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- Publisher Website: 10.3168/jds.S0022-0302(91)78344-6
- Scopus: eid_2-s2.0-0000844768
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Article: Effect of genetic polymorphism on the thermal stability β-Lactoglobulin and K-Casein mixture
Title | Effect of genetic polymorphism on the thermal stability β-Lactoglobulin and K-Casein mixture |
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Authors | |
Keywords | Genetic Polymorphism Β-Lactoglobulin K-Casein Thermal Stability |
Issue Date | 1991 |
Publisher | Elsevier 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/178369 |
ISSN | 2023 Impact Factor: 3.7 2023 SCImago Journal Rankings: 1.219 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Imafidon, IG | en_US |
dc.contributor.author | NgKwaiHang, KF | en_US |
dc.contributor.author | Harwalkar, VR | en_US |
dc.contributor.author | Ma, CY | en_US |
dc.date.accessioned | 2012-12-19T09:47:18Z | - |
dc.date.available | 2012-12-19T09:47:18Z | - |
dc.date.issued | 1991 | en_US |
dc.identifier.citation | Journal Of Dairy Science, 1991, v. 74 n. 6, p. 1791-1802 | en_US |
dc.identifier.issn | 0022-0302 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178369 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | Elsevier Inc. The Journal's web site is located at http://www.journalofdairyscience.org/ | en_US |
dc.relation.ispartof | Journal of Dairy Science | en_US |
dc.subject | Genetic Polymorphism Β-Lactoglobulin | en_US |
dc.subject | K-Casein | en_US |
dc.subject | Thermal Stability | en_US |
dc.title | Effect of genetic polymorphism on the thermal stability β-Lactoglobulin and K-Casein mixture | 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.doi | 10.3168/jds.S0022-0302(91)78344-6 | en_US |
dc.identifier.scopus | eid_2-s2.0-0000844768 | en_US |
dc.identifier.volume | 74 | en_US |
dc.identifier.issue | 6 | en_US |
dc.identifier.spage | 1791 | en_US |
dc.identifier.epage | 1802 | en_US |
dc.identifier.isi | WOS:A1991FU37900004 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | Imafidon, IG=6507368368 | en_US |
dc.identifier.scopusauthorid | NgKwaiHang, KF=7004851671 | en_US |
dc.identifier.scopusauthorid | Harwalkar, VR=35605979700 | en_US |
dc.identifier.scopusauthorid | Ma, CY=7402924944 | en_US |
dc.identifier.issnl | 0022-0302 | - |