dc.creator | Cavello, Ivana Alejandra | |
dc.creator | Hours, Roque Alberto | |
dc.creator | Cavalitto, Sebastian Fernando | |
dc.date.accessioned | 2020-01-07T19:55:37Z | |
dc.date.accessioned | 2022-10-15T01:02:58Z | |
dc.date.available | 2020-01-07T19:55:37Z | |
dc.date.available | 2022-10-15T01:02:58Z | |
dc.date.created | 2020-01-07T19:55:37Z | |
dc.date.issued | 2012-12 | |
dc.identifier | Cavello, Ivana Alejandra; Hours, Roque Alberto; Cavalitto, Sebastian Fernando; Bioprocessing of “Hair Waste” by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis; Hindawi Publishing Corporation; Biotechnology Research International; 2012; 12-2012; 1-12 | |
dc.identifier | 2090-3138 | |
dc.identifier | http://hdl.handle.net/11336/93905 | |
dc.identifier | 2090-3146 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/4327852 | |
dc.description.abstract | Paecilomyces lilacinus (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 Ca2+, Mg2+, or sorbitol was found to be effective in increasing thermal stability of the protease. PMSF and Hg2+ 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. | |
dc.language | eng | |
dc.publisher | Hindawi Publishing Corporation | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.hindawi.com/journals/btri/2012/369308/ | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1155/2012/369308 | |
dc.rights | https://creativecommons.org/licenses/by/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | Hair Waste | |
dc.subject | Detergent Stable | |
dc.subject | Serine Proteases | |
dc.subject | Keratinolytic Activity | |
dc.subject | Thermostability | |
dc.title | Bioprocessing of “Hair Waste” by Paecilomyces lilacinus as a Source of a Bleach-Stable, Alkaline, and Thermostable Keratinase with Potential Application as a Laundry Detergent Additive: Characterization and Wash Performance Analysis | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |