文献类型：期刊文献

英文题名：Identification of a Novel ACE Inhibitory Hexapeptide from Camellia Seed Cake and Evaluation of Its Stability

作者：Zhu, Qiaonan[1] Xue, Jiawen[1] Wang, Peng[1] Wang, Xianbo[2] Zhang, Jiaojiao[1] Fang, Xuezhi[3] He, Zhiping[1] Wu, Fenghua[4]

第一作者：Zhu, Qiaonan

通信作者：He, ZP[1];Wu, FH[2]

机构：[1]Zhejiang Agr & Forestry Univ, Coll Food & Hlth, Hangzhou 311300, Peoples R China;[2]Zhejiang Feixiangyuan Food Co Ltd, Lishui 323400, Peoples R China;[3]Chinese Acad Forestry, Res Inst Subtrop Forestry, Hangzhou 311400, Peoples R China;[4]Zhejiang Agr & Forestry Univ, Coll Adv Agr Sci, Hangzhou 311300, Peoples R China

年份：2023

卷号：12

期号：3

外文期刊名：FOODS

收录：;Scopus(收录号：2-s2.0-85147828402);WOS:【SCI-EXPANDED(收录号:WOS:000930424800001)】；

基金：This research was funded by the key research and development program of Zhejiang Province (No. 2021C02014).

语种：英文

外文关键词：camellia seed cake; ACE inhibitory peptide; inhibitory mechanism; molecular docking; stability

摘要：The camellia seed cake proteins (CP) used in this study were individually hydrolyzed with neutral protease, alkaline protease, papain, and trypsin. The results showed that the hydrolysate had the highest ACE inhibitory activity at 67.36 +/- 0.80% after four hours of neutral protease hydrolysis. Val-Val-Val-Pro-Gln-Asn (VVVPQN) was then obtained through ultrafiltration, Sephadex G-25 gel chromatography separation, LC-MS/MS analysis, and in silico screening. VVVPQN had ACE inhibitory activity with an IC50 value of 0.13 mg/mL (198.66 mu mol/L), and it inhibited ACE in a non-competitive manner. The molecular docking indicated that VVVPQN can combine with ACE to form eight hydrogen bonds. The results of the stability study showed that VVVPQN maintained high ACE-inhibitory activity in weakly acidic and neutral environments and that heat treatment (20-80 degrees C) and Na+, Mg2+, as well as Fe3+ metal ions had little effect on the activity of VVVPQN. Moreover, it remained relatively stable after in vitro simulated gastrointestinal digestion. These results revealed that VVVPQN identified in camellia seed cake has the potential to be applied in functional food or antihypertensive drugs.