Interactions of phenolic compounds with globular proteins and their effects on food-related functional properties

In order to modulate the functional properties of food proteins, the interactions between globular proteins and the monomeric phenolic, caffeoylquinic acid (CQA, chlorogenic acid), and the oligomeric phenolics, procyanidins, were characterized and investigated for their effect on protein functional properties. Non-covalent interactions between proteins and CQA involved a low affinity and did not affect protein solubility. Proteins show a medium affinity for procyanidins of an average degree of polymerization (DP) of 5.5, but weakly interacted with smaller procyanidins. Procyanidins of DP 5.5 strongly decreased protein solubility. Covalent interactions between proteins and CQA oxidised by polyphenol oxidase (PPO) or oxidised at alkaline pH resulted in protein modification mainly via dimeric CQA quinones. The covalent modifications of proteins with CQA strongly reduced protein solubility. Lysine, tyrosine, histidine and tryptophan were able to interact with CQA quinones. It can be concluded that for food non-covalent interactions are restricted to oligomeric phenolic