New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin

Detalhes bibliográficos
Autor(a) principal: Ferreira, Ederlan de Souza
Data de Publicação: 2018
Outros Autores: Capraro, Jessica, Sessa, Fabio, Magni, Chiara, Demonte, Aureluce [UNESP], Consonni, Alessandro, Neves, Valdir Augusto [UNESP], Cilli, Eduardo Maffud [UNESP], Duranti, Marcello, Scarafoni, Alessio
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1080/09168451.2017.1419855
http://hdl.handle.net/11449/163885
Resumo: Cowpea seed -vignin, a vicilin-like globulin, proved to exert various health favourable effects, including blood cholesterol reduction in animal models. The need of a simple scalable enrichment procedure for further studies for tailored applications of this seed protein is crucial. A chromatography-independent fractionation method allowing to obtain a protein preparation with a high degree of homogeneity was used. Further purification was pursued to deep the molecular characterisation of -vignin. The results showed: (i) differing glycosylation patterns of the two constituent polypeptides, in agreement with amino acid sequence features; (ii) the seed accumulation of a gene product never identified before; (iii) metal binding capacity of native protein, a property observed only in few other legume seed vicilins.
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spelling New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vigninVigna sspvicilin proteinsbeta-vigninglycosylationmetal ion bindingCowpea seed -vignin, a vicilin-like globulin, proved to exert various health favourable effects, including blood cholesterol reduction in animal models. The need of a simple scalable enrichment procedure for further studies for tailored applications of this seed protein is crucial. A chromatography-independent fractionation method allowing to obtain a protein preparation with a high degree of homogeneity was used. Further purification was pursued to deep the molecular characterisation of -vignin. The results showed: (i) differing glycosylation patterns of the two constituent polypeptides, in agreement with amino acid sequence features; (ii) the seed accumulation of a gene product never identified before; (iii) metal binding capacity of native protein, a property observed only in few other legume seed vicilins.Univ Fed Bahia, Sch Pharm, Dept Bromatol Anal, Salvador, BA, BrazilUniv Milan, Dept Food Environm & Nutr Sci DeFENS, Milan, ItalySao Paulo State Univ, Dept Food & Nutr, Araraquara, BrazilSao Paulo State Univ, Inst Chem, Araraquara, BrazilSao Paulo State Univ, Dept Food & Nutr, Araraquara, BrazilSao Paulo State Univ, Inst Chem, Araraquara, BrazilTaylor & Francis LtdUniversidade Federal da Bahia (UFBA)Univ MilanUniversidade Estadual Paulista (Unesp)Ferreira, Ederlan de SouzaCapraro, JessicaSessa, FabioMagni, ChiaraDemonte, Aureluce [UNESP]Consonni, AlessandroNeves, Valdir Augusto [UNESP]Cilli, Eduardo Maffud [UNESP]Duranti, MarcelloScarafoni, Alessio2018-11-26T17:48:17Z2018-11-26T17:48:17Z2018-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article285-291application/pdfhttp://dx.doi.org/10.1080/09168451.2017.1419855Bioscience Biotechnology And Biochemistry. Abingdon: Taylor & Francis Ltd, v. 82, n. 2, p. 285-291, 2018.0916-8451http://hdl.handle.net/11449/16388510.1080/09168451.2017.1419855WOS:000425675900014WOS000425675900014.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBioscience Biotechnology And Biochemistry0,498info:eu-repo/semantics/openAccess2024-06-21T12:47:12Zoai:repositorio.unesp.br:11449/163885Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T22:06:10.000756Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
title New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
spellingShingle New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
Ferreira, Ederlan de Souza
Vigna ssp
vicilin proteins
beta-vignin
glycosylation
metal ion binding
title_short New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
title_full New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
title_fullStr New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
title_full_unstemmed New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
title_sort New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
author Ferreira, Ederlan de Souza
author_facet Ferreira, Ederlan de Souza
Capraro, Jessica
Sessa, Fabio
Magni, Chiara
Demonte, Aureluce [UNESP]
Consonni, Alessandro
Neves, Valdir Augusto [UNESP]
Cilli, Eduardo Maffud [UNESP]
Duranti, Marcello
Scarafoni, Alessio
author_role author
author2 Capraro, Jessica
Sessa, Fabio
Magni, Chiara
Demonte, Aureluce [UNESP]
Consonni, Alessandro
Neves, Valdir Augusto [UNESP]
Cilli, Eduardo Maffud [UNESP]
Duranti, Marcello
Scarafoni, Alessio
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal da Bahia (UFBA)
Univ Milan
Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Ferreira, Ederlan de Souza
Capraro, Jessica
Sessa, Fabio
Magni, Chiara
Demonte, Aureluce [UNESP]
Consonni, Alessandro
Neves, Valdir Augusto [UNESP]
Cilli, Eduardo Maffud [UNESP]
Duranti, Marcello
Scarafoni, Alessio
dc.subject.por.fl_str_mv Vigna ssp
vicilin proteins
beta-vignin
glycosylation
metal ion binding
topic Vigna ssp
vicilin proteins
beta-vignin
glycosylation
metal ion binding
description Cowpea seed -vignin, a vicilin-like globulin, proved to exert various health favourable effects, including blood cholesterol reduction in animal models. The need of a simple scalable enrichment procedure for further studies for tailored applications of this seed protein is crucial. A chromatography-independent fractionation method allowing to obtain a protein preparation with a high degree of homogeneity was used. Further purification was pursued to deep the molecular characterisation of -vignin. The results showed: (i) differing glycosylation patterns of the two constituent polypeptides, in agreement with amino acid sequence features; (ii) the seed accumulation of a gene product never identified before; (iii) metal binding capacity of native protein, a property observed only in few other legume seed vicilins.
publishDate 2018
dc.date.none.fl_str_mv 2018-11-26T17:48:17Z
2018-11-26T17:48:17Z
2018-01-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1080/09168451.2017.1419855
Bioscience Biotechnology And Biochemistry. Abingdon: Taylor & Francis Ltd, v. 82, n. 2, p. 285-291, 2018.
0916-8451
http://hdl.handle.net/11449/163885
10.1080/09168451.2017.1419855
WOS:000425675900014
WOS000425675900014.pdf
url http://dx.doi.org/10.1080/09168451.2017.1419855
http://hdl.handle.net/11449/163885
identifier_str_mv Bioscience Biotechnology And Biochemistry. Abingdon: Taylor & Francis Ltd, v. 82, n. 2, p. 285-291, 2018.
0916-8451
10.1080/09168451.2017.1419855
WOS:000425675900014
WOS000425675900014.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Bioscience Biotechnology And Biochemistry
0,498
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 285-291
application/pdf
dc.publisher.none.fl_str_mv Taylor & Francis Ltd
publisher.none.fl_str_mv Taylor & Francis Ltd
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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