New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin
Cowpea seed β-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...
Gespeichert in:
Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2018-02, Vol.82 (2), p.285-291 |
---|---|
Hauptverfasser: | , , , , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 291 |
---|---|
container_issue | 2 |
container_start_page | 285 |
container_title | Bioscience, biotechnology, and biochemistry |
container_volume | 82 |
creator | de Souza Ferreira, Ederlan Capraro, Jessica Sessa, Fabio Magni, Chiara Demonte, Aureluce Consonni, Alessandro Augusto Neves, Valdir Maffud Cilli, Eduardo Duranti, Marcello Scarafoni, Alessio |
description | Cowpea seed β-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 β-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.
Using a shorted protocol, -vignin with a high degree of purity was obtain. A glycolylated gene product, never identified before, and its metal binding capacity were identified. |
doi_str_mv | 10.1080/09168451.2017.1419855 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmed_primary_29338640</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1080/09168451.2017.1419855</oup_id><sourcerecordid>1989585134</sourcerecordid><originalsourceid>FETCH-LOGICAL-c454t-6a9769bb8434643e21aaf0c5b6153221fee16b495cfea37a880450d9b1a56f433</originalsourceid><addsrcrecordid>eNqNkMtKxDAUhoMoOl4eQclSwY5Jc2mzUwZvMOjGyzKcdhKppE1NWgdfywfxmWyZ0aW4Cpx8_38OH0KHlEwpyckZUVTmXNBpSmg2pZyqXIgNNKGMZ4lUPNtEk5FJRmgH7cb4SsgwEHQb7aSKsVxyMkHzO7PEtXem7B0EbA10fTARe4tLv2wN4MJAg4-fqpcGcN-89NVIdnCK3RQ_g2tP8Ndn8j58V80-2rLgojlYv3vo8eryYXaTzO-vb2cX86TkgneJBJVJVRQ5Z1xyZlIKYEkpCkkFS1NqjaGy4EqUwzksgzwnXJCFKigIaTlje-h41dsG_9ab2Om6iqVxDhrj-6gHF0rkYlAxoGKFlsHHGIzVbahqCB-aEj2K1D8i9ShSr0UOuaP1ir6ozeI39WNuAMgK8H37787zVaRqrA81LH1wC93Bh_PBBmjKKmr2d8U3HHyOrg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1989585134</pqid></control><display><type>article</type><title>New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin</title><source>Oxford University Press Journals Current</source><source>Freely Accessible Japanese Titles</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>de Souza Ferreira, Ederlan ; Capraro, Jessica ; Sessa, Fabio ; Magni, Chiara ; Demonte, Aureluce ; Consonni, Alessandro ; Augusto Neves, Valdir ; Maffud Cilli, Eduardo ; Duranti, Marcello ; Scarafoni, Alessio</creator><creatorcontrib>de Souza Ferreira, Ederlan ; Capraro, Jessica ; Sessa, Fabio ; Magni, Chiara ; Demonte, Aureluce ; Consonni, Alessandro ; Augusto Neves, Valdir ; Maffud Cilli, Eduardo ; Duranti, Marcello ; Scarafoni, Alessio</creatorcontrib><description>Cowpea seed β-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 β-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.
Using a shorted protocol, -vignin with a high degree of purity was obtain. A glycolylated gene product, never identified before, and its metal binding capacity were identified.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1080/09168451.2017.1419855</identifier><identifier>PMID: 29338640</identifier><language>eng</language><publisher>England: Taylor & Francis</publisher><subject>glycosylation ; metal ion binding ; vicilin proteins ; Vigna ssp ; β-vignin</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2018-02, Vol.82 (2), p.285-291</ispartof><rights>2018 Japan Society for Bioscience, Biotechnology, and Agrochemistry 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-6a9769bb8434643e21aaf0c5b6153221fee16b495cfea37a880450d9b1a56f433</citedby><cites>FETCH-LOGICAL-c454t-6a9769bb8434643e21aaf0c5b6153221fee16b495cfea37a880450d9b1a56f433</cites><orcidid>0000-0003-1970-0122</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29338640$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de Souza Ferreira, Ederlan</creatorcontrib><creatorcontrib>Capraro, Jessica</creatorcontrib><creatorcontrib>Sessa, Fabio</creatorcontrib><creatorcontrib>Magni, Chiara</creatorcontrib><creatorcontrib>Demonte, Aureluce</creatorcontrib><creatorcontrib>Consonni, Alessandro</creatorcontrib><creatorcontrib>Augusto Neves, Valdir</creatorcontrib><creatorcontrib>Maffud Cilli, Eduardo</creatorcontrib><creatorcontrib>Duranti, Marcello</creatorcontrib><creatorcontrib>Scarafoni, Alessio</creatorcontrib><title>New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Cowpea seed β-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 β-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.
