Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis

<i>Paecilomyces lilacinus</i> (Thom) Samson LPS 876, a locally isolated fungal strain, was grown on minimal mineral medium containing “hair waste,” a residue from the hair-saving unhairing process, and produced a protease with keratinolytic activity. This enzyme was biochemically charact...

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Autores principales: Cavello, Ivana Alejandra, Hours, Roque Alberto, Cavalitto, Sebastián Fernando
Formato: Articulo
Lenguaje:Inglés
Publicado: 2012
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/104780
http://hdl.handle.net/11336/93905
https://www.hindawi.com/journals/btri/2012/369308/
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id I19-R120-10915-104780
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
hair waste
detergent stable
serine proteases
keratinolytic activity
thermostability
spellingShingle Ciencias Exactas
hair waste
detergent stable
serine proteases
keratinolytic activity
thermostability
Cavello, Ivana Alejandra
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
topic_facet Ciencias Exactas
hair waste
detergent stable
serine proteases
keratinolytic activity
thermostability
description <i>Paecilomyces lilacinus</i> (Thom) Samson LPS 876, a locally isolated fungal strain, was grown on minimal mineral medium containing “hair waste,” a residue from the hair-saving unhairing process, and produced a protease with keratinolytic activity. This enzyme was biochemically characterized. The optimum reaction conditions, determined with a response surface methodology, were 60°C and pH 6.0. It was remarkably stable in a wide range of pHs and temperatures. Addition of Ca<sup>2+</sup>, Mg<sup>2+</sup>, or sorbitol was found to be effective in increasing thermal stability of the protease. PMSF and Hg<sup>2+</sup> inhibited the proteolytic activity indicating the presence of a thiol-dependent serine protease. It showed high stability toward surfactants, bleaching agents, and solvents. It was also compatible with commercial detergents (7 mg/mL) such as Ariel, Skip, Drive, and Ace, retaining more than 70% of its proteolytic activity in all detergents after 1 h of incubation at 40°C. Wash performance analysis revealed that this protease could effectively remove blood stains. From these properties, this enzyme may be considered as a potential candidate for future use in biotechnological processes, as well as in the formulation of laundry detergents.
format Articulo
Articulo
author Cavello, Ivana Alejandra
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
author_facet Cavello, Ivana Alejandra
Hours, Roque Alberto
Cavalitto, Sebastián Fernando
author_sort Cavello, Ivana Alejandra
title Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
title_short Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
title_full Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
title_fullStr Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
title_full_unstemmed Bioprocessing of “Hair Waste” by <i>Paecilomyces lilacinus</i> as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis
title_sort bioprocessing of “hair waste” by <i>paecilomyces lilacinus</i> as a source of a bleach-stable, alkaline, and thermostable keratinase with potential application as a laundry detergent additive: characterization and wash performance analysis
publishDate 2012
url http://sedici.unlp.edu.ar/handle/10915/104780
http://hdl.handle.net/11336/93905
https://www.hindawi.com/journals/btri/2012/369308/
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