ArticleBiotechnology research international2012
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.
Article in Biotechnology research international, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Comparative Genomics Analysis Reveals the Genomic Basis of S8 Proteases, CAZymes, and Secondary Metabolism Associated with Nematode Biocontrol inInternational journal of molecular sciences · 2026Article
- Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization.Frontiers in microbiology · 2026Review
- In silico and experimental characterization of a new polyextremophilic subtilisin-like protease from3 Biotech · 2024Article
- Transcriptomics Reveals the Mechanism of Purpureocillium lilacinum GZAC18-2JMP in Degrading Keratin Material.Current microbiology · 2024Article
- Microbial enzymes catalyzing keratin degradation: Classification, structure, function.Biotechnology advances · 2020Review
- A new method to evaluate temperature vs. pH activity profiles for biotechnological relevant enzymes.Biotechnology for biofuels · 2017Article
- A Comparative Study of New Aspergillus Strains for Proteolytic Enzymes Production by Solid State Fermentation.Enzyme research · 2016Article
- Whole genome annotation and comparative genomic analyses of bio-control fungus Purpureocillium lilacinum.BMC genomics · 2015Article
- Plant Growth Promotion Activity of Keratinolytic Fungi Growing on a Recalcitrant Waste Known as "Hair Waste".Biotechnology research international · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
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 Ca(2+), Mg(2+), or sorbitol was found to be effective in increasing thermal stability of the protease. PMSF and Hg(2+) 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.
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Registered trials
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