Loading…

Investigation into the potential of commercially available lesser mealworm (A. diaperinus) protein to serve as sources of peptides with DPP‐IV inhibitory activity

Summary Food‐derived peptides are known to possess inhibitory activity against the dipeptidyl‐peptidase IV (DPP‐IV) enzyme, a target in the management of type 2 diabetes. While proteins from commonly consumed food commodities have been investigated as precursors of DPP‐IV‐inhibiting peptides, studie...

Full description

Saved in:
Bibliographic Details
Published in:International journal of food science & technology 2019-03, Vol.54 (3), p.696-704
Main Authors: Lacroix, Isabelle M. E., Dávalos Terán, Irene, Fogliano, Vincenzo, Wichers, Harry J.
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333
cites cdi_FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333
container_end_page 704
container_issue 3
container_start_page 696
container_title International journal of food science & technology
container_volume 54
creator Lacroix, Isabelle M. E.
Dávalos Terán, Irene
Fogliano, Vincenzo
Wichers, Harry J.
description Summary Food‐derived peptides are known to possess inhibitory activity against the dipeptidyl‐peptidase IV (DPP‐IV) enzyme, a target in the management of type 2 diabetes. While proteins from commonly consumed food commodities have been investigated as precursors of DPP‐IV‐inhibiting peptides, studies on novel protein sources, such as those from insects, are sparse. This research aimed to determine if DPP‐IV inhibitors can be generated upon in vitro digestion or enzymatic hydrolysis of lesser mealworm protein isolate and concentrate. Treatment of the proteins with digestive enzymes and proteases generated hydrolysates with varying potency, thermolysin being the most effective at releasing active peptides (IC50 = 0.63 and 0.60 mg mL−1 for the isolate and concentrate). Ultrafiltration of the thermolysin‐treated hydrolysates did not significantly improve the potency. This study shows that DPP‐IV inhibitors can be generated from lesser mealworm protein and provides insight on the potential of insects to serve as functional food ingredients. Generation of DPP‐IV inhibitory peptides by simulated gastrointestinal digestion and enzymatic hydrolysis of lesser mealworm (A. diaperinus) proteins.
doi_str_mv 10.1111/ijfs.13982
format article
fullrecord <record><control><sourceid>proquest_wagen</sourceid><recordid>TN_cdi_wageningen_narcis_oai_library_wur_nl_wurpubs_543207</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2196316743</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333</originalsourceid><addsrcrecordid>eNp9UUuO1DAQjRBINAMbTmCJDSClseN8OuxGAwONRmIkPlvLTirT1XLsYDvd6h1H4BCcjJNQoWeNFy6X_d6req4sey74WtB6g_shroVsN8WDbCVkXeVFXYiH2Yq3Fc-rspCPsycx7jnnhWzKVfZ76w4QE97phN4xdMmztAM2-QQuobbMD6zz4wiho8yemD5otNpYYBZihMBG0Pbow8heXq5Zj3qCgG6Or9gUSAQdI0nCHYDpyKKfQwdxUZ1gStjT-Yhpx97d3v75-Wv7nVrYocHkA5XqEh4wnZ5mjwZtIzy7jxfZt-v3X68-5jefP2yvLm_yriyqIodBNBW0G9E3De9Mb4yUxjRAVlvKDb32ZS85XYmu0UKWXOiWy7ruxYZLKS-yt2fdo74Dh4425TQZj8prVBZN0OGkjnNQzi5hmk1UVSkL3hD5xZlMtn_M9KdqT14d9asK0dZS1E25lHh9RnXBxxhgUFPAcVEVXC0jVMsI1b8REljc94MWTv9Bqu2n6y9nzl-03qQN</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2196316743</pqid></control><display><type>article</type><title>Investigation into the potential of commercially available lesser mealworm (A. diaperinus) protein to serve as sources of peptides with DPP‐IV inhibitory activity</title><source>Wiley</source><source>Oxford University Press Open Access</source><creator>Lacroix, Isabelle M. E. ; Dávalos Terán, Irene ; Fogliano, Vincenzo ; Wichers, Harry J.</creator><creatorcontrib>Lacroix, Isabelle M. E. ; Dávalos Terán, Irene ; Fogliano, Vincenzo ; Wichers, Harry J.