ACE inhibitory peptides from enzymatic hydrolysate of fermented black sesame seed: Random forest-based optimization, screening, and molecular docking analysis
文献类型： 外文期刊
作者： Du, Tonghao 1 ; Xu, Yazhou 1 ; Xu, Xiaoyan 1 ; Xiong, Shijin 1 ; Zhang, Linli 1 ; Dong, Biao 1 ; Huang, Jinqing 3 ; Huang, Tao 1 ; Xiao, Muyan 1 ; Xiong, Tao 1 ; Xie, Mingyong 1 ;
作者机构： 1.Nanchang Univ, Sch Food Sci & Technol, 235 Nanjing East Rd, Nanchang 330047, Jiangxi, Peoples R China
2.Nanchang Univ, State Key Lab Food Sci & Resources, 235 Nanjing East Rd, Nanchang 330047, Jiangxi, Peoples R China
3.Jiangxi Acad Agr Sci, Inst Agr Prod Proc, 602 Nanlian Rd, Nanchang 330200, Peoples R China
4.Nanchang Univ, Int Inst Food Innovat, Xiaolan Econ & Technol Dev Zone, Luozhu Rd, Nanchang 330052, Peoples R China
关键词： Black sesame seeds; RF-PSO optimization; Peptides; Angiotensin-I-converting enzyme; Inhibitory mechanism
期刊名称：FOOD CHEMISTRY （ 影响因子：8.8； 五年影响因子：8.6 ）
ISSN： 0308-8146
年卷期： 2024 年 437 卷
页码：
收录情况： SCI
摘要： In this study, black sesame seeds were fermented by Lactobacillus Plantarum NCU116 and then hydrolyzed using acid protease to improve Angiotensin-I-converting enzyme (ACE) inhibitory activity. The random forest-particle swarm optimization (RF-PSO) model was applied to predict the ACE inhibitory activity during the hydrolysis process based on the experimental data. After separating by adsorption chromatography, gel filtration chromatography, and reversed phased-high performance liquid chromatography and then screening in silico method, eight peptides were identified from fermented black sesame seed hydrolysates as ITAPHW, SLPNYHPSPR, QYLPR, IRPNGL, YHNAPIL, LSYPR, GFAGDDAPRA, and LDPNPRSF with IC50 values of 51.69 mu M, 146.67 mu M, 655.02 mu M, 752.60 mu M, 1.02 mM, 2.01 mM, 1.97 mM, and 3.43 mM, respectively. ITAPHW and SLPNYHPSPR exhibited high antioxidant activity and inhibited the ACE activity in a non-competitive pattern. Molecular docking revealed that the strong ACE inhibition of ITAPHW and SLPNYHPSPR is probably attributed to the interaction with Zn2+ of ACE.
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