Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest

Detalhes bibliográficos
Autor(a) principal: Iannucci,N.B.
Data de Publicação: 2003
Outros Autores: Wolman,F.J., Camperi,S.A., Cañizo,A.A.N., Grasselli,M., Cascone,O.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Chemical Engineering
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322003000100006
Resumo: High-performance affinity matrices were obtained by attaching pseudobiospecific ligands to hollow-fibre membranes. The neutral protease contained in FlavourzymeTM was purified to homogeneity with Yellow 4R-HE affinity hollow-fibre membranes. Immobilisation of Red HE-3B allowed purification of a milk-clotting enzyme obtained by solid-state culture of Mucor bacilliformis. Copper immobilisation through iminodiacetic acid allowed fractionation of Biocon Bioconcentrated PlusTM to separate the pectinesterase-containing fraction. The productivity of the developed processes - 1900, 94 and 750 U/ml.min, respectively - was 10- to 15-fold higher than that achieved with the same ligands immobilised on agarose-based soft gels, mainly due to the shortening of the purification processes.
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spelling Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interestaffinity chromatographypseudobiospecific ligandsprotein purificationHigh-performance affinity matrices were obtained by attaching pseudobiospecific ligands to hollow-fibre membranes. The neutral protease contained in FlavourzymeTM was purified to homogeneity with Yellow 4R-HE affinity hollow-fibre membranes. Immobilisation of Red HE-3B allowed purification of a milk-clotting enzyme obtained by solid-state culture of Mucor bacilliformis. Copper immobilisation through iminodiacetic acid allowed fractionation of Biocon Bioconcentrated PlusTM to separate the pectinesterase-containing fraction. The productivity of the developed processes - 1900, 94 and 750 U/ml.min, respectively - was 10- to 15-fold higher than that achieved with the same ligands immobilised on agarose-based soft gels, mainly due to the shortening of the purification processes.Brazilian Society of Chemical Engineering2003-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322003000100006Brazilian Journal of Chemical Engineering v.20 n.1 2003reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/S0104-66322003000100006info:eu-repo/semantics/openAccessIannucci,N.B.Wolman,F.J.Camperi,S.A.Cañizo,A.A.N.Grasselli,M.Cascone,O.eng2003-03-19T00:00:00Zoai:scielo:S0104-66322003000100006Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2003-03-19T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false
dc.title.none.fl_str_mv Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
title Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
spellingShingle Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
Iannucci,N.B.
affinity chromatography
pseudobiospecific ligands
protein purification
title_short Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
title_full Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
title_fullStr Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
title_full_unstemmed Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
title_sort Affinity chromatography with pseudobiospecific ligands on high-performance supports for purification of proteins of biotechnological interest
author Iannucci,N.B.
author_facet Iannucci,N.B.
Wolman,F.J.
Camperi,S.A.
Cañizo,A.A.N.
Grasselli,M.
Cascone,O.
author_role author
author2 Wolman,F.J.
Camperi,S.A.
Cañizo,A.A.N.
Grasselli,M.
Cascone,O.
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Iannucci,N.B.
Wolman,F.J.
Camperi,S.A.
Cañizo,A.A.N.
Grasselli,M.
Cascone,O.
dc.subject.por.fl_str_mv affinity chromatography
pseudobiospecific ligands
protein purification
topic affinity chromatography
pseudobiospecific ligands
protein purification
description High-performance affinity matrices were obtained by attaching pseudobiospecific ligands to hollow-fibre membranes. The neutral protease contained in FlavourzymeTM was purified to homogeneity with Yellow 4R-HE affinity hollow-fibre membranes. Immobilisation of Red HE-3B allowed purification of a milk-clotting enzyme obtained by solid-state culture of Mucor bacilliformis. Copper immobilisation through iminodiacetic acid allowed fractionation of Biocon Bioconcentrated PlusTM to separate the pectinesterase-containing fraction. The productivity of the developed processes - 1900, 94 and 750 U/ml.min, respectively - was 10- to 15-fold higher than that achieved with the same ligands immobilised on agarose-based soft gels, mainly due to the shortening of the purification processes.
publishDate 2003
dc.date.none.fl_str_mv 2003-03-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322003000100006
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322003000100006
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0104-66322003000100006
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
dc.source.none.fl_str_mv Brazilian Journal of Chemical Engineering v.20 n.1 2003
reponame:Brazilian Journal of Chemical Engineering
instname:Associação Brasileira de Engenharia Química (ABEQ)
instacron:ABEQ
instname_str Associação Brasileira de Engenharia Química (ABEQ)
instacron_str ABEQ
institution ABEQ
reponame_str Brazilian Journal of Chemical Engineering
collection Brazilian Journal of Chemical Engineering
repository.name.fl_str_mv Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)
repository.mail.fl_str_mv rgiudici@usp.br||rgiudici@usp.br
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