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Article: Effect of genetic polymorphism on the thermal stability β-Lactoglobulin and K-Casein mixture

TitleEffect of genetic polymorphism on the thermal stability β-Lactoglobulin and K-Casein mixture
Authors
KeywordsGenetic Polymorphism Β-Lactoglobulin
K-Casein
Thermal Stability
Issue Date1991
PublisherElsevier Inc. The Journal's web site is located at http://www.journalofdairyscience.org/
Citation
Journal Of Dairy Science, 1991, v. 74 n. 6, p. 1791-1802 How to Cite?
AbstractThe effect of calcium chloride and genetic variants of K-casein on the thermal stability of P-lactoglobulin isolated from bovine milk of known genetic types was investigated using differential scanning calorimetry. The effect of increasing calcium chloride from .10 to 1.0 M in piperazine-N,N'-bis(ethanesulfonic acid) buffer on the onset temperature, denaturation temperature, and width at half-peak height of these β-lactoglobu-lins was computed. β-Lactoglobulin BB was more stable than the other pheno-types at various β-lactoglobulin:K-casein ratios in phosphate buffer. The stability of β-lactoglobulin was enhanced by the presence of K-casein AA but lowered by K-casein AB and BB. Data obtained from an equal mixture of pMactoglobulin.-K-casein with various concentrations of calcium chloride also showed significant differences in thermal stability among the types of β-lactoglobulin and K-caseins. Polymorphic combinations of β-lactoglobulin BB:K-casein AA and β-lactoglobulin AB:x-casein AA produced the most stable system to heat perturbation but those of β-lactoglobulin AA and K-casein AA and β-lactoglobulin AA:K-casein BB, the least Our data also indicate that differences in width at half-peak height were associated with genetic polymorphism of these milk proteins. © 2012 American Dairy Science Association.
Persistent Identifierhttp://hdl.handle.net/10722/178369
ISSN
2015 Impact Factor: 2.408
2015 SCImago Journal Rankings: 1.401

 

DC FieldValueLanguage
dc.contributor.authorImafidon, IGen_US
dc.contributor.authorNgKwaiHang, KFen_US
dc.contributor.authorHarwalkar, VRen_US
dc.contributor.authorMa, CYen_US
dc.date.accessioned2012-12-19T09:47:18Z-
dc.date.available2012-12-19T09:47:18Z-
dc.date.issued1991en_US
dc.identifier.citationJournal Of Dairy Science, 1991, v. 74 n. 6, p. 1791-1802en_US
dc.identifier.issn0022-0302en_US
dc.identifier.urihttp://hdl.handle.net/10722/178369-
dc.description.abstractThe effect of calcium chloride and genetic variants of K-casein on the thermal stability of P-lactoglobulin isolated from bovine milk of known genetic types was investigated using differential scanning calorimetry. The effect of increasing calcium chloride from .10 to 1.0 M in piperazine-N,N'-bis(ethanesulfonic acid) buffer on the onset temperature, denaturation temperature, and width at half-peak height of these β-lactoglobu-lins was computed. β-Lactoglobulin BB was more stable than the other pheno-types at various β-lactoglobulin:K-casein ratios in phosphate buffer. The stability of β-lactoglobulin was enhanced by the presence of K-casein AA but lowered by K-casein AB and BB. Data obtained from an equal mixture of pMactoglobulin.-K-casein with various concentrations of calcium chloride also showed significant differences in thermal stability among the types of β-lactoglobulin and K-caseins. Polymorphic combinations of β-lactoglobulin BB:K-casein AA and β-lactoglobulin AB:x-casein AA produced the most stable system to heat perturbation but those of β-lactoglobulin AA and K-casein AA and β-lactoglobulin AA:K-casein BB, the least Our data also indicate that differences in width at half-peak height were associated with genetic polymorphism of these milk proteins. © 2012 American Dairy Science Association.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.journalofdairyscience.org/en_US
dc.relation.ispartofJournal of Dairy Scienceen_US
dc.subjectGenetic Polymorphism Β-Lactoglobulinen_US
dc.subjectK-Caseinen_US
dc.subjectThermal Stabilityen_US
dc.titleEffect of genetic polymorphism on the thermal stability β-Lactoglobulin and K-Casein mixtureen_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.doi10.3168/jds.S0022-0302(91)78344-6en_US
dc.identifier.scopuseid_2-s2.0-0000844768en_US
dc.identifier.volume74en_US
dc.identifier.issue6en_US
dc.identifier.spage1791en_US
dc.identifier.epage1802en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridImafidon, IG=6507368368en_US
dc.identifier.scopusauthoridNgKwaiHang, KF=7004851671en_US
dc.identifier.scopusauthoridHarwalkar, VR=35605979700en_US
dc.identifier.scopusauthoridMa, CY=7402924944en_US

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