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Article: Molecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and B

TitleMolecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and B
Authors
KeywordsΒ-Lactoglobulin
Denaturation
Differential Scanning Calorimetry
Electron Microscopy
Gelation
Genetic Variants
Infrared Spectroscopy
Issue Date1997
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcau
Citation
Journal Of Agricultural And Food Chemistry, 1997, v. 45 n. 5, p. 1608-1618 How to Cite?
AbstractThe thermal properties of β-lactoglobulins (β-lg) A and B at pH 3, 5, 7, and 8.6 were studied by differential scanning calorimetry. Fourier transform infrared spectroscopy was used to monitor changes in the secondary structure of the proteins when heated from 25 to 95 °C. The microstracture of β-lg A and B gels made from 10% (w/v) protein solutions by heating at 90 °C for 30 min was studied by scanning and transmission electron microscopy. β-Lg B had greater thermal stability and required more energy to denature than β-lg A; denaturation of β-lg B was also more cooperative. Infrared spectroscopy showed that β-lg B had a higher proportion of β-sheet than the A variant at pH 3 and 5. At pH 7 and 8.6 the secondary structures of the two variants were similar. At all four pH values, aggregation bands (1682 and ∼1622 cm -1) were observed when the proteins were heated. Electron microscopy showed that the gel matrix of β-lg B at both acid and alkaline pH was made up of larger aggregate structures than β-lg A. The aggregates formed by both variants were large (1-2 μm) and globular at acid pH but much smaller (nanometer range) and amorphous at alkaline pH. This information provides a useful model for studying the relationship between protein structure and function.
Persistent Identifierhttp://hdl.handle.net/10722/178843
ISSN
2015 Impact Factor: 2.857
2015 SCImago Journal Rankings: 1.246
References

 

DC FieldValueLanguage
dc.contributor.authorBoye, JIen_US
dc.contributor.authorMa, CYen_US
dc.contributor.authorIsmail, Aen_US
dc.contributor.authorHarwalkar, VRen_US
dc.contributor.authorKalab, Men_US
dc.date.accessioned2012-12-19T09:50:05Z-
dc.date.available2012-12-19T09:50:05Z-
dc.date.issued1997en_US
dc.identifier.citationJournal Of Agricultural And Food Chemistry, 1997, v. 45 n. 5, p. 1608-1618en_US
dc.identifier.issn0021-8561en_US
dc.identifier.urihttp://hdl.handle.net/10722/178843-
dc.description.abstractThe thermal properties of β-lactoglobulins (β-lg) A and B at pH 3, 5, 7, and 8.6 were studied by differential scanning calorimetry. Fourier transform infrared spectroscopy was used to monitor changes in the secondary structure of the proteins when heated from 25 to 95 °C. The microstracture of β-lg A and B gels made from 10% (w/v) protein solutions by heating at 90 °C for 30 min was studied by scanning and transmission electron microscopy. β-Lg B had greater thermal stability and required more energy to denature than β-lg A; denaturation of β-lg B was also more cooperative. Infrared spectroscopy showed that β-lg B had a higher proportion of β-sheet than the A variant at pH 3 and 5. At pH 7 and 8.6 the secondary structures of the two variants were similar. At all four pH values, aggregation bands (1682 and ∼1622 cm -1) were observed when the proteins were heated. Electron microscopy showed that the gel matrix of β-lg B at both acid and alkaline pH was made up of larger aggregate structures than β-lg A. The aggregates formed by both variants were large (1-2 μm) and globular at acid pH but much smaller (nanometer range) and amorphous at alkaline pH. This information provides a useful model for studying the relationship between protein structure and function.en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journal/jafcauen_US
dc.relation.ispartofJournal of Agricultural and Food Chemistryen_US
dc.subjectΒ-Lactoglobulinen_US
dc.subjectDenaturationen_US
dc.subjectDifferential Scanning Calorimetryen_US
dc.subjectElectron Microscopyen_US
dc.subjectGelationen_US
dc.subjectGenetic Variantsen_US
dc.subjectInfrared Spectroscopyen_US
dc.titleMolecular and Microstructural Studies of Thermal Denaturation and Gelation of β-Lactoglobulins A and Ben_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.scopuseid_2-s2.0-0642302370en_US
dc.identifier.hkuros35926-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0642302370&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume45en_US
dc.identifier.issue5en_US
dc.identifier.spage1608en_US
dc.identifier.epage1618en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBoye, JI=7003390065en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridIsmail, A=7201548364en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US
dc.identifier.scopusauthoridKalab, M=7005921318en_US

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