Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins

被引：19

作者：

Wang, Wei ^{[1
]}

Liu, Xiaoqing ^{[1
]}

Li, Yiju ^{[1
]}

You, Haixi ^{[1
]}

Yu, Zhipeng ^{[2
]}

Wang, Liying ^{[1
,3
]}

Liu, Xuebo ^{[1
]}

Ding, Long ^{[1
]}

机构：

[1] Northwest A&F Univ, Coll Food Sci & Engn, Xianyang 712100, Peoples R China

[2] Bohai Univ, Coll Food Sci & Engn, Jinzhou 121013, Peoples R China

[3] Univ Shaanxi Prov, Engn Res Ctr Grain & Oil Functionalized Proc, Xianyang 712100, Peoples R China

来源：

FOODS | 2022年 / 11卷 / 10期

基金：

中国国家自然科学基金;

关键词：

oats; polypeptide bioactive; dipeptidyl peptidase-IV; molecular docking; CRYSTAL-STRUCTURE; HYDROLYSIS; COMPLEX;

D O I：

10.3390/foods11101406

中图分类号：

TS2 [食品工业];

学科分类号：

100403 [营养与食品卫生学];

摘要：

In this study, flavourzyme, papain, neutrase, and alcalase, as well as gastrointestinal digestion simulated with pepsin and pancreatin, were used to hydrolyze oat protein, and the dipeptidyl peptidase-IV (DPP-IV) inhibitory activities of the oat protein hydrolysates were investigated. The results indicated that the oat protein hydrolysate by neutrase showed the most potent DPP-IV inhibitory property with an IC50 value of 2.55 +/- 0.38 mg/mL. Using UPLC-MS/MS, ten new DPP-IV inhibitory peptides were identified from the oat protein hydrolysate by neutrase. Among these peptides, IPQHY, VPQHY, VAVVPF, and VPLGGF exhibited the strongest DPP-IV inhibitory activity with IC50 values below 50 mu M, and all of them acted as mixed-type inhibitors. Molecular docking indicated that the above four oat-derived peptides were predicted to form hydrogen bonds, attractive charge, and hydrophobic interactions with the residues of the active site of DPP-IV. Therefore, our results suggest that oat is an excellent protein source for food-derived DPP-IV inhibitory peptides and it has the prospect of becoming a dietary supplement for T2DM.

引用

页数：11

共 32 条

[1]

DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].