Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility

The presence of so-called anti-nutritional factors can reduce the bioavailability of nutrients following consumption of seeds which are otherwise an excellent source of proteins, carbohydrates and micronutrients. Among the proteins associated with negative effects on quality in pea (Pisum sativum L....

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Autores: Olías, Raquel, Rayner, T., Clemente, Alfonso, Domoney, Claire
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2023
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/331995
Acceso en línea:http://hdl.handle.net/10261/331995
Access Level:acceso abierto
Palabra clave:Digestibility
Lectin
Mutants
Pea
Pea albumin 2
Seed proteins
Trypsin inhibitors
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spelling Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibilityOlías, RaquelRayner, T.Clemente, AlfonsoDomoney, ClaireDigestibilityLectinMutantsPeaPea albumin 2Seed proteinsTrypsin inhibitorsThe presence of so-called anti-nutritional factors can reduce the bioavailability of nutrients following consumption of seeds which are otherwise an excellent source of proteins, carbohydrates and micronutrients. Among the proteins associated with negative effects on quality in pea (Pisum sativum L.) seeds are lectin, pea albumin 2 (PA2) and trypsin inhibitors (TI). Here we have investigated the impact of these proteins on protein digestibility and amino acid availability, using naturally occurring and derived mutant lines of pea lacking these proteins. The mutations were stacked to generate a triple mutant which was compared with a wild-type progenitor and a line lacking the major seed trypsin inhibitors alone. In vitro digestions following the INFOGEST protocol revealed significant differences in the degree of hydrolysis, protein profile and apparent amino acid availability among the pea variants. Proteins resistant to digestion were identified by MALDI-TOF mass spectrometry and amino acid profiles of digested samples determined. The results indicate that pea seeds lacking certain proteins can be used in the development of novel foods which have improved protein digestibility, and without negative impact on seed protein concentration or yield.We gratefully acknowledge support for this work from the Department for Environment, Food and Rural Affairs (Defra) (CH0103, CH0111, Pulse Crop Genetic Improvement Network), the Biotechnology and Biological Sciences Research Council (BBSRC) (BB/P012523/1, BBS/E/J/000PR9799) and the John Innes Foundation. We acknowledge the financial support of AGL2017-83772-R funded by MCIN/AEI/ https://doi.org/10.13039/501100011033 and the European Union, and also the support from grant P20_00242 (PAIDI 2020) funded by Junta de Andalucía.ElsevierEuropean CommissionMinisterio de Ciencia e Innovación (España)Junta de AndalucíaBiotechnology and Biological Sciences Research Council (UK)John Innes FoundationConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2023202320232023info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/331995reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2017-83772-Rhttp://dx.doi.org/10.1016/j.foodres.2023.112825Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3319952026-05-22T06:33:51Z
dc.title.none.fl_str_mv Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
title Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
spellingShingle Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
Olías, Raquel
Digestibility
Lectin
Mutants
Pea
Pea albumin 2
Seed proteins
Trypsin inhibitors
title_short Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
title_full Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
title_fullStr Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
title_full_unstemmed Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
title_sort Combination of three null mutations affecting seed protein accumulation in pea (Pisum sativum L.) impacts positively on digestibility
dc.creator.none.fl_str_mv Olías, Raquel
Rayner, T.
Clemente, Alfonso
Domoney, Claire
author Olías, Raquel
author_facet Olías, Raquel
Rayner, T.
Clemente, Alfonso
Domoney, Claire
author_role author
author2 Rayner, T.
Clemente, Alfonso
Domoney, Claire
author2_role author
author
author
dc.contributor.none.fl_str_mv European Commission
Ministerio de Ciencia e Innovación (España)
Junta de Andalucía
Biotechnology and Biological Sciences Research Council (UK)
John Innes Foundation
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Digestibility
Lectin
Mutants
Pea
Pea albumin 2
Seed proteins
Trypsin inhibitors
topic Digestibility
Lectin
Mutants
Pea
Pea albumin 2
Seed proteins
Trypsin inhibitors
description The presence of so-called anti-nutritional factors can reduce the bioavailability of nutrients following consumption of seeds which are otherwise an excellent source of proteins, carbohydrates and micronutrients. Among the proteins associated with negative effects on quality in pea (Pisum sativum L.) seeds are lectin, pea albumin 2 (PA2) and trypsin inhibitors (TI). Here we have investigated the impact of these proteins on protein digestibility and amino acid availability, using naturally occurring and derived mutant lines of pea lacking these proteins. The mutations were stacked to generate a triple mutant which was compared with a wild-type progenitor and a line lacking the major seed trypsin inhibitors alone. In vitro digestions following the INFOGEST protocol revealed significant differences in the degree of hydrolysis, protein profile and apparent amino acid availability among the pea variants. Proteins resistant to digestion were identified by MALDI-TOF mass spectrometry and amino acid profiles of digested samples determined. The results indicate that pea seeds lacking certain proteins can be used in the development of novel foods which have improved protein digestibility, and without negative impact on seed protein concentration or yield.
publishDate 2023
dc.date.none.fl_str_mv 2023
2023
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/331995
url http://hdl.handle.net/10261/331995
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2017-83772-R
http://dx.doi.org/10.1016/j.foodres.2023.112825
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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