ReviewBiotechnology advances2020
Microbial enzymes catalyzing keratin degradation: Classification, structure, function.
Review in Biotechnology advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
69 citing papers in PubMed, 256 citations in OpenAlex.
- Seeking soil microbial degraders and enzymatic genes for efficient biomass recycling.Applied biochemistry and biotechnology · 2026Article
- Production, biochemical characterization, and kinetic/thermodynamic analysis of a novel keratinase from Bacillus sp. MSGU2024.Biotechnology letters · 2026Article
- Reengineering a thermostable keratinase past the boiling point.Applied and environmental microbiology · 2026Article
- Development and Field Evaluation of a Microbially-Inoculated Feather-Straw-Lignite Compost Material for the Reclamation of Post-Mining Soils.Materials (Basel, Switzerland) · 2026Article
- Integrated multiomics reveals starvation-driven keratin degradation and persistence iniScience · 2026Article
- Fermented Gallus gallus foot keratin-bone composites as peptide-mineral concentrate for aquafeed: ratio-dependent proximate compositional data.BMC research notes · 2026Article
- Integrated Transcriptomic and Proteomic Analyses Uncover the Mechanisms of Keratin Degradation inBiology · 2026Article
- Regulation of Keratin Chemical Modifications: Potential Molecular Mechanisms in Proliferative Diseases.International journal of molecular sciences · 2026Review
- Ultrasound-Assisted alkaline hydrolysis of feather keratin using a cup horn sonoreactor.Ultrasonics sonochemistry · 2026Article
- Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization.Frontiers in microbiology · 2026Review
- 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
- Harnessing Microbial Consortia for Efficient Keratinous Biomass Biotransformation.International journal of molecular sciences · 2025Review
- A Highly Active Keratinase fromBiomolecules · 2025Article
- Microbial Keratinolysis: Eco-Friendly Valorisation of Keratinous Waste into Functional Peptides.Microorganisms · 2025Review
- Bioconversion of Feather and Production of Alkaline Protease for Detergent and Dehairing Applications.Applied biochemistry and biotechnology · 2025Article
- Keratinase and its diverse applications.3 Biotech · 2025Review
- Comparative analysis of pre-treatment strategies and bacterial strain efficiency for improvement of feather hydrolysis.Microbial cell factories · 2025Article
- Keratinous bioresources: their generation, microbial degradation, and value enhancement for biotechnological applications.World journal of microbiology & biotechnology · 2025Review
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Keratin is an insoluble and protein-rich epidermal material found in e.g. feather, wool, hair. It is produced in substantial amounts as co-product from poultry processing plants and pig slaughterhouses. Keratin is packed by disulfide bonds and hydrogen bonds. Based on the secondary structure, keratin can be classified into α-keratin and β-keratin. Keratinases (EC 3.4.-.- peptide hydrolases) have major potential to degrade keratin for sustainable recycling of the protein and amino acids. Currently, the known keratinolytic enzymes belong to at least 14 different protease families: S1, S8, S9, S10, S16, M3, M4, M14, M16, M28, M32, M36, M38, M55 (MEROPS database). The various keratinolytic enzymes act via endo-attack (proteases in families S1, S8, S16, M4, M16, M36), exo-attack (proteases in families S9, S10, M14, M28, M38, M55) or by action only on oligopeptides (proteases in families M3, M32), respectively. Other enzymes, particularly disulfide reductases, also play a key role in keratin degradation as they catalyze the breakage of disulfide bonds for better keratinase catalysis. This review aims to contribute an overview of keratin biomass as an enzyme substrate and a systematic analysis of currently sequenced keratinolytic enzymes and their classification and reaction mechanisms. We also summarize and discuss keratinase assays, available keratinase structures and finally examine the available data on uses of keratinases in practical biorefinery protein upcycling applications.
Indexed as
Identifiers
What OpenQuestion holds
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.