Mechanistic studies of inhibition on acrolein by myricetin. (1st September 2020)

• Record Type: Journal Article
• Authors: Zhang, Dingmin; Jiang, Xiaoyun; Xiao, Liubang; Lu, Yongling; Sang, Shengmin; Lv, Lishuang; Dong, Wenjiang
• Is Part Of: Food chemistry. Volume 323(2020)
• Publication Date: 2020-09-01
• Subjects: ACR acrolein -- MA mono-ACR adduct of myricetin -- DA di-ACR adduct of myricetin -- TA tri-ACR adduct of myricetin; Acrolein (PubChem CID:7847) -- Myricetin (PubChem CID: 5281672) -- Inhibitory mechanism -- Cookies; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2020.126788
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: B-ring of flavonol is also the active site to trap ACR. Myricetin could trap ACR to form the ACR adducts. The major mono- and di-ACR-myricetin adducts were purified and identified. Myricetin could dose-dependently inhibit the formation of ACR in cookies. Abstract: Acrolein (ACR) is an unsaturated aldehyde with high activity and toxicity and is produced in vivo and in food. This study investigated the impact of B-ring structure on the trapping of ACR by flavonols and the trapping mechanism and efficacy of ACR by myricetin. Galangin, kaempferol, quercetin, and myricetin, which possess the same A- and C-ring but different numbers of –OH groups on the B-ring, were selected for this study. Our results suggested that increasing the number of –OH groups on the B-ring can enhance the ACR trapping efficacy of flavonol and myrectin was identified as the most active flavonol. The adducts of myricetin with ACR under different ratios and incubation times were analyzed using LC-MS/MS. We also purified and identified the major mono- and di-ACR-myricetin adducts. Furthermore, myricetin could dose-dependently inhibit the formation of ACR in cookies through the formation of mono- and di-ACR adducts.