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Article: Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry

TitleConformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetry
Authors
KeywordsAggregation
Buckwheat globulin
Denaturation
Differential scanning calorimetry
Fagopyrum esculentum Moench
FTIR spectroscopy
Protein conformation
Issue Date2005
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 2005, v. 53 n. 20, p. 8046-8053 How to Cite?
AbstractFourier transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC) were used to study changes in the conformation of globulin from common buckwheat (Fagopyrum esculentum Moench) (BWG) under various environmental conditions. The IR spectrum of the native BWG showed several major bands from 1691 to 1636 cm -1 in the amide I′ region, and the secondary structure composition was estimated as 34.5% β-sheets, 20.0% β-turns, 16.0% α-helices, and 14.4% random coils. Highly acidic and alkaline pH conditions induced decreases in β-sheet and α-helical contents, as well as in denaturation temperature (T d) and enthalpy of denaturation (ΔH), as shown in the DSC thermograms. Addition of chaotropic salts (1.0 M) caused progressive decreases in ordered structures and thermal stability following the lyotropic series of anions. The presence of several protein structure perturbants also led to changes in IR band intensities and DSC thermal stabilities, suggesting protein unfolding. Intermolecular antiparallel β-sheet (1620 and 1681 cm -1) band intensities started to increase when BWG was heated to 90°C, suggesting the initiation of protein aggregation. Increasing the time of the preheat treatment (at 100°C) caused progressive increases in T d and pronounced decreases in ΔH, suggesting partial denaturation and reassociation of protein molecules. © 2005 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/68521
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChoi, SMen_HK
dc.contributor.authorMa, CYen_HK
dc.date.accessioned2010-09-06T06:05:20Z-
dc.date.available2010-09-06T06:05:20Z-
dc.date.issued2005en_HK
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 2005, v. 53 n. 20, p. 8046-8053en_HK
dc.identifier.issn0021-8561en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68521-
dc.description.abstractFourier transform infrared (FTIR) spectroscopy and differential scanning calorimetry (DSC) were used to study changes in the conformation of globulin from common buckwheat (Fagopyrum esculentum Moench) (BWG) under various environmental conditions. The IR spectrum of the native BWG showed several major bands from 1691 to 1636 cm -1 in the amide I′ region, and the secondary structure composition was estimated as 34.5% β-sheets, 20.0% β-turns, 16.0% α-helices, and 14.4% random coils. Highly acidic and alkaline pH conditions induced decreases in β-sheet and α-helical contents, as well as in denaturation temperature (T d) and enthalpy of denaturation (ΔH), as shown in the DSC thermograms. Addition of chaotropic salts (1.0 M) caused progressive decreases in ordered structures and thermal stability following the lyotropic series of anions. The presence of several protein structure perturbants also led to changes in IR band intensities and DSC thermal stabilities, suggesting protein unfolding. Intermolecular antiparallel β-sheet (1620 and 1681 cm -1) band intensities started to increase when BWG was heated to 90°C, suggesting the initiation of protein aggregation. Increasing the time of the preheat treatment (at 100°C) caused progressive increases in T d and pronounced decreases in ΔH, suggesting partial denaturation and reassociation of protein molecules. © 2005 American Chemical Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_HK
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_HK
dc.subjectAggregationen_HK
dc.subjectBuckwheat globulinen_HK
dc.subjectDenaturationen_HK
dc.subjectDifferential scanning calorimetryen_HK
dc.subjectFagopyrum esculentum Moenchen_HK
dc.subjectFTIR spectroscopyen_HK
dc.subjectProtein conformationen_HK
dc.titleConformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by fourier transform infrared spectroscopy and differential scanning calorimetryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-8561&volume=53&spage=8046&epage=8053&date=2005&atitle=Conformational+study+of+globulin+from+common+buckwheat+(Fagopyrum+esculentum+Moench)+by+Fourier+transform+infrared+spectroscopy+and+differential+scanning+calorimetryen_HK
dc.identifier.emailMa, CY: macy@hkucc.hku.hken_HK
dc.identifier.authorityMa, CY=rp00759en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1021/jf051040ven_HK
dc.identifier.pmid16190669-
dc.identifier.scopuseid_2-s2.0-27144501099en_HK
dc.identifier.hkuros115291en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-27144501099&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume53en_HK
dc.identifier.issue20en_HK
dc.identifier.spage8046en_HK
dc.identifier.epage8053en_HK
dc.identifier.isiWOS:000232288800061-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChoi, SM=8873744400en_HK
dc.identifier.scopusauthoridMa, CY=7402924944en_HK

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