Mixtures of bovine serum albumin (BSA) and several low molecular weight phenolics were incubated and fractionated using G‐50 Sephadex chromatography. Fractions corresponding to the protein and the possible phenolic‐protein complexes and fractions corresponding to the free phenolics were collected, and their phenolic content was determined. Among the selected commercial phenolic standards tested ( p ‐coumaric acid, p ‐hydroxybenzoic acid, protocatechuic acid, caffeic acid and (+)‐catechin), the strongest BSA‐binding affinity was demonstrated by 3,4‐dihydroxy benzoic and cinnamic acids (protocatechuic acid and caffeic acid), whereas p ‐hydroxybenzoic acid did not interact with BSA. The methodology was also applied to a phenolic extract obtained from lentils containing p ‐coumaric acid, a p ‐coumaric acid derivative, (+)‐catechin and procyanidins B 3 [(+)‐catechin‐(4αÕ8)‐(+)‐catechin] and B 1 [(‐)‐epicatechin‐(4αÕ8)‐(+)‐catechin]. Interactions observed among the lentil phenolics and BSA were comparable to those observed among the commercial phenolic standards and BSA.
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Bartolomé et al. (2000) studied this question.