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Article: Effects of medium and chemical modification on thermal characteristics of β-lactoglobulin
Title | Effects of medium and chemical modification on thermal characteristics of β-lactoglobulin |
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Authors | |
Keywords | Β-Lactoglobulin Dsc Protein Modification Thermal Properties |
Issue Date | 1996 |
Publisher | Akademiai 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/178591 |
ISSN | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
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dc.contributor.author | Ma, CY | en_US |
dc.contributor.author | Harwalkar, VR | en_US |
dc.date.accessioned | 2012-12-19T09:48:32Z | - |
dc.date.available | 2012-12-19T09:48:32Z | - |
dc.date.issued | 1996 | en_US |
dc.identifier.citation | Journal Of Thermal Analysis, 1996, v. 47 n. 5, p. 1513-1525 | en_US |
dc.identifier.issn | 0368-4466 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178591 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | Akademiai Kiado Rt. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1388-6150 | en_US |
dc.relation.ispartof | Journal of Thermal Analysis | en_US |
dc.subject | Β-Lactoglobulin | en_US |
dc.subject | Dsc | en_US |
dc.subject | Protein Modification | en_US |
dc.subject | Thermal Properties | en_US |
dc.title | Effects of medium and chemical modification on thermal characteristics of β-lactoglobulin | en_US |
dc.type | Article | en_US |
dc.identifier.email | Ma, CY: macy@hkucc.hku.hk | en_US |
dc.identifier.authority | Ma, CY=rp00759 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.scopus | eid_2-s2.0-0030287516 | en_US |
dc.identifier.hkuros | 22421 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0030287516&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 47 | en_US |
dc.identifier.issue | 5 | en_US |
dc.identifier.spage | 1513 | en_US |
dc.identifier.epage | 1525 | en_US |
dc.identifier.isi | WOS:A1996WA33100023 | - |
dc.publisher.place | Hungary | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.scopusauthorid | Harwalkar, VR=35605979700 | en_US |
dc.identifier.issnl | 0368-4466 | - |