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Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates

Bibliographic Details
Main Author: Sousa, Pedro
Publication Date: 2020
Other Authors: Borges, Sandra, Pintado, Manuela
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: http://hdl.handle.net/10400.14/30315
Summary: Edible insects are a promising protein source for the future generation, due to their nutritional composition, sustainability and low environmental impact. Recent studies demonstrated their potential as a protein base to obtain bioactive peptides with potential applicability in the food industry. The aim of this study was to hydrolyze and analyze the potential of the edible insect Alphitobius diaperinus protein to develop an improved insect food ingredient with bioactive properties. After evaluating various conditions for the enzymatic hydrolysis with Alcalase 2.5L and Corolase PP, the best condition chosen for each enzyme was an enzyme : substrate ratio of 1.5% for 4 hours and a ratio of 3.0% for 6 hours, respectively. Insect protein hydrolysates are demonstrated to have relevant bioactive properties, namely antioxidant (by ABTS and ORAC methods) and antihypertensive activities (through the ability to inhibit the angiotensin converting enzyme, ACE), but no antimicrobial or antidiabetic properties were observed. Antioxidant activity values for hydrolysates obtained with Alcalase 2.5L and Corolase PP were 95.0 ± 0.8 and 95.7 ± 1.0 μmol Trolox equivalent per g insect powder by the ABTS method, 825.6 ± 85.5 and 944.8 ± 68.1 μmol Trolox equivalent per g insect powder by the ORAC method, respectively. Insect hydrolysates were able to inhibit the ACE and IC50 values for insect hydrolysates obtained with Alcalase 2.5L and Corolase PP were 55.5 ± 6.2 and 107.4 ± 9.7 μg of protein per mL, respectively. These insect protein hydrolysates can be used as a supplement/ingredient in the food industry with potential health benefits.
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spelling Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysatesEdible insects are a promising protein source for the future generation, due to their nutritional composition, sustainability and low environmental impact. Recent studies demonstrated their potential as a protein base to obtain bioactive peptides with potential applicability in the food industry. The aim of this study was to hydrolyze and analyze the potential of the edible insect Alphitobius diaperinus protein to develop an improved insect food ingredient with bioactive properties. After evaluating various conditions for the enzymatic hydrolysis with Alcalase 2.5L and Corolase PP, the best condition chosen for each enzyme was an enzyme : substrate ratio of 1.5% for 4 hours and a ratio of 3.0% for 6 hours, respectively. Insect protein hydrolysates are demonstrated to have relevant bioactive properties, namely antioxidant (by ABTS and ORAC methods) and antihypertensive activities (through the ability to inhibit the angiotensin converting enzyme, ACE), but no antimicrobial or antidiabetic properties were observed. Antioxidant activity values for hydrolysates obtained with Alcalase 2.5L and Corolase PP were 95.0 ± 0.8 and 95.7 ± 1.0 μmol Trolox equivalent per g insect powder by the ABTS method, 825.6 ± 85.5 and 944.8 ± 68.1 μmol Trolox equivalent per g insect powder by the ORAC method, respectively. Insect hydrolysates were able to inhibit the ACE and IC50 values for insect hydrolysates obtained with Alcalase 2.5L and Corolase PP were 55.5 ± 6.2 and 107.4 ± 9.7 μg of protein per mL, respectively. These insect protein hydrolysates can be used as a supplement/ingredient in the food industry with potential health benefits.Royal Society of ChemistryVeritatiSousa, PedroBorges, SandraPintado, Manuela20202020-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/30315eng2042-649610.1039/d0fo00188kinfo:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2025-03-13T15:13:20Zoai:repositorio.ucp.pt:10400.14/30315Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T02:11:13.884391Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
title Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
spellingShingle Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
Sousa, Pedro
title_short Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
title_full Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
title_fullStr Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
title_full_unstemmed Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
title_sort Enzymatic hydrolysis of insect Alphitobius diaperinus towards the development of bioactive peptide hydrolysates
author Sousa, Pedro
author_facet Sousa, Pedro
Borges, Sandra
Pintado, Manuela
author_role author
author2 Borges, Sandra
Pintado, Manuela
author2_role author
author
dc.contributor.none.fl_str_mv Veritati
dc.contributor.author.fl_str_mv Sousa, Pedro
Borges, Sandra
Pintado, Manuela
description Edible insects are a promising protein source for the future generation, due to their nutritional composition, sustainability and low environmental impact. Recent studies demonstrated their potential as a protein base to obtain bioactive peptides with potential applicability in the food industry. The aim of this study was to hydrolyze and analyze the potential of the edible insect Alphitobius diaperinus protein to develop an improved insect food ingredient with bioactive properties. After evaluating various conditions for the enzymatic hydrolysis with Alcalase 2.5L and Corolase PP, the best condition chosen for each enzyme was an enzyme : substrate ratio of 1.5% for 4 hours and a ratio of 3.0% for 6 hours, respectively. Insect protein hydrolysates are demonstrated to have relevant bioactive properties, namely antioxidant (by ABTS and ORAC methods) and antihypertensive activities (through the ability to inhibit the angiotensin converting enzyme, ACE), but no antimicrobial or antidiabetic properties were observed. Antioxidant activity values for hydrolysates obtained with Alcalase 2.5L and Corolase PP were 95.0 ± 0.8 and 95.7 ± 1.0 μmol Trolox equivalent per g insect powder by the ABTS method, 825.6 ± 85.5 and 944.8 ± 68.1 μmol Trolox equivalent per g insect powder by the ORAC method, respectively. Insect hydrolysates were able to inhibit the ACE and IC50 values for insect hydrolysates obtained with Alcalase 2.5L and Corolase PP were 55.5 ± 6.2 and 107.4 ± 9.7 μg of protein per mL, respectively. These insect protein hydrolysates can be used as a supplement/ingredient in the food industry with potential health benefits.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.14/30315
url http://hdl.handle.net/10400.14/30315
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2042-6496
10.1039/d0fo00188k
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dc.publisher.none.fl_str_mv Royal Society of Chemistry
publisher.none.fl_str_mv Royal Society of Chemistry
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instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
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