ArticleWorld journal of microbiology & biotechnology2011
Biodegradation of feather waste by extracellular keratinases and gelatinases from Bacillus spp.
Article in World journal of microbiology & biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 111 citations in OpenAlex.
- Composting Poultry Feathers with KeratinolyticMaterials (Basel, Switzerland) · 2025Article
- New Bacillus paralicheniformis strain with high proteolytic and keratinolytic activity.Scientific reports · 2024Article
- New Bacillus paralicheniformis strain with high proteolytic and keratinolytic activity.Scientific reports · 2024Article
- Article
- Screening ofHeliyon · 2024Article
- High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.PloS one · 2024Article
- Synthesis and characterization of keratinase laden green synthesized silver nanoparticles for valorization of feather keratin.Scientific reports · 2023Article
- Biochemical and molecular characterization of novel keratinolytic protease fromFrontiers in microbiology · 2023Article
- Microbial proteases and their applications.Frontiers in microbiology · 2023Review
- Parametrically optimized feather degradation by Bacillus velezensis NCIM 5802 and delineation of keratin hydrolysis by multi-scale analysis for poultry waste management.Scientific reports · 2022Article
- Overproduction of a thermo-stable halo-alkaline protease on agro-waste-based optimized medium through alternate combinatorial random mutagenesis ofBiotechnology reports (Amsterdam, Netherlands) · 2022Article
- Enhanced keratinase production by3 Biotech · 2022Article
- Isolation ofBiology · 2022Article
- Biodegradation of feather waste by keratinase produced from newly isolatedJournal, genetic engineering & biotechnology · 2018Article
- New keratinolytic bacteria in valorization of chicken feather waste.AMB Express · 2018Article
- Production, partial optimization and characterization of keratinase enzyme by Arthrobacter sp. NFH5 isolated from soil samples.AMB Express · 2017Article
- Biodegradation and extracellular enzymatic activities of Pseudomonas aeruginosa strain GF31 on β-cypermethrin.Environmental science and pollution research international · 2015Article
- Extracellular peptidases from Deinococcus radiodurans.Extremophiles : life under extreme conditions · 2015Article
- Feather keratin hydrolysates obtained from microbial keratinases: effect on hair fiber.BMC biotechnology · 2013Article
- Keratinases and sulfide from Bacillus subtilis SLC to recycle feather waste.World journal of microbiology & biotechnology · 2012Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, three feather degrading bacterial strains were isolated from agroindustrial residues from a Brazilian poultry farm. Three Gram-positive, spore-forming, rod-shaped bacteria and were identified as B. subtilis 1271, B. licheniformis 1269 and B. cereus 1268 using biochemical, physiologic and molecular methods. These Bacillus spp. strains grew and produced keratinases and peptidases using chicken feather as the sole source of nitrogen and carbon. B. subtilis 1271 degraded feathers completely after 7 days at room temperature and produced the highest levels of keratinase (446 U ml(-1)). Feather hydrolysis resulted in the production of serine, glycine, glutamic acid, valine and leucine as the major amino acids. Enzymography and zymography analyses demonstrated that enzymatic extracts from the Bacillus spp. effectively degraded keratin and gelatin substrates as well as, casein, hemoglobin and bovine serum albumin. Zymography showed that B. subtilis 1271 and B. licheniformis 1269 produced peptidases and keratinases in the 15-140 kDa range, and B. cereus produced a keratinase of ~200 kDa using feathers as the carbon and nitrogen source in culture medium. All peptidases and keratinases observed were inhibited by the serine specific peptidase inhibitor phenylmethylsulfonyl fluoride (PMSF). The optimum assay conditions of temperature and pH for keratinase activity were 40-50°C and pH 10.0 for all strains. For gelatinases the best temperature and pH ranges were 50-70°C and pH 7.0-11. These isolates have potential for the biodegradation of feather wastes and production of proteolytic enzymes using feather as a cheap and eco-friendly substrate.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.