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Influence of whey peptides on the surface activity of κ‐casein and β‐lactoglobulin A
Author(s) -
HAQUE ZAHUR U,
BOHOUA GUICHARD L,
WILLIAMS J BYRON,
BENJY MIKEL W
Publication year - 2010
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/j.1471-0307.2010.00578.x
Subject(s) - hydrolysate , whey protein , casein , chemistry , chromatography , beta lactoglobulin , food science , coating , biochemistry , hydrolysis , organic chemistry
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.