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Investigation into the interaction between resveratrol and whey proteins using fluorescence spectroscopy
Author(s) -
Hemar Yacine,
Gerbeaud Marie,
Oliver Christine M.,
Augustin Mary Ann
Publication year - 2011
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.2011.02728.x
Subject(s) - resveratrol , lactoferrin , whey protein isolate , whey protein , chemistry , lactalbumin , fluorescence spectroscopy , protein aggregation , biochemistry , food science , chromatography , fluorescence , physics , quantum mechanics
Summary Fluorescence spectroscopy was used to investigate the interaction between resveratrol and whey proteins. The whey proteins examined were lactoferrin, holo‐lactoferrin, apo‐lactoferrin, whey protein isolate (WPI) and the β‐lactoglobulin‐ and α‐lactalbumin‐rich fractions of WPI. Both an analytical‐grade and food‐grade resveratrol were examined. In all the systems studied, it was found that resveratrol interacted with the whey proteins to form a 1:1 complex. The binding constant, K s, for the protein–resveratrol complex for all the proteins examined varied from 1.7 × 10 4 to 1.2 × 10 5 m −1 . Furthermore, the interaction between the whey proteins and resveratrol did not affect the secondary structure of the proteins.