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Article: Thermal Denaturation and Gelation Characteristics of β-Lactoglobulin Genetic Variants

TitleThermal Denaturation and Gelation Characteristics of β-Lactoglobulin Genetic Variants
Authors
Issue Date1998
Citation
Acs Symposium Series, 1998, v. 708, p. 168-183 How to Cite?
AbstractThe thermal characteristics of β-lactoglobulin (β-lg) genetic variants A and B were studied at pH 3.0, 5.0, 7.0 and 8.6 by differential scanning calorimetry (DSC). The β-lg B exhibited higher denaturation temperature and enthalpy than β-lg A and also denatured in a more cooperative fashion as indicated by a lower width at half-peak height. Fourier transform infrared spectroscopy (FTIR) was used to monitor changes in secondary structure of the two proteins when heated from 25 to 95°C. Results showed that β-lg A had a lower β-sheet content than the B variant at pH 3.0 and 5.0. At pH 7.0 and 8.6 the secondary structure of the two variants were similar. Aggregation bands (1682 cm -1 and ∼1622 cm -1) were observed when the proteins were heated at all pH values. The microstructure of gels made from 10% (w/v) solutions of β-lg A and B heated at 90°C for 30 min was studied by electron microscopy. The gel matrix of β-lg B at both acidic and alkaline pH was found to be made up of larger aggregates than the A variant. The aggregates of both variants were large (1-2 μm) and globular at acidic pH but much smaller (nanometer range) and amorphous at alkaline pH.
Persistent Identifierhttp://hdl.handle.net/10722/178809
ISSN
2005 Impact Factor: 0.566
2015 SCImago Journal Rankings: 0.163
References

 

DC FieldValueLanguage
dc.contributor.authorBoye, JIen_US
dc.contributor.authorMa, CYen_US
dc.contributor.authorIsmail, AAen_US
dc.date.accessioned2012-12-19T09:49:52Z-
dc.date.available2012-12-19T09:49:52Z-
dc.date.issued1998en_US
dc.identifier.citationAcs Symposium Series, 1998, v. 708, p. 168-183en_US
dc.identifier.issn0097-6156en_US
dc.identifier.urihttp://hdl.handle.net/10722/178809-
dc.description.abstractThe thermal characteristics of β-lactoglobulin (β-lg) genetic variants A and B were studied at pH 3.0, 5.0, 7.0 and 8.6 by differential scanning calorimetry (DSC). The β-lg B exhibited higher denaturation temperature and enthalpy than β-lg A and also denatured in a more cooperative fashion as indicated by a lower width at half-peak height. Fourier transform infrared spectroscopy (FTIR) was used to monitor changes in secondary structure of the two proteins when heated from 25 to 95°C. Results showed that β-lg A had a lower β-sheet content than the B variant at pH 3.0 and 5.0. At pH 7.0 and 8.6 the secondary structure of the two variants were similar. Aggregation bands (1682 cm -1 and ∼1622 cm -1) were observed when the proteins were heated at all pH values. The microstructure of gels made from 10% (w/v) solutions of β-lg A and B heated at 90°C for 30 min was studied by electron microscopy. The gel matrix of β-lg B at both acidic and alkaline pH was found to be made up of larger aggregates than the A variant. The aggregates of both variants were large (1-2 μm) and globular at acidic pH but much smaller (nanometer range) and amorphous at alkaline pH.en_US
dc.languageengen_US
dc.relation.ispartofACS Symposium Seriesen_US
dc.titleThermal Denaturation and Gelation Characteristics of β-Lactoglobulin Genetic Variantsen_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-s2.0-0042355257en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0042355257&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume708en_US
dc.identifier.spage168en_US
dc.identifier.epage183en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBoye, JI=7003390065en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridIsmail, AA=7201548364en_US

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