Bioseparation of alpha-amylase by forming insoluble complexes with

Autores
Porfiri, María Cecilia; Farruggia, Beatriz Monica; Romanini, Diana
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Precipitation of insoluble complexes between alpha-amylase from Aspergillus oryzae and polyacrylic acid was studied by us in a previous work as a strategy of protein concentration and purification. Here we studied the effect of these polyelectrolytes on the stability of the enzyme at the pH of higher interaction (3.00), as well as the stability of the precipitates formed after applied the above methodology. The polymers showed a stabilizing effect on the activity of alpha-amylase at pH 3.00, intensified when complexes are in the solid precipitated form before redissolve. In a subsequent step, a strain of Aspergillus oryzae was used as enzymatic source. In order to stimulate alpha-amylase production and secretion by the microorganism, we used a minimum culture medium with wheat processing residues as substrate. This has economic and environmental benefits, because of the recycling of agricultural wastes. When the technique of concentration and purification of alpha-amylase was implemented from these cultures we obtained satisfactory results, which demonstrate that this methodology is suitable for the concentration and purification of alpha-amylase from A. oryzae in an inexpensive way, since it uses agricultural materials without commercial value.
Fil: Porfiri, María Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Farruggia, Beatriz Monica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Romanini, Diana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
PRECIPITATION
INSOLUBLE COMPLEXES
ALPHA AMYLASE
POLYACRYLIC ACID
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/243217
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Bioseparation of alpha-amylase by forming insoluble complexes withPorfiri, María CeciliaFarruggia, Beatriz MonicaRomanini, DianaPRECIPITATIONINSOLUBLE COMPLEXESALPHA AMYLASEPOLYACRYLIC ACIDhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Precipitation of insoluble complexes between alpha-amylase from Aspergillus oryzae and polyacrylic acid was studied by us in a previous work as a strategy of protein concentration and purification. Here we studied the effect of these polyelectrolytes on the stability of the enzyme at the pH of higher interaction (3.00), as well as the stability of the precipitates formed after applied the above methodology. The polymers showed a stabilizing effect on the activity of alpha-amylase at pH 3.00, intensified when complexes are in the solid precipitated form before redissolve. In a subsequent step, a strain of Aspergillus oryzae was used as enzymatic source. In order to stimulate alpha-amylase production and secretion by the microorganism, we used a minimum culture medium with wheat processing residues as substrate. This has economic and environmental benefits, because of the recycling of agricultural wastes. When the technique of concentration and purification of alpha-amylase was implemented from these cultures we obtained satisfactory results, which demonstrate that this methodology is suitable for the concentration and purification of alpha-amylase from A. oryzae in an inexpensive way, since it uses agricultural materials without commercial value.Fil: Porfiri, María Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Farruggia, Beatriz Monica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; ArgentinaFil: Romanini, Diana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaElsevier Science2012-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/243217Porfiri, María Cecilia; Farruggia, Beatriz Monica; Romanini, Diana; Bioseparation of alpha-amylase by forming insoluble complexes with; Elsevier Science; Separation and Purification Technology; 92; 5-2012; 11-161383-5866CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1383586612001542info:eu-repo/semantics/altIdentifier/doi/10.1016/j.seppur.2012.03.004info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:59:31Zoai:ri.conicet.gov.ar:11336/243217instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:59:32.16CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Bioseparation of alpha-amylase by forming insoluble complexes with
title Bioseparation of alpha-amylase by forming insoluble complexes with
spellingShingle Bioseparation of alpha-amylase by forming insoluble complexes with
Porfiri, María Cecilia
PRECIPITATION
INSOLUBLE COMPLEXES
ALPHA AMYLASE
POLYACRYLIC ACID
title_short Bioseparation of alpha-amylase by forming insoluble complexes with
title_full Bioseparation of alpha-amylase by forming insoluble complexes with
title_fullStr Bioseparation of alpha-amylase by forming insoluble complexes with
title_full_unstemmed Bioseparation of alpha-amylase by forming insoluble complexes with
title_sort Bioseparation of alpha-amylase by forming insoluble complexes with
dc.creator.none.fl_str_mv Porfiri, María Cecilia
Farruggia, Beatriz Monica
Romanini, Diana
author Porfiri, María Cecilia
author_facet Porfiri, María Cecilia
Farruggia, Beatriz Monica
Romanini, Diana
author_role author
author2 Farruggia, Beatriz Monica
Romanini, Diana
author2_role author
author
dc.subject.none.fl_str_mv PRECIPITATION
INSOLUBLE COMPLEXES
ALPHA AMYLASE
POLYACRYLIC ACID
topic PRECIPITATION
INSOLUBLE COMPLEXES
ALPHA AMYLASE
POLYACRYLIC ACID
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Precipitation of insoluble complexes between alpha-amylase from Aspergillus oryzae and polyacrylic acid was studied by us in a previous work as a strategy of protein concentration and purification. Here we studied the effect of these polyelectrolytes on the stability of the enzyme at the pH of higher interaction (3.00), as well as the stability of the precipitates formed after applied the above methodology. The polymers showed a stabilizing effect on the activity of alpha-amylase at pH 3.00, intensified when complexes are in the solid precipitated form before redissolve. In a subsequent step, a strain of Aspergillus oryzae was used as enzymatic source. In order to stimulate alpha-amylase production and secretion by the microorganism, we used a minimum culture medium with wheat processing residues as substrate. This has economic and environmental benefits, because of the recycling of agricultural wastes. When the technique of concentration and purification of alpha-amylase was implemented from these cultures we obtained satisfactory results, which demonstrate that this methodology is suitable for the concentration and purification of alpha-amylase from A. oryzae in an inexpensive way, since it uses agricultural materials without commercial value.
Fil: Porfiri, María Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Farruggia, Beatriz Monica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina
Fil: Romanini, Diana. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Química y Física. Área Fisicoquímica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Precipitation of insoluble complexes between alpha-amylase from Aspergillus oryzae and polyacrylic acid was studied by us in a previous work as a strategy of protein concentration and purification. Here we studied the effect of these polyelectrolytes on the stability of the enzyme at the pH of higher interaction (3.00), as well as the stability of the precipitates formed after applied the above methodology. The polymers showed a stabilizing effect on the activity of alpha-amylase at pH 3.00, intensified when complexes are in the solid precipitated form before redissolve. In a subsequent step, a strain of Aspergillus oryzae was used as enzymatic source. In order to stimulate alpha-amylase production and secretion by the microorganism, we used a minimum culture medium with wheat processing residues as substrate. This has economic and environmental benefits, because of the recycling of agricultural wastes. When the technique of concentration and purification of alpha-amylase was implemented from these cultures we obtained satisfactory results, which demonstrate that this methodology is suitable for the concentration and purification of alpha-amylase from A. oryzae in an inexpensive way, since it uses agricultural materials without commercial value.
publishDate 2012
dc.date.none.fl_str_mv 2012-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/243217
Porfiri, María Cecilia; Farruggia, Beatriz Monica; Romanini, Diana; Bioseparation of alpha-amylase by forming insoluble complexes with; Elsevier Science; Separation and Purification Technology; 92; 5-2012; 11-16
1383-5866
CONICET Digital
CONICET
url http://hdl.handle.net/11336/243217
identifier_str_mv Porfiri, María Cecilia; Farruggia, Beatriz Monica; Romanini, Diana; Bioseparation of alpha-amylase by forming insoluble complexes with; Elsevier Science; Separation and Purification Technology; 92; 5-2012; 11-16
1383-5866
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1383586612001542
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.seppur.2012.03.004
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.238319

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