Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment

Autores
Martínez, Yanina; Cavello, Ivana Alejandra; Hours, Roque Alberto; Cavalitto, Sebastián Fernando; Castro, Guillermo R.
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A keratinase isolated from Paecilomyces lilacinus (LPS #876) was tested against proteins present in the skin but the high enzyme activity was detected on collagen. Keratinase was physically immobilized onto PVA–pectin cryogels and enzyme release was 20.8 ± 2.1%, 63.8 ± 0.2%, 41.5 ± 3.5% and 26.0 ± 3.5% in cryogels containing pectins with esterification degrees (DE) 33.0%, 55.0%, 62.7% and 71.7% respectively at 37 ºC after 3 h incubation. In presence of 0.75 M NaCl, the percentage of enzyme release changed to: 57.5 ± 1.5, 65.8 ± 3.8, 57.3 ± 0.2 and 34.0 ± 4.0 for the four pectins respectively. In-vitro studies of enrofloxacin release from PVA–pectin cryogels at pH close to the human skin (pH = 5.5) showed 15.0% free antibiotic following first order kinetic at 37 ºC after 5 h incubation. However, in the presence of keratinase only 6.9% of enrofloxacin was released under the same experimental conditions.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
Materia
Bioquímica
PVA cryogels
Keratinase
Enrofloxacin
Controlled release
Wound healing
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/153219
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/153219
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatmentMartínez, YaninaCavello, Ivana AlejandraHours, Roque AlbertoCavalitto, Sebastián FernandoCastro, Guillermo R.BioquímicaPVA cryogelsKeratinaseEnrofloxacinControlled releaseWound healingA keratinase isolated from Paecilomyces lilacinus (LPS #876) was tested against proteins present in the skin but the high enzyme activity was detected on collagen. Keratinase was physically immobilized onto PVA–pectin cryogels and enzyme release was 20.8 ± 2.1%, 63.8 ± 0.2%, 41.5 ± 3.5% and 26.0 ± 3.5% in cryogels containing pectins with esterification degrees (DE) 33.0%, 55.0%, 62.7% and 71.7% respectively at 37 ºC after 3 h incubation. In presence of 0.75 M NaCl, the percentage of enzyme release changed to: 57.5 ± 1.5, 65.8 ± 3.8, 57.3 ± 0.2 and 34.0 ± 4.0 for the four pectins respectively. In-vitro studies of enrofloxacin release from PVA–pectin cryogels at pH close to the human skin (pH = 5.5) showed 15.0% free antibiotic following first order kinetic at 37 ºC after 5 h incubation. However, in the presence of keratinase only 6.9% of enrofloxacin was released under the same experimental conditions.Centro de Investigación y Desarrollo en Fermentaciones Industriales2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf280-284http://sedici.unlp.edu.ar/handle/10915/153219enginfo:eu-repo/semantics/altIdentifier/issn/1873-2976info:eu-repo/semantics/altIdentifier/issn/1873-2976info:eu-repo/semantics/altIdentifier/doi/10.1016/j.biortech.2013.02.063info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:20:32Zoai:sedici.unlp.edu.ar:10915/153219Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:20:32.662SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
title Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
spellingShingle Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
Martínez, Yanina
Bioquímica
PVA cryogels
Keratinase
Enrofloxacin
Controlled release
Wound healing
title_short Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
title_full Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
title_fullStr Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
title_full_unstemmed Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
title_sort Immobilized keratinase and enrofloxacin loaded on pectin PVA cryogel patches for antimicrobial treatment
dc.creator.none.fl_str_mv Martínez, Yanina
Cavello, Ivana Alejandra
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
Castro, Guillermo R.
author Martínez, Yanina
author_facet Martínez, Yanina
Cavello, Ivana Alejandra
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
Castro, Guillermo R.
author_role author
author2 Cavello, Ivana Alejandra
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
Castro, Guillermo R.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
PVA cryogels
Keratinase
Enrofloxacin
Controlled release
Wound healing
topic Bioquímica
PVA cryogels
Keratinase
Enrofloxacin
Controlled release
Wound healing
dc.description.none.fl_txt_mv A keratinase isolated from Paecilomyces lilacinus (LPS #876) was tested against proteins present in the skin but the high enzyme activity was detected on collagen. Keratinase was physically immobilized onto PVA–pectin cryogels and enzyme release was 20.8 ± 2.1%, 63.8 ± 0.2%, 41.5 ± 3.5% and 26.0 ± 3.5% in cryogels containing pectins with esterification degrees (DE) 33.0%, 55.0%, 62.7% and 71.7% respectively at 37 ºC after 3 h incubation. In presence of 0.75 M NaCl, the percentage of enzyme release changed to: 57.5 ± 1.5, 65.8 ± 3.8, 57.3 ± 0.2 and 34.0 ± 4.0 for the four pectins respectively. In-vitro studies of enrofloxacin release from PVA–pectin cryogels at pH close to the human skin (pH = 5.5) showed 15.0% free antibiotic following first order kinetic at 37 ºC after 5 h incubation. However, in the presence of keratinase only 6.9% of enrofloxacin was released under the same experimental conditions.
Centro de Investigación y Desarrollo en Fermentaciones Industriales
description A keratinase isolated from Paecilomyces lilacinus (LPS #876) was tested against proteins present in the skin but the high enzyme activity was detected on collagen. Keratinase was physically immobilized onto PVA–pectin cryogels and enzyme release was 20.8 ± 2.1%, 63.8 ± 0.2%, 41.5 ± 3.5% and 26.0 ± 3.5% in cryogels containing pectins with esterification degrees (DE) 33.0%, 55.0%, 62.7% and 71.7% respectively at 37 ºC after 3 h incubation. In presence of 0.75 M NaCl, the percentage of enzyme release changed to: 57.5 ± 1.5, 65.8 ± 3.8, 57.3 ± 0.2 and 34.0 ± 4.0 for the four pectins respectively. In-vitro studies of enrofloxacin release from PVA–pectin cryogels at pH close to the human skin (pH = 5.5) showed 15.0% free antibiotic following first order kinetic at 37 ºC after 5 h incubation. However, in the presence of keratinase only 6.9% of enrofloxacin was released under the same experimental conditions.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/153219
url http://sedici.unlp.edu.ar/handle/10915/153219
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1873-2976
info:eu-repo/semantics/altIdentifier/issn/1873-2976
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.biortech.2013.02.063
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
280-284
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 12.982451

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