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dc.contributor.author
Cavello, Ivana Alejandra
dc.contributor.author
Cavalitto, Sebastian Fernando
dc.contributor.author
Hours, Roque Alberto
dc.date.available
2019-09-23T14:57:09Z
dc.date.issued
2012-07
dc.identifier.citation
Cavello, Ivana Alejandra; Cavalitto, Sebastian Fernando; Hours, Roque Alberto; Biodegradation of a keratin waste and the concomitant production of detergent stable serine proteases from Paecilomyces lilacinus; Springer; Applied Biochemistry And Biotechnology; 167; 5; 7-2012; 945-958
dc.identifier.issn
0273-2289
dc.identifier.uri
http://hdl.handle.net/11336/84107
dc.description.abstract
Paecilomyces lilacinus (LPS 876) efficiently degraded keratin in chicken feather during submerged cultivation producing extracellular proteases. Characterization of crude protease activity was done including its compatibility in commercial detergents. Optimum pH and temperature were 10.0 and 60 °C, respectively. Protease activity was enhanced by Ca2+ but was strongly inhibited by PMSF and by Hg2+ suggesting the presence of thiol-dependent serine proteases. The crude protease showed extreme stability toward non-ionic (Tween 20, Tween 85, and Triton X-100) and anionic (SDS) surfactants, and relative stability toward oxidizing agent (H2O2 and sodium perborate). In addition, it showed excellent stability and compatibility with various solid and liquid commercial detergents from 30 to 50 °C. The enzyme preparation retained more than 95% of its initial activity with solid detergents (Ariel™ and Drive™) and 97% of its original activity with a liquid detergent (Ace™) after pre-incubation at 40 °C. The protective effect of polyols (propylene glycol, PEG 4000, and glycerol) on the heat inactivation was also examined and the best results were obtained with glycerol from 50 to 60 °C. Considering its promising properties, P. lilacinus enzymatic preparation may be considered as a candidate for use in biotechnological processes (i.e., as detergent additive) and in the processing of keratinous wastes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Paecilomyces Lilacinus
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Alkaline Serine Proteases
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Keratinolytic Activity
dc.subject
Chicken Feather
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Detergent Stable
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Bioprocesamiento Tecnológico, Biocatálisis, Fermentación
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Biotecnología Industrial
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INGENIERÍAS Y TECNOLOGÍAS
dc.title
Biodegradation of a keratin waste and the concomitant production of detergent stable serine proteases from Paecilomyces lilacinus
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-04-26T18:20:55Z
dc.identifier.eissn
1559-0291
dc.journal.volume
167
dc.journal.number
5
dc.journal.pagination
945-958
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Nueva York
dc.description.fil
Fil: Cavello, Ivana Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
dc.description.fil
Fil: Cavalitto, Sebastian Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
dc.description.fil
Fil: Hours, Roque Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Fermentaciones Industriales. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Fermentaciones Industriales; Argentina
dc.journal.title
Applied Biochemistry And Biotechnology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s12010-012-9650-7
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12010-012-9650-7
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