Competitive adsorption of water soluble plasma proteins from egg yolk at the oil/water interface

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Competitive adsorption of water soluble plasma proteins from egg yolk at the oil/water interface. / Nilsson, Lars; Osmark, Peter; Fernandez, Celine; Andersson, Marcus; Bergenståhl, Björn.

I: Journal of Agricultural and Food Chemistry, Vol. 54, Nr. 18, 2006, s. 6881-6887.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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T1 - Competitive adsorption of water soluble plasma proteins from egg yolk at the oil/water interface

AU - Nilsson, Lars

AU - Osmark, Peter

AU - Fernandez, Celine

AU - Andersson, Marcus

AU - Bergenståhl, Björn

PY - 2006

Y1 - 2006

N2 - Water soluble plasma proteins were fractionated from hen's egg yolk, and the molecular weight and pI of the most abundant protein species were characterized with gel electrophoresis. The proteins were identified by mass spectrometry. The protein fraction was used to produce oil-in-water emulsions, both at various protein concentrations and at various pH values, and the surface load was determined through serum depletion. The competitive adsorption was studied through the determination of nonadsorbing species with gel electrophoresis. The results show that it was possible to form an oil-in-water emulsion for which droplet size and maximum surface load depended on the protein concentration and pH. Serum albumin and YGP40 adsorbed selectively at the oil/water interface throughout the pH range investigated, and for albumin the selectivity increased close to its pI. It is suggested that this selective adsorption is due to long hydrophobic stretches in the polypeptide chain, which are present in the selectively adsorbing species but absent in less adsorbing species.

AB - Water soluble plasma proteins were fractionated from hen's egg yolk, and the molecular weight and pI of the most abundant protein species were characterized with gel electrophoresis. The proteins were identified by mass spectrometry. The protein fraction was used to produce oil-in-water emulsions, both at various protein concentrations and at various pH values, and the surface load was determined through serum depletion. The competitive adsorption was studied through the determination of nonadsorbing species with gel electrophoresis. The results show that it was possible to form an oil-in-water emulsion for which droplet size and maximum surface load depended on the protein concentration and pH. Serum albumin and YGP40 adsorbed selectively at the oil/water interface throughout the pH range investigated, and for albumin the selectivity increased close to its pI. It is suggested that this selective adsorption is due to long hydrophobic stretches in the polypeptide chain, which are present in the selectively adsorbing species but absent in less adsorbing species.

KW - competitive adsorption

KW - emulsion

KW - egg yolk proteins

KW - livetin

KW - interface

KW - oil/water

U2 - 10.1021/jf060738l

DO - 10.1021/jf060738l

M3 - Article

VL - 54

SP - 6881

EP - 6887

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 18

ER -