Preparation and identification of dipeptidyl peptidase IV inhibitory peptides from quinoa protein

[Display omitted] •Quinoa protein hydrolysates 

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Veröffentlicht in:Food research international 2022-06, Vol.156, p.111176-111176, Article 111176
Hauptverfasser: You, Haixi, Wu, Tianliang, Wang, Wei, Li, Yiju, Liu, Xuebo, Ding, Long
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container_title Food research international
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creator You, Haixi
Wu, Tianliang
Wang, Wei
Li, Yiju
Liu, Xuebo
Ding, Long
description [Display omitted] •Quinoa protein hydrolysates 
doi_str_mv 10.1016/j.foodres.2022.111176
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The objective of this study was to investigate the dipeptidyl peptidase IV (DPP-IV) inhibitory properties of quinoa protein-derived peptides. After germination, quinoa protein was extracted and then hydrolyzed by different enzymes such as papain, Alcalase, Neutrase, and Flavourzyme and pepsin-trypsin digestion. Results showed that the quinoa protein hydrolysates (QPH) by pepsin-trypsin digestion displayed the highest DPP-IV inhibitory activity. When ultrafiltrated, the fraction of quinoa protein hydrolysate with molecular weight less than 1 kDa (QPH1) exhibited a superior DPP-IV inhibitory activity with IC50 of 3.40 ± 0.20 mg/mL in vitro and 2.20 ± 0.29 mg/mL in Caco-2 based in situ. Furthermore, the peptide sequences of QPH1 were identified by UPLC-MS/MS. Twenty quinoa-derived peptides were determined with in vitro DPP-IV inhibitory activities with IC50 values less than 500 μM. The peptides IPI, IPV, VAYPL and IPIN showed the highest in vitro DPP-IV inhibitory activities with IC50 of 5.25 ± 0.16, 26.15 ± 0.58, 42.93 ± 1.15, and 56.58 ± 3.36 μM, respectively. The in situ DPP-IV activities of Caco-2 cells were also attenuated by these four peptides with IC50 of 10.75 ± 0.87, 29.11 ± 1.79, 61.9 ± 4.23, and 92.59 ± 12.89 µM, respectively. Moreover, these four peptides were identified as competitive inhibitors of DPP-IV. Molecular docking showed that quinoa peptides IPI and IPV were predicted to form multiple hydrogen bonds, attractive charge, and hydrophobic interactions with the residues of active site of DPP-IV. This study confirms that quinoa protein is a good source for DPP-IV inhibitory peptides and has potential as ingredients in functional foods for the prevention or management of type 2 diabetes.</description><identifier>ISSN: 0963-9969</identifier><identifier>EISSN: 1873-7145</identifier><identifier>DOI: 10.1016/j.foodres.2022.111176</identifier><identifier>PMID: 35651037</identifier><language>eng</language><publisher>Canada: Elsevier Ltd</publisher><subject>Bioactive peptide ; Dipeptidyl peptidase IV ; Molecular docking ; Peptide identification ; Quinoa protein ; Type 2 diabetes</subject><ispartof>Food research international, 2022-06, Vol.156, p.111176-111176, Article 111176</ispartof><rights>2022 Elsevier Ltd</rights><rights>Copyright © 2022 Elsevier Ltd. 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The objective of this study was to investigate the dipeptidyl peptidase IV (DPP-IV) inhibitory properties of quinoa protein-derived peptides. After germination, quinoa protein was extracted and then hydrolyzed by different enzymes such as papain, Alcalase, Neutrase, and Flavourzyme and pepsin-trypsin digestion. Results showed that the quinoa protein hydrolysates (QPH) by pepsin-trypsin digestion displayed the highest DPP-IV inhibitory activity. When ultrafiltrated, the fraction of quinoa protein hydrolysate with molecular weight less than 1 kDa (QPH1) exhibited a superior DPP-IV inhibitory activity with IC50 of 3.40 ± 0.20 mg/mL in vitro and 2.20 ± 0.29 mg/mL in Caco-2 based in situ. Furthermore, the peptide sequences of QPH1 were identified by UPLC-MS/MS. Twenty quinoa-derived peptides were determined with in vitro DPP-IV inhibitory activities with IC50 values less than 500 μM. The peptides IPI, IPV, VAYPL and IPIN showed the highest in vitro DPP-IV inhibitory activities with IC50 of 5.25 ± 0.16, 26.15 ± 0.58, 42.93 ± 1.15, and 56.58 ± 3.36 μM, respectively. The in situ DPP-IV activities of Caco-2 cells were also attenuated by these four peptides with IC50 of 10.75 ± 0.87, 29.11 ± 1.79, 61.9 ± 4.23, and 92.59 ± 12.89 µM, respectively. Moreover, these four peptides were identified as competitive inhibitors of DPP-IV. Molecular docking showed that quinoa peptides IPI and IPV were predicted to form multiple hydrogen bonds, attractive charge, and hydrophobic interactions with the residues of active site of DPP-IV. This study confirms that quinoa protein is a good source for DPP-IV inhibitory peptides and has potential as ingredients in functional foods for the prevention or management of type 2 diabetes.