AbstractBACKGROUND: The interactions between phenolic compounds and proteins can modify protein properties important in the food industry. To understand the effects of these interactions, the covalent interactions between caffeoylquinic acid (chlorogenic acid, CQA) oxidised by polyphenol oxidase (PPO) at acidic pH 6 (pH 6) and α‐lactalbumin, lysozyme and bovine serum albumin (BSA) were compared with non‐enzymatically induced covalent interactions at alkaline pH (pH 9). The effects of these modifications on protein properties were examined.RESULTS: Both ways of modification seemed to result in protein modification mainly via dimeric rather than monomeric CQA quinones. These modifications led to a decrease in the number of free primary amino groups of the proteins. Modification with CQA alone induced a low degree of protein dimerisation, which also occurred through the action of PPO alone. Modification drastically reduced the solubility of lysozyme over a broad pH range, whereas that of α‐lactalbumin was strongly reduced only at pH values close to its pI. The solubility of BSA was much less affected than that of the other proteins and only at acidic pH.CONCLUSION: These results indicate some similarities between modifications at pH 6 and 9 and that both modifications clearly change the functional properties of globular proteins. Copyright © 2007 Society of Chemical Industry