Effect of the attachment of valine residues on the physicochemical and functional properties of bovine serum albumin

Murphy, Margaret; Howell, Nazlin K.

doi:10.1002/jsfa.2740540211

Cited by 2 publications

(3 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Surface (So) and exposed (Se) hydrophobicity were determined using a fluorescent probe cis-parinaric acid (Howell &Taylor, 1991;Murphy &Howell, 1991). The surface hydrophobicity has been correlated with emulsification whereas the exposed hydrophobicity of proteins, heat denatured prior to measurement, has been reported to correlate well with foaming and gelation (Townsend & Nakai, 1983;Kato & Nakai, 1980).…”

Section: Physico-chemical Characterization Of Proteins Treated With Amentioning

confidence: 99%

“…In this case the ascorbic acid will adsorb more rapidly than the protein due to its higher diffusion co-efficient. It is possible that the presence of ascorbic acid or binding of ascorbic acid to the protein at the interface may alter the orientation of the protein or cause a conformation change, evidenced by the changes in hydrophobicity (Kato et al, 1981;Murphy & Howell, 1991), which led to enhanced foaming particularly for BSA. Secondly, hydrophobic interactions are also considered to be important.…”

Section: Functional Property Characterisationmentioning

confidence: 99%

See 1 more Smart Citation

Effect of ascorbic acid on the foaming and gelling of globular proteins

Howell

Taylor

1995

Int J of Food Sci Tech

View full text Add to dashboard Cite

Foam expansion and foam stability of plasma and egg albumen proteins were enhanced in the presence of increasing concentrations of ascorbic acid (0.1-1 .O%). BSA showed the greatest improvement in foaming properties following treatment with ascorbic acid, whilst foaming properties of egg albumen were improved to a limited extent. A combination of partial acid hydrolysis and treatment with 1% ascorbic acid was required to dramatically improve the foaming properties of bovine blood plasma. In the presence of sucrose, foam expansion of both native and ascorbic acid-treated blood plasma was decreased. In contrast the foam expansion of ascorbic acid-treated egg albumen was greater although this effect decreased slightly on incubation. The gelation of ascorbic acid treated proteins increased with increasing temperatures over 8O-9O0C, particularly for BSA and blood plasma, and with increasing concentrations of ascorbic acid. Ascorbic acid-treated proteins exhibited enhanced surface and exposed hydrophobicity and reduced numbers of sulphydryl groups indicating the involvement of these factors in foam and gel formation. KeywordsBovine blood plasma, bovine serum albumin, egg albumen, hydrophobicity, ovalbumin, protein modification, sulphydryl content.

show abstract

Section: Physico-chemical Characterization Of Proteins Treated With Amentioning

confidence: 99%

Section: Functional Property Characterisationmentioning

confidence: 99%

Effect of ascorbic acid on the foaming and gelling of globular proteins

Howell

Taylor

1995

Int J of Food Sci Tech

View full text Add to dashboard Cite

show abstract

“…The noted differences in the significance of BSA may be partly explained by methodical difficulties in the correct analysis of BSA. Currently available methods for the determination of BSA include radial immunodiffusion [3,22], isoelectric focusing and SDS-PAGE [16,20] or SE-chromatography [13].…”

Section: Introductionmentioning

confidence: 99%

An improved analytical approach for the determination of bovine serum albumin in milk

Lieske

Jantz²,

Finke³

2005

Lait

View full text Add to dashboard Cite

-The content of bovine serum albumin (BSA) in milk is considered as a marker of the mammary gland health of the cow. Based on its physico-chemical properties, BSA tends to form aggregates hindering its exact determination with the previously known colorimetric bromcresol green dye (BCG) procedure. The BCG method was improved by adjusting the milk salt buffer system for the exact determination of BSA in milk. In a parallel approach, size-exclusion chromatography was applied. It was found that the analytical availability of BSA in milk samples was best when milk samples were directly analyzed with BCG without sample treatments such as precipitation and filtration. Spiked milk samples showed a recovery of 98.8% (+/-1.5%) with the improved method. The revised BCG method was fast and reliable in comparison with size-exclusion chromatography, allowing an exact determination of BSA in milk. Based on the spectrometric and chromatographic results it was concluded that the partial oligomerization of BSA occurring in milk depends on different factors: pH, ionic strength, concentration of BSA, actual immunological status and substances affiliated to it. The improved BCG method could be effectively used for the control of the mammary gland health status of cows.bovine serum albumin / bromcresol green dye method / udder's health status Résumé -Une approche analytique améliorée pour la détermination de la sérum-albumine dans le lait de vache. La teneur du lait en sérum-albumine (BSA) est considérée comme un indice de la santé de la glande mammaire de la vache. En raison de ses propriétés physicochimiques, la BSA a tendance à s'agréger, ce qui en empêche la détermination précise avec la méthode colorimé-trique au vert de bromocrésol (BCG) actuellement connue. La méthode au BCG a été améliorée en ajustant le système tampon salin du lait en vue de la détermination exacte de la BSA dans le lait. Parallèlement, on a appliqué la chromatographie d'exclusion. La mise en évidence analytique de la BSA dans l'échantillon de lait était meilleure quand on analysait les échantillons de lait directement avec la procédure au BCG sans les avoir préalablement traités par des méthodes comme la précipi-tation et la filtration. Les échantillons de lait surchargés ont présenté un taux de récupération de 98,8 % (+/-1,5 %) avec la méthode améliorée. La méthode au BCG améliorée s'est montrée rapide et fiable par rapport à la chromatographie d'exclusion et a permis la détermination exacte de la BSA dans le lait. On a pu conclure, sur la base des résultats spectrométriques et chromatographiques obtenus, que l'oligomérisation partielle de la BSA qui se produit dans le lait dépend de plusieurs facteurs : le pH, la force ionique, la concentration de la BSA, le statut immunologique effectif et la présence des substances qui y sont liées. La méthode au BCG améliorée pourrait donner de bons résultats dans la surveillance du statut sanitaire des glandes mammaires de la vache. sérum-albumine bovine / méthode au vert de bromocrésol / statut sanitaire de...

show abstract

Effect of the attachment of valine residues on the physicochemical and functional properties of bovine serum albumin

Cited by 2 publications

References 16 publications

Effect of ascorbic acid on the foaming and gelling of globular proteins

Effect of ascorbic acid on the foaming and gelling of globular proteins

An improved analytical approach for the determination of bovine serum albumin in milk

Contact Info

Product

Resources

About