</description><subject>Bioactive peptide</subject><subject>Dipeptidyl peptidase IV</subject><subject>Molecular docking</subject><subject>Peptide identification</subject><subject>Quinoa protein</subject><subject>Type 2 diabetes</subject><issn>0963-9969</issn><issn>1873-7145</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNqFkE9r3DAQxUVoSDZ_PkKLjr14K1mWZJ1KWdpkIdAeklyFZI3ILLuWI9mF_fZx8DbXzmWGx5t5zI-Qz5ytOePq224dUwoZyrpmdb3mc2l1Rla81aLSvJGfyIoZJSpjlLkkV6XsGGNKanNBLoVUkjOhV8T9yTC47EZMPXV9oBigHzFit0gp0oADDCOG454ugytAt88U-xf0OKZ8POlQaMzpQF8n7JOjQ04jYH9DzqPbF7g99Wvy9Ovn4-a-evh9t938eKi62six8r6DtjYixDayRknf1J61QrWKydiqRmhpmBfQSOU5ADe-BQ_GhSiZY-DENfm63J1zXycooz1g6WC_dz2kqdha6VqzRig9W-Vi7XIqJUO0Q8aDy0fLmX2na3f2RNe-07UL3Xnvyyli8gcIH1v_cM6G74sB5kf_ImRbOoS-g4AZutGGhP-JeAOCx4_Y</recordid><startdate>202206</startdate><enddate>202206</enddate><creator>You, Haixi</creator><creator>Wu, Tianliang</creator><creator>Wang, Wei</creator><creator>Li, Yiju</creator><creator>Liu, Xuebo</creator><creator>Ding, Long</creator><general>Elsevier Ltd</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>202206</creationdate><title>Preparation and identification of dipeptidyl peptidase IV inhibitory peptides from quinoa protein</title><author>You, Haixi ; Wu, Tianliang ; Wang, Wei ; Li, Yiju ; Liu, Xuebo ; Ding, Long</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c295t-bbce8293df8f0465b42b08368605f86437590b3e456b1ee19b8ebe9adf50a0ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Bioactive peptide</topic><topic>Dipeptidyl peptidase IV</topic><topic>Molecular docking</topic><topic>Peptide identification</topic><topic>Quinoa protein</topic><topic>Type 2 diabetes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>You, Haixi</creatorcontrib><creatorcontrib>Wu, Tianliang</creatorcontrib><creatorcontrib>Wang, Wei</creatorcontrib><creatorcontrib>Li, Yiju</creatorcontrib><creatorcontrib>Liu, Xuebo</creatorcontrib><creatorcontrib>Ding, Long</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Food research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>You, Haixi</au><au>Wu, Tianliang</au><au>Wang, Wei</au><au>Li, Yiju</au><au>Liu, Xuebo</au><au>Ding, Long</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preparation and identification of dipeptidyl peptidase IV inhibitory peptides from quinoa protein</atitle><jtitle>Food research international</jtitle><addtitle>Food Res Int</addtitle><date>2022-06</date><risdate>2022</risdate><volume>156</volume><spage>111176</spage><epage>111176</epage><pages>111176-111176</pages><artnum>111176</artnum><issn>0963-9969</issn><eissn>1873-7145</eissn><abstract>[Display omitted] •Quinoa protein hydrolysates &lt; 1 kDa inhibited in-vitro and in-situ DPP-IV activities.•Quinoa germinated for 2 h significantly increased the DPP-IV inhibitory activities.•Quinoa peptides IPI and IPV showed DPP-IV inhibitory activities with IC50 &lt; 30 μM in-vitro and in-situ.•IPI and IPV behaved as competitive inhibitors on DPP-IV.•IPI and IPV bound to DPP-IV with hydrogen bonds, attractive charge, and hydrophobic interactions. The objective of this study was to investigate the dipeptidyl peptidase IV (DPP-IV) inhibitory properties of quinoa protein-derived peptides. After germination, quinoa protein was extracted and then hydrolyzed by different enzymes such as papain, Alcalase, Neutrase, and Flavourzyme and pepsin-trypsin digestion. Results showed that the quinoa protein hydrolysates (QPH) by pepsin-trypsin digestion displayed the highest DPP-IV inhibitory activity. When ultrafiltrated, the fraction of quinoa protein hydrolysate with molecular weight less than 1 kDa (QPH1) exhibited a superior DPP-IV inhibitory activity with IC50 of 3.40 ± 0.20 mg/mL in vitro and 2.20 ± 0.29 mg/mL in Caco-2 based in situ. Furthermore, the peptide sequences of QPH1 were identified by UPLC-MS/MS. Twenty quinoa-derived peptides were determined with in vitro DPP-IV inhibitory activities with IC50 values less than 500 μM. The peptides IPI, IPV, VAYPL and IPIN showed the highest in vitro DPP-IV inhibitory activities with IC50 of 5.25 ± 0.16, 26.15 ± 0.58, 42.93 ± 1.15, and 56.58 ± 3.36 μM, respectively. The in situ DPP-IV activities of Caco-2 cells were also attenuated by these four peptides with IC50 of 10.75 ± 0.87, 29.11 ± 1.79, 61.9 ± 4.23, and 92.59 ± 12.89 µM, respectively. Moreover, these four peptides were identified as competitive inhibitors of DPP-IV. Molecular docking showed that quinoa peptides IPI and IPV were predicted to form multiple hydrogen bonds, attractive charge, and hydrophobic interactions with the residues of active site of DPP-IV. This study confirms that quinoa protein is a good source for DPP-IV inhibitory peptides and has potential as ingredients in functional foods for the prevention or management of type 2 diabetes.</abstract><cop>Canada</cop><pub>Elsevier Ltd</pub><pmid>35651037</pmid><doi>10.1016/j.foodres.2022.111176</doi><tpages>1</tpages></addata></record>
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subjects Bioactive peptide
Dipeptidyl peptidase IV
Molecular docking
Peptide identification
Quinoa protein
Type 2 diabetes
title Preparation and identification of dipeptidyl peptidase IV inhibitory peptides from quinoa protein
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