Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876

A keratinolytic serine protease secreted by <i>Purpureocillium lilacinum</i> (formerly <i>Paecilomyces lilacinus</i>) 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...

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Detalles Bibliográficos
Autores principales: Cavello, Ivana Alejandra, Hours, Roque Alberto, Rojas, Natalia Lorena, Cavalitto, Sebastián Fernando
Formato: Articulo Preprint
Lenguaje:Inglés
Publicado: 2013
Materias:
Ciencias Exactas
Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/104353
http://hdl.handle.net/11336/4312
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-104353
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
spellingShingle Ciencias Exactas
Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
Cavello, Ivana Alejandra
Hours, Roque Alberto
Rojas, Natalia Lorena
Cavalitto, Sebastián Fernando
Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
topic_facet Ciencias Exactas
Enzyme purification
Keratinase
Serine protease
Hair waste
Purpureocillium lilacinum
description A keratinolytic serine protease secreted by <i>Purpureocillium lilacinum</i> (formerly <i>Paecilomyces lilacinus</i>) 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 <i>P. lilacinum</i> 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.
format Articulo
Preprint
author Cavello, Ivana Alejandra
Hours, Roque Alberto
Rojas, Natalia Lorena
Cavalitto, Sebastián Fernando
author_facet Cavello, Ivana Alejandra
Hours, Roque Alberto
Rojas, Natalia Lorena
Cavalitto, Sebastián Fernando
author_sort Cavello, Ivana Alejandra
title Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
title_short Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
title_full Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
title_fullStr Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
title_full_unstemmed Purification and characterization of a keratinolytic serine protease from <i>Purpureocillium lilacinum</i> LPS # 876
title_sort purification and characterization of a keratinolytic serine protease from <i>purpureocillium lilacinum</i> lps # 876
publishDate 2013
url http://sedici.unlp.edu.ar/handle/10915/104353
http://hdl.handle.net/11336/4312
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