</creatorcontrib><description>Summary Food‐derived peptides are known to possess inhibitory activity against the dipeptidyl‐peptidase IV (DPP‐IV) enzyme, a target in the management of type 2 diabetes. While proteins from commonly consumed food commodities have been investigated as precursors of DPP‐IV‐inhibiting peptides, studies on novel protein sources, such as those from insects, are sparse. This research aimed to determine if DPP‐IV inhibitors can be generated upon in vitro digestion or enzymatic hydrolysis of lesser mealworm protein isolate and concentrate. Treatment of the proteins with digestive enzymes and proteases generated hydrolysates with varying potency, thermolysin being the most effective at releasing active peptides (IC50 = 0.63 and 0.60 mg mL−1 for the isolate and concentrate). Ultrafiltration of the thermolysin‐treated hydrolysates did not significantly improve the potency. This study shows that DPP‐IV inhibitors can be generated from lesser mealworm protein and provides insight on the potential of insects to serve as functional food ingredients. Generation of DPP‐IV inhibitory peptides by simulated gastrointestinal digestion and enzymatic hydrolysis of lesser mealworm (A. diaperinus) proteins.</description><identifier>ISSN: 0950-5423</identifier><identifier>EISSN: 1365-2621</identifier><identifier>DOI: 10.1111/ijfs.13982</identifier><language>eng</language><publisher>Oxford: Wiley Subscription Services, Inc</publisher><subject>Commodities ; Diabetes mellitus ; Diabetes mellitus (non-insulin dependent) ; Digestive enzymes ; Dipeptidyl-peptidase IV ; Dipeptidyl-peptidase IV inhibitors ; Food ; Functional foods &amp; nutraceuticals ; Hydrolysates ; in vitro digestion ; Inhibitors ; Insects ; in vitro digestion ; lesser mealworm (A. diaperinus) protein ; Peptidase ; Peptides ; Protein sources ; Proteins ; Thermolysin ; type 2 diabetes ; Ultrafiltration</subject><ispartof>International journal of food science &amp; technology, 2019-03, Vol.54 (3), p.696-704</ispartof><rights>2018 The Authors. published by John Wiley &amp; Sons Ltd on behalf of Institute of Food, Science and Technology (IFSTTF)</rights><rights>2018. This article is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Wageningen University &amp; Research</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333</citedby><cites>FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333</cites><orcidid>0000-0003-4185-5753</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids></links><search><creatorcontrib>Lacroix, Isabelle M. E.</creatorcontrib><creatorcontrib>Dávalos Terán, Irene</creatorcontrib><creatorcontrib>Fogliano, Vincenzo</creatorcontrib><creatorcontrib>Wichers, Harry J.</creatorcontrib><title>Investigation into the potential of commercially available lesser mealworm (A. diaperinus) protein to serve as sources of peptides with DPP‐IV inhibitory activity</title><title>International journal of food science &amp; technology</title><description>Summary Food‐derived peptides are known to possess inhibitory activity against the dipeptidyl‐peptidase IV (DPP‐IV) enzyme, a target in the management of type 2 diabetes. While proteins from commonly consumed food commodities have been investigated as precursors of DPP‐IV‐inhibiting peptides, studies on novel protein sources, such as those from insects, are sparse. This research aimed to determine if DPP‐IV inhibitors can be generated upon in vitro digestion or enzymatic hydrolysis of lesser mealworm protein isolate and concentrate. Treatment of the proteins with digestive enzymes and proteases generated hydrolysates with varying potency, thermolysin being the most effective at releasing active peptides (IC50 = 0.63 and 0.60 mg mL−1 for the isolate and concentrate). Ultrafiltration of the thermolysin‐treated hydrolysates did not significantly improve the potency. This study shows that DPP‐IV inhibitors can be generated from lesser mealworm protein and provides insight on the potential of insects to serve as functional food ingredients. Generation of DPP‐IV inhibitory peptides by simulated gastrointestinal digestion and enzymatic hydrolysis of lesser mealworm (A. diaperinus) proteins.</description><subject>Commodities</subject><subject>Diabetes mellitus</subject><subject>Diabetes mellitus (non-insulin dependent)</subject><subject>Digestive enzymes</subject><subject>Dipeptidyl-peptidase IV</subject><subject>Dipeptidyl-peptidase IV inhibitors</subject><subject>Food</subject><subject>Functional foods &amp; nutraceuticals</subject><subject>Hydrolysates</subject><subject>in vitro digestion</subject><subject>Inhibitors</subject><subject>Insects</subject><subject>in vitro digestion</subject><subject>lesser mealworm (A. diaperinus) protein</subject><subject>Peptidase</subject><subject>Peptides</subject><subject>Protein sources</subject><subject>Proteins</subject><subject>Thermolysin</subject><subject>type 2 diabetes</subject><subject>Ultrafiltration</subject><issn>0950-5423</issn><issn>1365-2621</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><recordid>eNp9UUuO1DAQjRBINAMbTmCJDSClseN8OuxGAwONRmIkPlvLTirT1XLsYDvd6h1H4BCcjJNQoWeNFy6X_d6req4sey74WtB6g_shroVsN8WDbCVkXeVFXYiH2Yq3Fc-rspCPsycx7jnnhWzKVfZ76w4QE97phN4xdMmztAM2-QQuobbMD6zz4wiho8yemD5otNpYYBZihMBG0Pbow8heXq5Zj3qCgG6Or9gUSAQdI0nCHYDpyKKfQwdxUZ1gStjT-Yhpx97d3v75-Wv7nVrYocHkA5XqEh4wnZ5mjwZtIzy7jxfZt-v3X68-5jefP2yvLm_yriyqIodBNBW0G9E3De9Mb4yUxjRAVlvKDb32ZS85XYmu0UKWXOiWy7ruxYZLKS-yt2fdo74Dh4425TQZj8prVBZN0OGkjnNQzi5hmk1UVSkL3hD5xZlMtn_M9KdqT14d9asK0dZS1E25lHh9RnXBxxhgUFPAcVEVXC0jVMsI1b8REljc94MWTv9Bqu2n6y9nzl-03qQN</recordid><startdate>201903</startdate><enddate>201903</enddate><creator>Lacroix, Isabelle M. E.</creator><creator>Dávalos Terán, Irene</creator><creator>Fogliano, Vincenzo</creator><creator>Wichers, Harry J.</creator><general>Wiley Subscription Services, Inc</general><scope>24P</scope><scope>WIN</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7ST</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>SOI</scope><scope>QVL</scope><orcidid>https://orcid.org/0000-0003-4185-5753</orcidid></search><sort><creationdate>201903</creationdate><title>Investigation into the potential of commercially available lesser mealworm (A. diaperinus) protein to serve as sources of peptides with DPP‐IV inhibitory activity</title><author>Lacroix, Isabelle M. E. ; Dávalos Terán, Irene ; Fogliano, Vincenzo ; Wichers, Harry J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Commodities</topic><topic>Diabetes mellitus</topic><topic>Diabetes mellitus (non-insulin dependent)</topic><topic>Digestive enzymes</topic><topic>Dipeptidyl-peptidase IV</topic><topic>Dipeptidyl-peptidase IV inhibitors</topic><topic>Food</topic><topic>Functional foods &amp; nutraceuticals</topic><topic>Hydrolysates</topic><topic>in vitro digestion</topic><topic>Inhibitors</topic><topic>Insects</topic><topic>in vitro digestion</topic><topic>lesser mealworm (A. diaperinus) protein</topic><topic>Peptidase</topic><topic>Peptides</topic><topic>Protein sources</topic><topic>Proteins</topic><topic>Thermolysin</topic><topic>type 2 diabetes</topic><topic>Ultrafiltration</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lacroix, Isabelle M. E.</creatorcontrib><creatorcontrib>Dávalos Terán, Irene</creatorcontrib><creatorcontrib>Fogliano, Vincenzo</creatorcontrib><creatorcontrib>Wichers, Harry J.</creatorcontrib><collection>Wiley Online Library Open Access</collection><collection>Wiley Online Library Free Content</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics &amp; Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical &amp; Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology &amp; Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environment Abstracts</collection><collection>NARCIS:Publications</collection><jtitle>International journal of food science &amp; technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lacroix, Isabelle M. E.</au><au>Dávalos Terán, Irene</au><au>Fogliano, Vincenzo</au><au>Wichers, Harry J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Investigation into the potential of commercially available lesser mealworm (A. diaperinus) protein to serve as sources of peptides with DPP‐IV inhibitory activity</atitle><jtitle>International journal of food science &amp; technology</jtitle><date>2019-03</date><risdate>2019</risdate><volume>54</volume><issue>3</issue><spage>696</spage><epage>704</epage><pages>696-704</pages><issn>0950-5423</issn><eissn>1365-2621</eissn><abstract>Summary Food‐derived peptides are known to possess inhibitory activity against the dipeptidyl‐peptidase IV (DPP‐IV) enzyme, a target in the management of type 2 diabetes. While proteins from commonly consumed food commodities have been investigated as precursors of DPP‐IV‐inhibiting peptides, studies on novel protein sources, such as those from insects, are sparse. This research aimed to determine if DPP‐IV inhibitors can be generated upon in vitro digestion or enzymatic hydrolysis of lesser mealworm protein isolate and concentrate. Treatment of the proteins with digestive enzymes and proteases generated hydrolysates with varying potency, thermolysin being the most effective at releasing active peptides (IC50 = 0.63 and 0.60 mg mL−1 for the isolate and concentrate). Ultrafiltration of the thermolysin‐treated hydrolysates did not significantly improve the potency. This study shows that DPP‐IV inhibitors can be generated from lesser mealworm protein and provides insight on the potential of insects to serve as functional food ingredients. Generation of DPP‐IV inhibitory peptides by simulated gastrointestinal digestion and enzymatic hydrolysis of lesser mealworm (A. diaperinus) proteins.</abstract><cop>Oxford</cop><pub>Wiley Subscription Services, Inc</pub><doi>10.1111/ijfs.13982</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-4185-5753</orcidid><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0950-5423
ispartof International journal of food science & technology, 2019-03, Vol.54 (3), p.696-704
issn 0950-5423
1365-2621
language eng
recordid cdi_wageningen_narcis_oai_library_wur_nl_wurpubs_543207
source Wiley; Oxford University Press Open Access
subjects Commodities
Diabetes mellitus
Diabetes mellitus (non-insulin dependent)
Digestive enzymes
Dipeptidyl-peptidase IV
Dipeptidyl-peptidase IV inhibitors
Food
Functional foods & nutraceuticals
Hydrolysates
in vitro digestion
Inhibitors
Insects
in vitro digestion
lesser mealworm (A. diaperinus) protein
Peptidase
Peptides
Protein sources
Proteins
Thermolysin
type 2 diabetes
Ultrafiltration
title Investigation into the potential of commercially available lesser mealworm (A. diaperinus) protein to serve as sources of peptides with DPP‐IV inhibitory activity
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T20%3A30%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_wagen&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Investigation%20into%20the%20potential%20of%20commercially%20available%20lesser%20mealworm%20(A.%20diaperinus)%20protein%20to%20serve%20as%20sources%20of%20peptides%20with%20DPP%E2%80%90IV%20inhibitory%20activity&rft.jtitle=International%20journal%20of%20food%20science%20&%20technology&rft.au=Lacroix,%20Isabelle%20M.%20E.&rft.date=2019-03&rft.volume=54&rft.issue=3&rft.spage=696&rft.epage=704&rft.pages=696-704&rft.issn=0950-5423&rft.eissn=1365-2621&rft_id=info:doi/10.1111/ijfs.13982&rft_dat=%3Cproquest_wagen%3E2196316743%3C/proquest_wagen%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c4252-ef175e981d770cbdbb33bb7e02390cbb175d4d30b7e1c7a13401a90366d180333%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2196316743&rft_id=info:pmid/&rfr_iscdi=true