Effects of anthocyanins on β-lactoglobulin glycoxidation: a study of mechanisms and structure–activity relationship. Issue 21 (27th September 2021)

• Record Type: Journal Article
• Authors: Wang, Ruifeng; Khalifa, Ibrahim; Du, Xia; Li, Kaikai; Xu, Yujuan; Li, Chunmei
• Is Part Of: Food & function. Volume 12:Issue 21(2021)
• Page Start: 10550
• Page End: 10562
• Publication Date: 2021-09-27
• Subjects: Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; Nutrition -- Periodicals; 664.07
• DOI: 10.1039/d1fo01665b
• Languages: English
• ISSNs: 2042-6496

Abstract

Abstract : We elucidated the underlying mechanisms of the anti-glycoxidation effects of five structurally different anthocyanins on glycated-β-lactoglobulin (β-Lg). Abstract : We elucidated the underlying mechanisms of the anti-glycoxidation effects of five structurally different anthocyanins on glycated-β-lactoglobulin (β-Lg). The results indicated that anthocyanins structurally inhibited the formation of advanced glycation end-products, where petunidin-3-rutinoside-( p -coumaryl)-5-glucoside (Pt-Gl) exerted higher effects than those of others ( p < 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.