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Binding of olive oil phenolics to food proteins
Author(s) -
Pripp Are Hugo,
Vreeker Rob,
van Duynhoven John
Publication year - 2005
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1992
Subject(s) - chemistry , tyrosol , tannic acid , isothermal titration calorimetry , hydroxytyrosol , gallic acid , chromatography , food science , binding constant , bovine serum albumin , olive oil , polyphenol , biochemistry , organic chemistry , antioxidant , binding site
In this paper we investigate the interaction of phenolics extracted from olive oil with different food proteins (sodium caseinate, bovine serum albumin, β‐lactoglobulin and gelatin). Binding parameters are estimated using different experimental techniques: gel filtration, HPLC, isothermal titration calorimetry and NMR diffusion measurements. For comparison, the binding properties of gallic acid and tannic acid are also studied. The affinity of olive oil phenolics for the different food proteins is found to be relatively weak (compared with tannic acid). Binding constants are measured for the different phenolics in the extract: tyrosol and hydroxytyrosol do not (or very weakly) bind to the proteins, whereas other phenolics in the extract had binding constants of the order 10 2 –10 4 M −1 . The binding parameters determined have been discussed in relation to the possible effect of proteins on sensory properties (bitterness) of food emulsions containing olive oil. Copyright © 2004 Society of Chemical Industry