Effects of anthocyanins on β-lactoglobulin glycoxidation: a study of mechanisms and structure–activity relationship
Ruifeng Wang, Ibrahim Khalifa, Xia Du, Kaikai Li, Yujuan Xu, Chunmei Li
Abstract
< 0.05). Through the three main steps of glycoxidation, anthocyanins trapped intermediate dicarbonyls and blocked some of the glycation sites of β-Lg. UPLC-ESI-Q-TOF-MS characterized that these anthocyanins structurally formed mono- and di-GO/MGO adducts, and Pt-Gl formed adducts with both dicarbonyls. More importantly, Pt-Gl interacted with some of the glycation sites of β-Lg such as Lys100, Lys101, and Arg124. Structurally, it was found that high-molecular weight anthocyanins with coumaric acid acylation seem to be better than others, which was followed by di- and mono-glycoside anthocyanins. Overall, GO/MGO-trapping and β-Lg-anthocyanin binding are revealed as the key mechanisms of the anti-glycoxidation effects of anthocyanins on β-Lg, which could be used as effective glycation inhibitors in protein-rich matrices.