File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Effects of medium and chemical modification on thermal characteristics of β-lactoglobulin

TitleEffects of medium and chemical modification on thermal characteristics of β-lactoglobulin
Authors
KeywordsΒ-Lactoglobulin
Dsc
Protein Modification
Thermal Properties
Issue Date1996
PublisherAkademiai Kiado Rt. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1388-6150
Citation
Journal Of Thermal Analysis, 1996, v. 47 n. 5, p. 1513-1525 How to Cite?
AbstractThe thermal properties of β-lactoglobulin (β-LG) were studied by differential scanning calorimetry (DSC) under different medium conditions. pH, neutral salts, protein perturbants, and polyols all affected the DSC characteristics of β-LG. Acylation with fatty acids also changed the thermal properties, particularly peak width at half-height. The results suggest that the structural stability of β-LG is controlled by non-covalent forces, particularly electrostatic and hydrophobic interactions. Disulfide bonds did not contribute to the thermal response of β-LG. Fatty N-acylamino acids caused marked increases in thermal stability and decreases in denaturation enthalpy, and additional peaks were observed in the presence of some palmiloyl derivatives. © 1996 Akadémiai Kiadó.
Persistent Identifierhttp://hdl.handle.net/10722/178591
ISSN
1998 Impact Factor: 0.655
References

 

DC FieldValueLanguage
dc.contributor.authorMa, CYen_US
dc.contributor.authorHarwalkar, VRen_US
dc.date.accessioned2012-12-19T09:48:32Z-
dc.date.available2012-12-19T09:48:32Z-
dc.date.issued1996en_US
dc.identifier.citationJournal Of Thermal Analysis, 1996, v. 47 n. 5, p. 1513-1525en_US
dc.identifier.issn0368-4466en_US
dc.identifier.urihttp://hdl.handle.net/10722/178591-
dc.description.abstractThe thermal properties of β-lactoglobulin (β-LG) were studied by differential scanning calorimetry (DSC) under different medium conditions. pH, neutral salts, protein perturbants, and polyols all affected the DSC characteristics of β-LG. Acylation with fatty acids also changed the thermal properties, particularly peak width at half-height. The results suggest that the structural stability of β-LG is controlled by non-covalent forces, particularly electrostatic and hydrophobic interactions. Disulfide bonds did not contribute to the thermal response of β-LG. Fatty N-acylamino acids caused marked increases in thermal stability and decreases in denaturation enthalpy, and additional peaks were observed in the presence of some palmiloyl derivatives. © 1996 Akadémiai Kiadó.en_US
dc.languageengen_US
dc.publisherAkademiai Kiado Rt. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1388-6150en_US
dc.relation.ispartofJournal of Thermal Analysisen_US
dc.subjectΒ-Lactoglobulinen_US
dc.subjectDscen_US
dc.subjectProtein Modificationen_US
dc.subjectThermal Propertiesen_US
dc.titleEffects of medium and chemical modification on thermal characteristics of β-lactoglobulinen_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-s2.0-0030287516en_US
dc.identifier.hkuros22421-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030287516&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume47en_US
dc.identifier.issue5en_US
dc.identifier.spage1513en_US
dc.identifier.epage1525en_US
dc.publisher.placeHungaryen_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats