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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...
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Published in: | International journal of food science & technology 2019-03, Vol.54 (3), p.696-704 |
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container_title | International journal of food science & technology |
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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 |
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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 & 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 & technology, 2019-03, Vol.54 (3), p.696-704</ispartof><rights>2018 The Authors. published by John Wiley & 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 & 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 & 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 & 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. 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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 & 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 & 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 & 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 & 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 & technology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lacroix, Isabelle M. 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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> |
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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 |
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