New molecular features of cowpea bean (Vigna unguiculata, l. Walp) beta-vignin
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , , , |
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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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 |
|
_version_ |
1808129392399876096 |