Using a shorted protocol, -vignin with a high degree of purity was obtain. A glycolylated gene product, never identified before, and its metal binding capacity were identified.</description><subject>glycosylation</subject><subject>metal ion binding</subject><subject>vicilin proteins</subject><subject>Vigna ssp</subject><subject>β-vignin</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNqNkMtKxDAUhoMoOl4eQclSwY5Jc2mzUwZvMOjGyzKcdhKppE1NWgdfywfxmWyZ0aW4Cpx8_38OH0KHlEwpyckZUVTmXNBpSmg2pZyqXIgNNKGMZ4lUPNtEk5FJRmgH7cb4SsgwEHQb7aSKsVxyMkHzO7PEtXem7B0EbA10fTARe4tLv2wN4MJAg4-fqpcGcN-89NVIdnCK3RQ_g2tP8Ndn8j58V80-2rLgojlYv3vo8eryYXaTzO-vb2cX86TkgneJBJVJVRQ5Z1xyZlIKYEkpCkkFS1NqjaGy4EqUwzksgzwnXJCFKigIaTlje-h41dsG_9ab2Om6iqVxDhrj-6gHF0rkYlAxoGKFlsHHGIzVbahqCB-aEj2K1D8i9ShSr0UOuaP1ir6ozeI39WNuAMgK8H37787zVaRqrA81LH1wC93Bh_PBBmjKKmr2d8U3HHyOrg</recordid><startdate>20180201</startdate><enddate>20180201</enddate><creator>de Souza Ferreira, Ederlan</creator><creator>Capraro, Jessica</creator><creator>Sessa, Fabio</creator><creator>Magni, Chiara</creator><creator>Demonte, Aureluce</creator><creator>Consonni, Alessandro</creator><creator>Augusto Neves, Valdir</creator><creator>Maffud Cilli, Eduardo</creator><creator>Duranti, Marcello</creator><creator>Scarafoni, Alessio</creator><general>Taylor & Francis</general><general>Oxford University Press</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-1970-0122</orcidid></search><sort><creationdate>20180201</creationdate><title>New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin</title><author>de Souza Ferreira, Ederlan ; Capraro, Jessica ; Sessa, Fabio ; Magni, Chiara ; Demonte, Aureluce ; Consonni, Alessandro ; Augusto Neves, Valdir ; Maffud Cilli, Eduardo ; Duranti, Marcello ; Scarafoni, Alessio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-6a9769bb8434643e21aaf0c5b6153221fee16b495cfea37a880450d9b1a56f433</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>glycosylation</topic><topic>metal ion binding</topic><topic>vicilin proteins</topic><topic>Vigna ssp</topic><topic>β-vignin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>de Souza Ferreira, Ederlan</creatorcontrib><creatorcontrib>Capraro, Jessica</creatorcontrib><creatorcontrib>Sessa, Fabio</creatorcontrib><creatorcontrib>Magni, Chiara</creatorcontrib><creatorcontrib>Demonte, Aureluce</creatorcontrib><creatorcontrib>Consonni, Alessandro</creatorcontrib><creatorcontrib>Augusto Neves, Valdir</creatorcontrib><creatorcontrib>Maffud Cilli, Eduardo</creatorcontrib><creatorcontrib>Duranti, Marcello</creatorcontrib><creatorcontrib>Scarafoni, Alessio</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de Souza Ferreira, Ederlan</au><au>Capraro, Jessica</au><au>Sessa, Fabio</au><au>Magni, Chiara</au><au>Demonte, Aureluce</au><au>Consonni, Alessandro</au><au>Augusto Neves, Valdir</au><au>Maffud Cilli, Eduardo</au><au>Duranti, Marcello</au><au>Scarafoni, Alessio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2018-02-01</date><risdate>2018</risdate><volume>82</volume><issue>2</issue><spage>285</spage><epage>291</epage><pages>285-291</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Cowpea seed β-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 β-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.
Using a shorted protocol, -vignin with a high degree of purity was obtain. A glycolylated gene product, never identified before, and its metal binding capacity were identified.</abstract><cop>England</cop><pub>Taylor & Francis</pub><pmid>29338640</pmid><doi>10.1080/09168451.2017.1419855</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-1970-0122</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0916-8451 |
ispartof | Bioscience, biotechnology, and biochemistry, 2018-02, Vol.82 (2), p.285-291 |
issn | 0916-8451 1347-6947 |
language | eng |
recordid | cdi_pubmed_primary_29338640 |
source | Oxford University Press Journals Current; Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals |
subjects | glycosylation metal ion binding vicilin proteins Vigna ssp β-vignin |
title | New molecular features of cowpea bean (Vigna unguiculata, l. Walp) β-vignin |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-01T14%3A53%3A28IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=New%20molecular%20features%20of%20cowpea%20bean%20(Vigna%20unguiculata,%20l.%20Walp)%20%CE%B2-vignin&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=de%20Souza%20Ferreira,%20Ederlan&rft.date=2018-02-01&rft.volume=82&rft.issue=2&rft.spage=285&rft.epage=291&rft.pages=285-291&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/10.1080/09168451.2017.1419855&rft_dat=%3Cproquest_pubme%3E1989585134%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1989585134&rft_id=info:pmid/29338640&rft_oup_id=10.1080/09168451.2017.1419855&rfr_iscdi=true |