ArticleScientific reports2017
The discovery of novel heat-stable keratinases from Meiothermus taiwanensis WR-220 and other extremophiles.
Article in Scientific reports, 2017. 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, 75 citations in OpenAlex.
- Targeted pathway mining reveals novel modified hexapeptides from the demiguisin family.Communications chemistry · 2026Article
- Functional identification of a feather-degrading thermitase-like S8 serine protease fromFrontiers in microbiology · 2026Article
- 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
- An update on thermostable keratinases for protein engineering against feather pollutants.Applied microbiology and biotechnology · 2025Review
- Current Understanding of Feather Keratin and Keratinase and Their Applications in Biotechnology.Biochemistry research international · 2025Review
- Structural Catalytic Core in Subtilisin-like Proteins and Its Comparison to Trypsin-like Serine Proteases and Alpha/Beta-Hydrolases.International journal of molecular sciences · 2024Review
- Isolation, Selection, and Identification of Keratinolytic Bacteria for Green Management of Keratin Waste.Molecules (Basel, Switzerland) · 2024Article
- Microbial production of keratinase fromHeliyon · 2024Article
- High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.PloS one · 2024Article
- Identification of molecular interactions of pesticides with keratinase for their potential to inhibit keratin biodegradation.In silico pharmacology · 2024Article
- 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
- Discrimination of psychrophilic enzymes using machine learning algorithms with amino acid composition descriptor.Frontiers in microbiology · 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
- High-efficiency decomposition of eggshell membrane by a keratinase from Meiothermus taiwanensis.Scientific reports · 2022Article
- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
- Chicken Feather Waste Valorization Into Nutritive Protein Hydrolysate: Role of Novel Thermostable Keratinase FromFrontiers in microbiology · 2022Article
- Keratinases as Versatile Enzymatic Tools for Sustainable Development.Biomolecules · 2021Review
- Autogenous Cross-Linking of Recycled Keratin from Poultry-Feather Waste to Hydrogels for Plant-Growth Media.Polymers · 2021Article
- Feather protein lysate optimization and feather meal formation using YNDH protease with keratinolytic activity afterward enzyme partial purification and characterization.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Billions of tons of keratin bio-wastes are generated by poultry industry annually but discarded that result in serious environmental pollution. Keratinase is a broad spectrum protease with the unique ability to degrade keratin, providing an eco-friendly way to convert keratin wastes to valuable amino acids. In this report, a feather-degrading thermophilic bacterium, Meiothermus taiwanensis WR-220, was investigated due to its ability to apparently complete feather decay at 65 °C in two days. By genomics, proteomics, and biochemical approaches, the extracellular heat-stable keratinase (MtaKer) from M. taiwanensis WR-220 was identified. The recombinant MtaKer (rMtaKer) possesses keratinolytic activities at temperatures ranging from 25 to 75 °C and pH from 4 to 11, with a maximum keratinolytic activity at 65 °C and pH 10. The phylogenetic and structural analysis revealed that MtaKer shares low sequence identity but high structural similarity with known keratinases. Accordingly, our findings have enabled the discovery of more keratinases from other extremophiles, Thermus and Deinococcus. Proteins encoded in the extremophiles shall be evolved to be functional in the extreme conditions. Hence, our study expands the current boundary of hunting keratinases that can tolerate extreme conditions for keratin wastes biorecycle and other industrial applications.
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