Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads

Autores
Cavello, Ivana Alejandra; Contreras Esquivel, Juan Carlos; Cavalitto, Sebastian Fernando
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Keratinase from Purpureocillium lilacinum LPSC # 876 was immobilized on chitosan beads using two different cross-linking agents: glutaraldehyde and genipin. For its immobilization certain parameters were optimized such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, enzyme immobilization resulted to be 96 and 92.8% for glutaraldehyde and genipin, respectively, with an activity recovery reaching up to 81% when genipin was used. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form, retaining more than 85% of its activity at pH 11 and 74% at 50 °C after 1 h of incubation. The residual activity of immobilized keratinase remained more than 60% of its initial value after five hydrolytic cycles. The results in this study support that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization.
Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentina
Fil: Contreras Esquivel, Juan Carlos. Universidad Autónoma de Coahuila; México
Fil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentina
Materia
Keratinase
Immobilization
Genipin
Chitosan Beads
Hair Waste
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/16111
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beadsCavello, Ivana AlejandraContreras Esquivel, Juan CarlosCavalitto, Sebastian FernandoKeratinaseImmobilizationGenipinChitosan BeadsHair Wastehttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Keratinase from Purpureocillium lilacinum LPSC # 876 was immobilized on chitosan beads using two different cross-linking agents: glutaraldehyde and genipin. For its immobilization certain parameters were optimized such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, enzyme immobilization resulted to be 96 and 92.8% for glutaraldehyde and genipin, respectively, with an activity recovery reaching up to 81% when genipin was used. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form, retaining more than 85% of its activity at pH 11 and 74% at 50 °C after 1 h of incubation. The residual activity of immobilized keratinase remained more than 60% of its initial value after five hydrolytic cycles. The results in this study support that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; ArgentinaFil: Contreras Esquivel, Juan Carlos. Universidad Autónoma de Coahuila; MéxicoFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; ArgentinaElsevier2014-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/16111Cavello, Ivana Alejandra; Contreras Esquivel, Juan Carlos; Cavalitto, Sebastian Fernando; Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads; Elsevier; Process Biochemistry; 49; 8; 8-2014; 1332-13361359-5113enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2014.04.016info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511314002645info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:54:41Zoai:ri.conicet.gov.ar:11336/16111instacron: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:34982025-09-29 09:54:42.206CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
title Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
spellingShingle Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
Cavello, Ivana Alejandra
Keratinase
Immobilization
Genipin
Chitosan Beads
Hair Waste
title_short Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
title_full Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
title_fullStr Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
title_full_unstemmed Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
title_sort Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads
dc.creator.none.fl_str_mv Cavello, Ivana Alejandra
Contreras Esquivel, Juan Carlos
Cavalitto, Sebastian Fernando
author Cavello, Ivana Alejandra
author_facet Cavello, Ivana Alejandra
Contreras Esquivel, Juan Carlos
Cavalitto, Sebastian Fernando
author_role author
author2 Contreras Esquivel, Juan Carlos
Cavalitto, Sebastian Fernando
author2_role author
author
dc.subject.none.fl_str_mv Keratinase
Immobilization
Genipin
Chitosan Beads
Hair Waste
topic Keratinase
Immobilization
Genipin
Chitosan Beads
Hair Waste
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Keratinase from Purpureocillium lilacinum LPSC # 876 was immobilized on chitosan beads using two different cross-linking agents: glutaraldehyde and genipin. For its immobilization certain parameters were optimized such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, enzyme immobilization resulted to be 96 and 92.8% for glutaraldehyde and genipin, respectively, with an activity recovery reaching up to 81% when genipin was used. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form, retaining more than 85% of its activity at pH 11 and 74% at 50 °C after 1 h of incubation. The residual activity of immobilized keratinase remained more than 60% of its initial value after five hydrolytic cycles. The results in this study support that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization.
Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentina
Fil: Contreras Esquivel, Juan Carlos. Universidad Autónoma de Coahuila; México
Fil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales. Universidad Nacional de la Plata. Facultad de Cs.exactas. Centro de Investigación y Desarrollo En Fermentaciones Industriales; Argentina
description Keratinase from Purpureocillium lilacinum LPSC # 876 was immobilized on chitosan beads using two different cross-linking agents: glutaraldehyde and genipin. For its immobilization certain parameters were optimized such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, enzyme immobilization resulted to be 96 and 92.8% for glutaraldehyde and genipin, respectively, with an activity recovery reaching up to 81% when genipin was used. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form, retaining more than 85% of its activity at pH 11 and 74% at 50 °C after 1 h of incubation. The residual activity of immobilized keratinase remained more than 60% of its initial value after five hydrolytic cycles. The results in this study support that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization.
publishDate 2014
dc.date.none.fl_str_mv 2014-08
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/11336/16111
Cavello, Ivana Alejandra; Contreras Esquivel, Juan Carlos; Cavalitto, Sebastian Fernando; Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads; Elsevier; Process Biochemistry; 49; 8; 8-2014; 1332-1336
1359-5113
url http://hdl.handle.net/11336/16111
identifier_str_mv Cavello, Ivana Alejandra; Contreras Esquivel, Juan Carlos; Cavalitto, Sebastian Fernando; Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads; Elsevier; Process Biochemistry; 49; 8; 8-2014; 1332-1336
1359-5113
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2014.04.016
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511314002645
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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_ 1844613659630764032
score 13.070432

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