ArticleApplied microbiology and biotechnology2015
Genome and secretome analyses provide insights into keratin decomposition by novel proteases from the non-pathogenic fungus Onygena corvina.
Article in Applied microbiology and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 92 citations in OpenAlex.
- Integrated Transcriptomic and Proteomic Analyses Uncover the Mechanisms of Keratin Degradation inBiology · 2026Article
- Proteolytic and non-proteolytic mechanisms of keratin degradation inApplied and environmental microbiology · 2025Article
- Improved genome assembly of Onygena corvina, a keratin-degrading fungus.BMC research notes · 2025Article
- Efficient Mining and Characterization of Two Novel Keratinases from Metagenomic Database.Biomolecules · 2025Article
- Microbial Keratinolysis: Eco-Friendly Valorisation of Keratinous Waste into Functional Peptides.Microorganisms · 2025Review
- Keratinous bioresources: their generation, microbial degradation, and value enhancement for biotechnological applications.World journal of microbiology & biotechnology · 2025Review
- Transcriptomic and proteomic insights into feather keratin degradation byFrontiers in microbiology · 2025Article
- Comprehensive insights into the mechanism of keratin degradation and exploitation of keratinase to enhance the bioaccessibility of soybean protein.Biotechnology for biofuels and bioproducts · 2023Article
- Insights into the keratin efficient degradation mechanism mediated by Bacillus sp. CN2 based on integrating functional degradomics.Biotechnology for biofuels and bioproducts · 2023Article
- 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
- Keratinases as Versatile Enzymatic Tools for Sustainable Development.Biomolecules · 2021Review
- Article
- Comparative Genomics Analysis of Keratin-DegradingMicroorganisms · 2021Article
- A highly efficient protein degradation system in Bacillus sp. CN2: a functional-degradomics study.Applied microbiology and biotechnology · 2021Article
- Microbial enzymes catalyzing keratin degradation: Classification, structure, function.Biotechnology advances · 2020Review
- Enzyme Bioprospection of Marine-Derived Actinobacteria from the Chilean Coast and New Insight in the Mechanism of Keratin Degradation inMarine drugs · 2020Article
- Enzymatic removal of dags from livestock: an agricultural application of enzyme technology.Applied microbiology and biotechnology · 2020Review
- An alternative for proteinase K-heat-sensitive protease from fungus Onygena corvina for biotechnology: cloning, engineering, expression, characterization and special application for protein sequencing.Microbial cell factories · 2020Article
- Novel keratinolytic enzymes, discovered from a talented and efficient bacterial keratin degrader.Scientific reports · 2020Article
- In vitro synergistic effects of three enzymes from3 Biotech · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poultry processing plants and slaughterhouses produce huge quantities of feathers and hair/bristle waste annually. These keratinaceous wastes are highly resistant to degradation. Onygena corvina, a non-pathogenic fungus, grows specifically on feathers, hooves, horn, and hair in nature. Hence, the proteases secreted by O. corvina are interesting in view of their potential relevance for industrial decomposition of keratinaceous wastes. We sequenced and assembled the genome of O. corvina and used a method called peptide pattern recognition to identify 73 different proteases. Comparative genome analysis of proteases in keratin-degrading and non-keratin-degrading fungi indicated that 18 putative secreted proteases from four protease families (M36, M35, M43, and S8) may be responsible for keratin decomposition. Twelve of the 18 predicted protease genes could be amplified from O. corvina grown on keratinaceous materials and were transformed into Pichia pastoris. One of the recombinant proteases belonging to the S8 family showed high keratin-degrading activity. Furthermore, 29 different proteases were identified by mass spectrometry in the culture broth of O. corvina grown on feathers and bristle. The culture broth was fractionated by ion exchange chromatography to isolate active fractions with five novel proteases belonging to three protease families (S8, M28, and M3). Enzyme blends composed of three of these five proteases, one from each family, showed high degree of degradation of keratin in vitro. A blend of novel proteases, such as those we discovered, could possibly find a use for degrading keratinaceous wastes and provide proteins, peptides, and amino acids as valuable ingredients for animal feed.
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