ReviewApplied microbiology and biotechnology2025
An update on thermostable keratinases for protein engineering against feather pollutants.
Review in Applied microbiology and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Combined computational, rational, and empirical design of boiling-resistant keratinase.Applied and environmental microbiology · 2026Article
- Functional identification of a feather-degrading thermitase-like S8 serine protease fromFrontiers in microbiology · 2026Article
- Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization.Frontiers in microbiology · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Every year, the poultry business worldwide produces at least 8.5 billion tonnes of chicken feathers, making it one of the major landfill pollutants in the world. Biodegradation and recycling of native feathers is difficult due to the presence of numerous disulfide linkages in the feather's major constituent, keratin. Denaturation of such recalcitrant protein is thermodynamically favored at high temperatures. Therefore, the lookout for the enzymes that degrade keratin (keratinases) from thermophilic bacteria resulted in the identification of thermostable enzymes favoring feather degradation at high temperatures. This review presents a comprehensive analysis of the biochemical properties and structural attributes of thermostable keratinases, emphasizing their catalytic mechanisms, stability at high temperatures, and substrate specificity. Our exploration of structural features enables us to understand the molecular architecture of these enzymes for protein engineering that might enhance the keratinolytic activity and thermostability further. As the field of protein engineering advances, there exists a pressing requirement for integration of structural data with pragmatic engineering applications. Our review addresses for the first time the detailed structural aspects of thermostable bacterial keratinolytic enzymes that will facilitate the development of modified keratinases through protein engineering for a broad range of industrial applications, such as in the production of biofuels, leather processing, and waste management. KEYPOINTS: • Efficient eco-friendly bioremediation of feather landfill pollutant using thermophilic keratinases. • Detailed structural and biochemical aspects of different thermophilic bacterial keratinases. • Combinations of thermostable keratinases for the enhanced feather degradation process.
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Registered trials
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