ArticleScientific reports2022
Parametrically optimized feather degradation by Bacillus velezensis NCIM 5802 and delineation of keratin hydrolysis by multi-scale analysis for poultry waste management.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 39 citations in OpenAlex.
- Tyrosinase Structural Perturbation and Functional Inhibition by an Ostrich-Derived Keratin-Diospyros lotus Nanobiocomposite: Biochemical Mechanism and Melanoma Cell Response.The protein journal · 2026Article
- Biodegradation of hair waste for keratinase production using Bacillus altitudinis VK-1120 and its application in enzymatic dehairing.Biodegradation · 2026Article
- Alternating magnetic fields enhance growth and co-production of cellulase and protease in Bacillus velezensis fermentation.Archives of microbiology · 2026Article
- Harnessing Bacillus velezensis for enhanced protease biosynthesis: optimization, purification, and kinetic profiling.BMC microbiology · 2026Article
- Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025Article
- Microbial Keratinolysis: Eco-Friendly Valorisation of Keratinous Waste into Functional Peptides.Microorganisms · 2025Review
- Feather Waste Biodegradation and Biostimulant Potential ofInternational journal of molecular sciences · 2025Article
- An update on thermostable keratinases for protein engineering against feather pollutants.Applied microbiology and biotechnology · 2025Review
- Comprehensive biochemical, molecular and structural characterization of subtilisin with fibrinolytic potential in bioprocessing.Bioresources and bioprocessing · 2025Article
- Current Understanding of Feather Keratin and Keratinase and Their Applications in Biotechnology.Biochemistry research international · 2025Review
- Microbial production of keratinase fromHeliyon · 2024Article
- Article
- Biodegradation of Keratin Waste by Bacillus velezensis HFS_F2 through Optimized Keratinase Production Medium.Current microbiology · 2024Article
- Response surface methodology based optimization of keratinase fromSaudi journal of biological sciences · 2023Article
- Synthesis and characterization of keratinase laden green synthesized silver nanoparticles for valorization of feather keratin.Scientific reports · 2023Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enormous amounts of keratinaceous waste make a significant and unexploited protein reserve that can be utilized through bioconversion into high-value products using microbial keratinases. This study was intended to assess the keratinase production from a newly isolated B. velezensis NCIM 5802 that can proficiently hydrolyze chicken feathers. Incubation parameters used to produce keratinase enzyme were optimized through the Response Surface Methodology (RSM) with chicken feathers as substrate. Optimization elevated the keratinase production and feather degradation by 4.92-folds (109.7 U/mL) and 2.5 folds (95.8%), respectively. Time-course profile revealed a direct correlation among bacterial growth, feather degradation, keratinase production and amino acid generation. Biochemical properties of the keratinase were evaluated, where it showed optimal activity at 60 °C and pH 10.0. The keratinase was inhibited by EDTA and PMSF, indicating it to be a serine-metalloprotease. Zymography revealed the presence of four distinct keratinases (Mr ~ 100, 62.5, 36.5 and 25 kDa) indicating its multiple forms. NMR and mass spectroscopic studies confirmed the presence of 18 free amino acids in the feather hydrolysates. Changes in feather keratin brought about by the keratinase action were studied by X-ray diffraction (XRD) and spectroscopic (FTIR, Raman) analyses, which showed a decrease in the total crystallinity index (TCI) (1.00-0.63) and confirmed the degradation of its crystalline domain. Scanning electron microscopy (SEM) revealed the sequential structural changes occurring in the feather keratin during degradation. Present study explored the use of keratinolytic potential of the newly isolated B. velezensis NCIM 5802 in chicken feather degradation and also, unraveled the underlying keratin hydrolysis mechanism through various analyses.
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