Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876

Autores
Cavello, Ivana Alejandra; Hours, Roque Alberto; Rojas, Natalia Lorena; Cavalitto, Sebastian Fernando
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A keratinolytic serine protease secreted by Purpureocillium lilacinum (formerly Paecilomyces lilacinus) upon culture in a basal medium containing 1% (w/v) hair waste as carbon and nitrogen source was purified and characterized. After purification the keratinase was resolved by SDS-PAGE as a homogeneus protein band of molecular mass 37.0 kDa. The extracellular keratinase of P. lilacinum was characterized by its appreciable stability over a broad pH range (from 4.0 to 9.0), and up to 65 °C, along with its strong inhibition by phenylmethylsulphonyl fluoride among the protease inhibitors tested (98.2% of inhibition), thus suggesting its nature as a serine protease. The enzyme was active and stable in the presence of organic solvents such as dimethylsulfoxide, methanol, and isopropanol; certain surfactants such as Triton X-100, sodium dodecylsulfate, and Tween 85; and bleaching agents such as hydrogen peroxide. These biochemical characteristics suggest the potential use of this enzyme in numerous industrial applications.
Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Fil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Fil: Rojas, Natalia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Fil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Materia
Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
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:11336/4312
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/4312
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876Cavello, Ivana AlejandraHours, Roque AlbertoRojas, Natalia LorenaCavalitto, Sebastian FernandoEnzyme purificationKeratinaseSerine proteaseHair wastePurpureocillium lilacinumhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2A keratinolytic serine protease secreted by Purpureocillium lilacinum (formerly Paecilomyces lilacinus) upon culture in a basal medium containing 1% (w/v) hair waste as carbon and nitrogen source was purified and characterized. After purification the keratinase was resolved by SDS-PAGE as a homogeneus protein band of molecular mass 37.0 kDa. The extracellular keratinase of P. lilacinum was characterized by its appreciable stability over a broad pH range (from 4.0 to 9.0), and up to 65 °C, along with its strong inhibition by phenylmethylsulphonyl fluoride among the protease inhibitors tested (98.2% of inhibition), thus suggesting its nature as a serine protease. The enzyme was active and stable in the presence of organic solvents such as dimethylsulfoxide, methanol, and isopropanol; certain surfactants such as Triton X-100, sodium dodecylsulfate, and Tween 85; and bleaching agents such as hydrogen peroxide. These biochemical characteristics suggest the potential use of this enzyme in numerous industrial applications.Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Rojas, Natalia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaFil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); ArgentinaElsevier2013-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4312Cavello, Ivana Alejandra; Hours, Roque Alberto; Rojas, Natalia Lorena; Cavalitto, Sebastian Fernando; Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876; Elsevier; Process Biochemistry; 48; 5-6; 4-2013; 972-9781359-5113enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511313001426info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2013.03.012info:eu-repo/semantics/altIdentifier/issn/1359-5113info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:58:09Zoai:ri.conicet.gov.ar:11336/4312instacron: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:34982025-10-15 14:58:10.199CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
title Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
spellingShingle Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
Cavello, Ivana Alejandra
Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
title_short Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
title_full Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
title_fullStr Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
title_full_unstemmed Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
title_sort Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
dc.creator.none.fl_str_mv Cavello, Ivana Alejandra
Hours, Roque Alberto
Rojas, Natalia Lorena
Cavalitto, Sebastian Fernando
author Cavello, Ivana Alejandra
author_facet Cavello, Ivana Alejandra
Hours, Roque Alberto
Rojas, Natalia Lorena
Cavalitto, Sebastian Fernando
author_role author
author2 Hours, Roque Alberto
Rojas, Natalia Lorena
Cavalitto, Sebastian Fernando
author2_role author
author
author
dc.subject.none.fl_str_mv Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
topic Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv A keratinolytic serine protease secreted by Purpureocillium lilacinum (formerly Paecilomyces lilacinus) upon culture in a basal medium containing 1% (w/v) hair waste as carbon and nitrogen source was purified and characterized. After purification the keratinase was resolved by SDS-PAGE as a homogeneus protein band of molecular mass 37.0 kDa. The extracellular keratinase of P. lilacinum was characterized by its appreciable stability over a broad pH range (from 4.0 to 9.0), and up to 65 °C, along with its strong inhibition by phenylmethylsulphonyl fluoride among the protease inhibitors tested (98.2% of inhibition), thus suggesting its nature as a serine protease. The enzyme was active and stable in the presence of organic solvents such as dimethylsulfoxide, methanol, and isopropanol; certain surfactants such as Triton X-100, sodium dodecylsulfate, and Tween 85; and bleaching agents such as hydrogen peroxide. These biochemical characteristics suggest the potential use of this enzyme in numerous industrial applications.
Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Fil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Fil: Rojas, Natalia Lorena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
Fil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico la Plata. Centro de Investigación y Desarrollo En Fermentaciones Industriales (i); Argentina
description A keratinolytic serine protease secreted by Purpureocillium lilacinum (formerly Paecilomyces lilacinus) upon culture in a basal medium containing 1% (w/v) hair waste as carbon and nitrogen source was purified and characterized. After purification the keratinase was resolved by SDS-PAGE as a homogeneus protein band of molecular mass 37.0 kDa. The extracellular keratinase of P. lilacinum was characterized by its appreciable stability over a broad pH range (from 4.0 to 9.0), and up to 65 °C, along with its strong inhibition by phenylmethylsulphonyl fluoride among the protease inhibitors tested (98.2% of inhibition), thus suggesting its nature as a serine protease. The enzyme was active and stable in the presence of organic solvents such as dimethylsulfoxide, methanol, and isopropanol; certain surfactants such as Triton X-100, sodium dodecylsulfate, and Tween 85; and bleaching agents such as hydrogen peroxide. These biochemical characteristics suggest the potential use of this enzyme in numerous industrial applications.
publishDate 2013
dc.date.none.fl_str_mv 2013-04
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/11336/4312
Cavello, Ivana Alejandra; Hours, Roque Alberto; Rojas, Natalia Lorena; Cavalitto, Sebastian Fernando; Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876; Elsevier; Process Biochemistry; 48; 5-6; 4-2013; 972-978
1359-5113
url http://hdl.handle.net/11336/4312
identifier_str_mv Cavello, Ivana Alejandra; Hours, Roque Alberto; Rojas, Natalia Lorena; Cavalitto, Sebastian Fernando; Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876; Elsevier; Process Biochemistry; 48; 5-6; 4-2013; 972-978
1359-5113
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1359511313001426
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.procbio.2013.03.012
info:eu-repo/semantics/altIdentifier/issn/1359-5113
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
application/pdf
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
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score 13.22299

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