Artículo
Purification and characterization of a keratinolytic serine protease from Purpureocillium lilacinum LPS # 876
Cavello, Ivana Alejandra
; Hours, Roque Alberto
; Rojas, Natalia Lorena
; Cavalitto, Sebastian Fernando
![Icon](/themes/CONICETDigital/images/conicet.png)
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Fecha de publicación:
04/2013
Editorial:
Elsevier
Revista:
Process Biochemistry
ISSN:
1359-5113
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
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Articulos(CINDEFI)
Articulos de CENT.DE INV EN FERMENTACIONES INDUSTRIALES (I)
Articulos de CENT.DE INV EN FERMENTACIONES INDUSTRIALES (I)
Citación
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
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