Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins
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 in...
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| Format: | Article |
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MDPI AG
2022-05-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/10/1406 |
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| author | Wei Wang Xiaoqing Liu Yiju Li Haixi You Zhipeng Yu Liying Wang Xuebo Liu Long Ding |
| author_facet | Wei Wang Xiaoqing Liu Yiju Li Haixi You Zhipeng Yu Liying Wang Xuebo Liu Long Ding |
| author_sort | Wei Wang |
| collection | DOAJ |
| description | 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 IC<sub>50</sub> 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 IC<sub>50</sub> values below 50 μM, 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. |
| first_indexed | 2024-03-10T03:54:15Z |
| format | Article |
| id | doaj.art-85733538f76940d6b6d5f6348acf99c5 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-10T03:54:15Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-85733538f76940d6b6d5f6348acf99c52023-11-23T10:58:41ZengMDPI AGFoods2304-81582022-05-011110140610.3390/foods11101406Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat ProteinsWei Wang0Xiaoqing Liu1Yiju Li2Haixi You3Zhipeng Yu4Liying Wang5Xuebo Liu6Long Ding7College of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Bohai University, Jinzhou 121013, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaCollege of Food Science and Engineering, Northwest A&F University, Xianyang 712100, ChinaIn 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 IC<sub>50</sub> 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 IC<sub>50</sub> values below 50 μM, 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.https://www.mdpi.com/2304-8158/11/10/1406oatspolypeptide bioactivedipeptidyl peptidase-IVmolecular docking |
| spellingShingle | Wei Wang Xiaoqing Liu Yiju Li Haixi You Zhipeng Yu Liying Wang Xuebo Liu Long Ding Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins Foods oats polypeptide bioactive dipeptidyl peptidase-IV molecular docking |
| title | Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins |
| title_full | Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins |
| title_fullStr | Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins |
| title_full_unstemmed | Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins |
| title_short | Identification and Characterization of Dipeptidyl Peptidase-IV Inhibitory Peptides from Oat Proteins |
| title_sort | identification and characterization of dipeptidyl peptidase iv inhibitory peptides from oat proteins |
| topic | oats polypeptide bioactive dipeptidyl peptidase-IV molecular docking |
| url | https://www.mdpi.com/2304-8158/11/10/1406 |
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