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

Nilsson, Lars (author): Lund University,Lunds universitet,Livsmedelsteknik,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Department of Food Technology, Engineering and Nutrition,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH

Osmark, Peter (author): Lund University,Lunds universitet,Molekylär endokrinologi,Forskargrupper vid Lunds universitet,Molecular Endocrinology,Lund University Research Groups

Fernandez, Celine (author): Lund University,Lunds universitet,Molekylär endokrinologi,Forskargrupper vid Lunds universitet,Molecular Endocrinology,Lund University Research Groups

Andersson, Marcus (author)

Bergenståhl, Björn (author): Lund University,Lunds universitet,Livsmedelsteknik,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Department of Food Technology, Engineering and Nutrition,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH

(creator_code:org_t)

2006-08-05
2006
English.
In: Journal of Agricultural and Food Chemistry. - : American Chemical Society (ACS). - 0021-8561 .- 1520-5118. ; 54:18, s. 6881-6887

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Abstract Subject headings

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.

By the author/editor: Nilsson, Lars; Osmark, Peter; Fernandez, Celin ...; Andersson, Marcu ...; Bergenståhl, Bjö ...

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