 7.4 suggests that its secondary structure composition is dominated by β-sheets and random coils. Extreme pH values caused the amide I and amide III bands to shift, suggesting a transition from an ordered structure (α-helix or β-sheet) to a random coil conformation. The decreases of the intensity of the band near 760 cm-1, at acidic and basic pHs, indicate an unfolding of the protein, leading to exposure of hydrophobic residues. Increasing concentrations of added NaCl led to progressive increases of the band intensity near 760 cm-1, suggesting an increased "buriedness" of tryptophan residues. Protein structure perturbants, including sodium dodecyl sulfate (SDS), β-mercaptoethanol (β-ME), dithiothreitol (DTT), N-ethylmaleimide (NEM) and ethylene glycol (EG) were also found to have a marked influence on the conformation of RBG. The Raman data indicate progressive denaturation of RBG during heat treatment at 90C. Heat-induced aggregation caused changes in the protein backbone vibrations, and increases in the tryptophan band intensity, suggesting that hydrophobic interactions may play an important role in RBG aggregation. The shifts in amide III bands indicate that β-sheet is the major secondary structure in the heat-induced aggregates. © 2002 Elsevier Science Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68390
ISSN
2015 Impact Factor: 4.052
2015 SCImago Journal Rankings: 1.620
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMeng, Gen_HK
dc.contributor.authorMa, CYen_HK
dc.contributor.authorPhillips, DLen_HK
dc.date.accessioned2010-09-06T06:04:11Z-
dc.date.available2010-09-06T06:04:11Z-
dc.date.issued2003en_HK
dc.identifier.citationFood Chemistry, 2003, v. 81 n. 3, p. 411-420en_HK
dc.identifier.issn0308-8146en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68390-
dc.description.abstractFourier-transform Raman spectroscopy was used to study the conformation of red bean globulin (RBG) in various buffered environments and on heat treatment. The Raman spectrum of 20% (w/v) freeze-dried RBG in 0.01 M phosphate buffer at pH 7.4 suggests that its secondary structure composition is dominated by β-sheets and random coils. Extreme pH values caused the amide I and amide III bands to shift, suggesting a transition from an ordered structure (α-helix or β-sheet) to a random coil conformation. The decreases of the intensity of the band near 760 cm-1, at acidic and basic pHs, indicate an unfolding of the protein, leading to exposure of hydrophobic residues. Increasing concentrations of added NaCl led to progressive increases of the band intensity near 760 cm-1, suggesting an increased "buriedness" of tryptophan residues. Protein structure perturbants, including sodium dodecyl sulfate (SDS), β-mercaptoethanol (β-ME), dithiothreitol (DTT), N-ethylmaleimide (NEM) and ethylene glycol (EG) were also found to have a marked influence on the conformation of RBG. The Raman data indicate progressive denaturation of RBG during heat treatment at 90C. Heat-induced aggregation caused changes in the protein backbone vibrations, and increases in the tryptophan band intensity, suggesting that hydrophobic interactions may play an important role in RBG aggregation. The shifts in amide III bands indicate that β-sheet is the major secondary structure in the heat-induced aggregates. © 2002 Elsevier Science Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/foodchemen_HK
dc.relation.ispartofFood Chemistryen_HK
dc.rightsFood Chemistry. Copyright © Elsevier BV.en_HK
dc.subjectProtein conformationen_HK
dc.subjectRaman spectroscopyen_HK
dc.subjectRed bean globulinen_HK
dc.titleRaman spectroscopic study of globulin from Phaseolus angularis (red bean)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0308-8146&volume=81&issue=3&spage=411&epage=420&date=2003&atitle=Raman+spectroscopic+study+of+globulin+from+phaseolus+angularis+(red+bean)en_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.emailPhillips, DL: phillips@hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.identifier.authorityPhillips, DL=rp00770en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0308-8146(02)00471-5en_HK
dc.identifier.scopuseid_2-s2.0-0037409125en_HK
dc.identifier.hkuros81027en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037409125&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume81en_HK
dc.identifier.issue3en_HK
dc.identifier.spage411en_HK
dc.identifier.epage420en_HK
dc.identifier.isiWOS:000182288300014-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridMeng, G=13405928600en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.scopusauthoridPhillips, DL=7404519365en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats