Influence of whey peptides on the surface activity of κ-casein and β-lactoglobulin A

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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.

Keywords: Functionality; Hydrophobicity; Peptide; Surface activity; Whey

Document Type: Research Article


Affiliations: 1: Ecole des Sciences de la Nature Centre, Universitaire d′Abobo Adjame, Abidjan, Cote d′Ivoire 2: 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: May 1, 2010

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