α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite

Autores
Rodriguez, J.; Soria, F.; Geronazzo, Hugo Isidoro; Destefanis, Hugo Alberto
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The α-amylase from Aspergillus oryzae was immobilized covalently onto expanded perlite (EP) and modified EP by treatment with TiO2 (EP-TiO2), dye HE3B (EP-HE3B) polyethylene terephthalate (PET)-hydrazide (EP-PET) and magnetite (EP-magnetite). The modified EP was characterized using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The supports were functionalized with aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The optimum pH for free and immobilized α-amylase was 5.5. Temperature of maximum activity for free enzyme and immobilized enzyme on EP-HE3B was 50°C. The immobilized enzyme in EP-APTES this value was 55°C. The immobilized α-amylase in EP-APTES and EP-HE3B-APTES exhibited better thermostability than free enzyme. The immobilized derivatives showed moderate operational stability by retaining 50% of initial activity after seven successive reuses.
Fil: Rodriguez, J.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Fil: Soria, F.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Fil: Geronazzo, Hugo Isidoro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Fil: Destefanis, Hugo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Materia
Perlitas
Zeolitas
Enzima Inmovilizada
Α-Amilasa
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:11336/4752
Acceder
id CONICETDig_2acff2ed5679ebaad8b46e77aa7efc09
oai_identifier_str oai:ri.conicet.gov.ar:11336/4752
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling α-Amylase Aspergillus oryzae Immobilized on Modified Expanded PerliteRodriguez, J.Soria, F.Geronazzo, Hugo IsidoroDestefanis, Hugo AlbertoPerlitasZeolitasEnzima InmovilizadaΑ-Amilasahttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The α-amylase from Aspergillus oryzae was immobilized covalently onto expanded perlite (EP) and modified EP by treatment with TiO2 (EP-TiO2), dye HE3B (EP-HE3B) polyethylene terephthalate (PET)-hydrazide (EP-PET) and magnetite (EP-magnetite). The modified EP was characterized using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The supports were functionalized with aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The optimum pH for free and immobilized α-amylase was 5.5. Temperature of maximum activity for free enzyme and immobilized enzyme on EP-HE3B was 50°C. The immobilized enzyme in EP-APTES this value was 55°C. The immobilized α-amylase in EP-APTES and EP-HE3B-APTES exhibited better thermostability than free enzyme. The immobilized derivatives showed moderate operational stability by retaining 50% of initial activity after seven successive reuses.Fil: Rodriguez, J.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); ArgentinaFil: Soria, F.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); ArgentinaFil: Geronazzo, Hugo Isidoro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); ArgentinaFil: Destefanis, Hugo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); ArgentinaDe Gruyter2014-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/mswordapplication/pdfhttp://hdl.handle.net/11336/4752Rodriguez, J.; Soria, F.; Geronazzo, Hugo Isidoro; Destefanis, Hugo Alberto; α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite; De Gruyter; International Journal Of Chemical Reactor Engineering; 12; 1; 10-2014; 2194-57481542-6580enginfo:eu-repo/semantics/altIdentifier/url/http://www.degruyter.com/view/j/ijcre.2014.12.issue-1/ijcre-2013-0145/ijcre-2013-0145.xmlinfo:eu-repo/semantics/altIdentifier/doi/10.1515/ijcre-2013-0145info:eu-repo/semantics/altIdentifier/issn/1542-6580info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:03:12Zoai:ri.conicet.gov.ar:11336/4752instacron: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:34982025-09-03 10:03:13.212CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
title α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
spellingShingle α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
Rodriguez, J.
Perlitas
Zeolitas
Enzima Inmovilizada
Α-Amilasa
title_short α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
title_full α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
title_fullStr α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
title_full_unstemmed α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
title_sort α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite
dc.creator.none.fl_str_mv Rodriguez, J.
Soria, F.
Geronazzo, Hugo Isidoro
Destefanis, Hugo Alberto
author Rodriguez, J.
author_facet Rodriguez, J.
Soria, F.
Geronazzo, Hugo Isidoro
Destefanis, Hugo Alberto
author_role author
author2 Soria, F.
Geronazzo, Hugo Isidoro
Destefanis, Hugo Alberto
author2_role author
author
author
dc.subject.none.fl_str_mv Perlitas
Zeolitas
Enzima Inmovilizada
Α-Amilasa
topic Perlitas
Zeolitas
Enzima Inmovilizada
Α-Amilasa
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The α-amylase from Aspergillus oryzae was immobilized covalently onto expanded perlite (EP) and modified EP by treatment with TiO2 (EP-TiO2), dye HE3B (EP-HE3B) polyethylene terephthalate (PET)-hydrazide (EP-PET) and magnetite (EP-magnetite). The modified EP was characterized using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The supports were functionalized with aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The optimum pH for free and immobilized α-amylase was 5.5. Temperature of maximum activity for free enzyme and immobilized enzyme on EP-HE3B was 50°C. The immobilized enzyme in EP-APTES this value was 55°C. The immobilized α-amylase in EP-APTES and EP-HE3B-APTES exhibited better thermostability than free enzyme. The immobilized derivatives showed moderate operational stability by retaining 50% of initial activity after seven successive reuses.
Fil: Rodriguez, J.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Fil: Soria, F.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Fil: Geronazzo, Hugo Isidoro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
Fil: Destefanis, Hugo Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Salta. Instituto de Investigación Para la Industria Química (i); Argentina
description The α-amylase from Aspergillus oryzae was immobilized covalently onto expanded perlite (EP) and modified EP by treatment with TiO2 (EP-TiO2), dye HE3B (EP-HE3B) polyethylene terephthalate (PET)-hydrazide (EP-PET) and magnetite (EP-magnetite). The modified EP was characterized using Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). The supports were functionalized with aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The optimum pH for free and immobilized α-amylase was 5.5. Temperature of maximum activity for free enzyme and immobilized enzyme on EP-HE3B was 50°C. The immobilized enzyme in EP-APTES this value was 55°C. The immobilized α-amylase in EP-APTES and EP-HE3B-APTES exhibited better thermostability than free enzyme. The immobilized derivatives showed moderate operational stability by retaining 50% of initial activity after seven successive reuses.
publishDate 2014
dc.date.none.fl_str_mv 2014-10
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/11336/4752
Rodriguez, J.; Soria, F.; Geronazzo, Hugo Isidoro; Destefanis, Hugo Alberto; α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite; De Gruyter; International Journal Of Chemical Reactor Engineering; 12; 1; 10-2014; 2194-5748
1542-6580
url http://hdl.handle.net/11336/4752
identifier_str_mv Rodriguez, J.; Soria, F.; Geronazzo, Hugo Isidoro; Destefanis, Hugo Alberto; α-Amylase Aspergillus oryzae Immobilized on Modified Expanded Perlite; De Gruyter; International Journal Of Chemical Reactor Engineering; 12; 1; 10-2014; 2194-5748
1542-6580
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.degruyter.com/view/j/ijcre.2014.12.issue-1/ijcre-2013-0145/ijcre-2013-0145.xml
info:eu-repo/semantics/altIdentifier/doi/10.1515/ijcre-2013-0145
info:eu-repo/semantics/altIdentifier/issn/1542-6580
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/msword
application/pdf
dc.publisher.none.fl_str_mv De Gruyter
publisher.none.fl_str_mv De Gruyter
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
_version_ 1842269788964913152
score 13.13397

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