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Article: Study of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetry

TitleStudy of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetry
Authors
Law, HYChoi, SMMa, CY
KeywordsDenaturation
Differential scanning calorimetry
Dolichos lablab
FTIR spectroscopy
Phaseolus calcaratus
Protein conformation
Thermal stability
Vicilin
Issue Date2008
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodres
Citation
Food Research International, 2008, v. 41 n. 7, p. 720-729 How to Cite?
DOI: http://dx.doi.org/10.1016/j.foodres.2008.05.004
AbstractFourier-transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC) were used to monitor changes in the secondary structure and thermal stability of vicilin from Dolichos lablab (DLV) and Phaseolus calcaratus (PCV) under different environmental conditions. The IR spectra of DLV and PCV in the amide I′ region (1700-1600 cm -1) showed that β-sheets and β-turns were the major secondary structures. Highly acidic and alkaline pH conditions induced changes in the secondary structure. DSC thermograms showed that raising pH from near neutrality decreased denaturation temperature (T d) and enthalpy of denaturation (ΔH). Chaotropic salts (1.0 M) caused a transition from β-sheet to random coil structures, and their effects on thermal stability followed the lyotropic series of anions. Addition of several protein structure perturbants caused changes in IR band intensities and DSC thermal characteristics, indicating protein denaturation. © 2008 Elsevier Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/149289
ISSN
0963-9969
2023 Impact Factor: 7.0
2023 SCImago Journal Rankings: 1.495
ISI Accession Number ID
WOS:000258736400006
References
References in Scopus

 

DC FieldValueLanguage
dc.contributor.authorLaw, HYen_HK
dc.contributor.authorChoi, SMen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2012-06-22T06:34:48Z-
dc.date.available2012-06-22T06:34:48Z-
dc.date.issued2008en_HK
dc.identifier.citationFood Research International, 2008, v. 41 n. 7, p. 720-729en_HK
dc.identifier.issn0963-9969en_HK
dc.identifier.urihttp://hdl.handle.net/10722/149289-
dc.description.abstractFourier-transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC) were used to monitor changes in the secondary structure and thermal stability of vicilin from Dolichos lablab (DLV) and Phaseolus calcaratus (PCV) under different environmental conditions. The IR spectra of DLV and PCV in the amide I′ region (1700-1600 cm -1) showed that β-sheets and β-turns were the major secondary structures. Highly acidic and alkaline pH conditions induced changes in the secondary structure. DSC thermograms showed that raising pH from near neutrality decreased denaturation temperature (T d) and enthalpy of denaturation (ΔH). Chaotropic salts (1.0 M) caused a transition from β-sheet to random coil structures, and their effects on thermal stability followed the lyotropic series of anions. Addition of several protein structure perturbants caused changes in IR band intensities and DSC thermal characteristics, indicating protein denaturation. © 2008 Elsevier Ltd. All rights reserved.en_HK
dc.languageengen_US
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/foodresen_HK
dc.relation.ispartofFood Research Internationalen_HK
dc.subjectDenaturationen_HK
dc.subjectDifferential scanning calorimetryen_HK
dc.subjectDolichos lablaben_HK
dc.subjectFTIR spectroscopyen_HK
dc.subjectPhaseolus calcaratusen_HK
dc.subjectProtein conformationen_HK
dc.subjectThermal stabilityen_HK
dc.subjectVicilinen_HK
dc.titleStudy of conformation of vicilin from Dolichos lablab and Phaseolus calcaratus by Fourier-transform infrared spectroscopy and differential scanning calorimetryen_HK
dc.typeArticleen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.foodres.2008.05.004en_HK
dc.identifier.scopuseid_2-s2.0-48149103212en_HK
dc.identifier.hkuros200333en_US
dc.identifier.hkuros147950-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-48149103212&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume41en_HK
dc.identifier.issue7en_HK
dc.identifier.spage720en_HK
dc.identifier.epage729en_HK
dc.identifier.isiWOS:000258736400006-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridLaw, HY=24399625800en_HK
dc.identifier.scopusauthoridChoi, SM=8873744400en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK
dc.identifier.issnl0963-9969-

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