| dc.creator | Cavello, Ivana Alejandra | |
| dc.creator | Hours, Roque Alberto | |
| dc.creator | Cavalitto, Sebastián Fernando | |
| dc.date | 2012 | |
| dc.date | 2020-09-16T17:03:55Z | |
| dc.date.accessioned | 2023-07-14T21:59:09Z | |
| dc.date.available | 2023-07-14T21:59:09Z | |
| dc.identifier | http://sedici.unlp.edu.ar/handle/10915/104780 | |
| dc.identifier | http://hdl.handle.net/11336/93905 | |
| dc.identifier | https://www.hindawi.com/journals/btri/2012/369308/ | |
| dc.identifier | issn:2090-3146 | |
| dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/7445164 | |
| dc.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. | |
| dc.description | Facultad de Ciencias Exactas | |
| dc.description | Centro de Investigación y Desarrollo en Fermentaciones Industriales | |
| dc.format | application/pdf | |
| dc.language | en | |
| dc.rights | http://creativecommons.org/licenses/by/3.0/ | |
| dc.rights | Creative Commons Attribution 3.0 Unported (CC BY 3.0) | |
| dc.subject | Ciencias Exactas | |
| 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 <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 | |
| dc.type | Articulo | |
| dc.type | Articulo | |
