Identification of peptides in Qingke baijiu and evaluation of its angiotensin converting enzyme (ACE) inhibitory activity and stability. (30th November 2022)

• Record Type: Journal Article
• Authors: Yin, Zhongtian; Yan, Ruyu; Jiang, Yunsong; Feng, Shengbao; Sun, Hailang; Sun, Jinyuan; Zhao, Dongrui; Li, Hehe; Wang, Bowen; Zhang, Ning
• Is Part Of: Food chemistry. Volume 395(2022)
• Publication Date: 2022-11-30
• Subjects: Qingke baijiu -- ACE inhibitory peptides -- Molecular docking -- Simulated gastrointestinal digestion -- Cell viability; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.133551
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Four novel ACEI peptides were identified from Qingke baijiu. Hydrophobicity contributed significantly to the ACEI activity of the peptides. Molecular docking illustrated the mechanism of action between peptides and ACE. Time-activity response curve evaluated the stability of the peptides' ACEI activity. Abstract: The active peptides in Qingke baijiu fermented from Qingke (highland barley) are rarely reported. This work was designed to accurately identify peptides in Qingke baijiu and evaluate their angiotensin-converting enzyme inhibitory activities in vitro . Four novel peptides, Val-Val-Thr-Gly-Val-Gly-Gly-Gln (VVTGVGGQ), Leu-Pro-Val-Gly-Pro (LPVGP), Leu-Leu-Ser-Pro-Pro (LLSPP), and Phe-Pro-Leu-Gln-Pro-His-Gln-Pro (FPLQPHQP) were identified by Nano-UPLC-MS/MS. Molecular docking showed that LPVGP and FPLQPHQP had a high affinity with ACE (binding energy −8.78, −10.02 kcal mol −1 ), which matched its in vitro ACE inhibitory activity (IC50 9.05, 5.03 µM). This might be related to their high hydrophobicity. Moreover, three peptides have C-terminal proline, which may contribute to their anti-digestive activity. The content of LPVGP was over 91.23% after digestion, while the content of VVTGVGGQ dropped to 55.47%. Finally, the four peptides have no obvious toxicity to Caco-2 cells. This study clarifies the ACE inhibitory activity and the structure–activity relationship of the four peptides identified in Qingke baijiu.