Influence of whey peptides on the surface activity of κ-casein and β-lactoglobulin A
Whey protein hydrolysate (WPH) was fractionated by reverse-phase chromatography to obtain fractions of varying surface-hydrophobicities. A model oil–water interface (MI) was pre-coated with the WPH or fractions thereof. Contact angle (θ) of sessile drops of κ-casein (κ-CN) or β-lactoglobulin A (β-LGA) were measured on the MI. Pre-coating of MI with un-fractionated WPH decreased θ, that is, increased surface activity, of both κ-CN (35–8.3°) and β-LGA (38–21.3°). Conversely, pre-coating of MI with the fractions significantly increased θ of both proteins as a function of hydrophobicity. Data provide insight into variability of whey protein functionality in food applications.
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Document Type: Research Article
Ecole des Sciences de la Nature Centre, Universitaire d′Abobo Adjame, Abidjan, Cote d′Ivoire
Department of Food Science, Nutrition and Health Promotion, MAFES, Mississippi State University, 203 Herzer Building, Stone Boulevard, Box 9805, Starkville, MS 39762, USA
Publication date: 01 May 2010