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

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...

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

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