# Keratinases: microbial sources, mechanisms, and industrial applications in waste valorization

**Authors:** Yuqing Chu, Shan Chu, Fengna Hu, Mohan Huang, Haoran Lu, Zhiqiao Liu, Fenglian Shan, Xiaotang Chen

PMC · DOI: 10.3389/fmicb.2026.1793191 · Frontiers in Microbiology · 2026-02-23

## TL;DR

This paper reviews keratinase enzymes that break down tough keratin waste, exploring their sources, mechanisms, and potential industrial uses for sustainable waste management.

## Contribution

The paper provides a comprehensive review of keratinase properties, sources, and applications, highlighting challenges and future directions for industrial use.

## Key findings

- Keratinase can effectively degrade keratinous waste like feathers and horns.
- Applications include biogas production, bioactive peptides, and bioplastic manufacturing.
- Challenges include low enzyme expression and stability under industrial conditions.

## Abstract

Keratinous waste, a major by-product of agriculture and animal husbandry, is produced in massive quantities and is notoriously recalcitrant to degradation. With the expansion of the poultry and livestock industries, keratinous waste accumulation (e.g., feathers, hooves, and horns) has become a pressing environmental concern. Keratin’s highly cross-linked disulfide bond structure is resistant to breakdown by common proteases. Keratinase, a specialized protease capable of specifically degrading keratin, has emerges as a pivotal tool for the valorization of keratinous waste, demonstrating significant potential in waste management and resource recovery. This review systematically summarizes the enzymatic properties, mechanisms of action, and microbial sources of keratinases. It elaborates on innovative keratinase applications in waste valorization (including biogas production, the generation of bioactive peptides and amino acid feedstocks, and bioplastic manufacturing) and green industries (including leather and textile processing), as well as in the pharmaceutical, cosmetic, and detergent sectors. This review provides an in-depth discussion of the major challenges hindering industrial-scale keratinase application, including low heterologous expression efficiency and insufficient stability under industrial conditions. Finally, it outlines future research directions, encompassing protein engineering, artificial intelligence (AI)-assisted design, and multi-enzyme synergistic catalysis systems, aiming to offer forward-looking theoretical insights for advanced keratinase development and industrial application.

## Full-text entities

- **Genes:** FGG (fibrinogen gamma chain) [NCBI Gene 395837] {aka fibrinogen, gamma-fibrinogen}, Serine protease [NCBI Gene 29404860], lipase [NCBI Gene 29407803], LOC396479 (keratin) [NCBI Gene 396479]
- **Diseases:** Acne (MESH:D000152), CUPP (MESH:C565529), TDS (MESH:D018250), CLEAs (MESH:C537866), thrombus (MESH:D013927), PPC (OMIM:211750), prion disease (MESH:D017096), COD (MESH:D000860), inflammation (MESH:D007249), tinea corporis (MESH:D014005), HL (MESH:C538324), skin diseases (MESH:D012871), onychomycosis (MESH:D014009)
- **Chemicals:** thioglycolate (MESH:D013864), citric acid (MESH:D019343), glutathione (MESH:D005978), cysteine (MESH:D003545), lipids (MESH:D008055), bioplastic (MESH:D001704), ammonium sulfate (MESH:D000645), PB (MESH:D007854), hydrogen (MESH:D006859), Sulfite (MESH:D013447), Dichloroisocyanuric acid (MESH:C011765), formaldehyde (MESH:D005557), calcium (MESH:D002118), heavy metal (MESH:D019216), lime (MESH:C016538), terbinafine (MESH:D000077291), AgNPs (-), alpha-ketoglutarate (MESH:D007656), disulfide (MESH:D004220), glycerol (MESH:D005990), sulfhydryl (MESH:D013438), PMSF (MESH:D010664), amino acid (MESH:D000596), urea (MESH:D014508), chlorine (MESH:D002713), starch (MESH:D013213), succinyl-CoA (MESH:C012046), peptides (MESH:D010455), Silver (MESH:D012834), DTT (MESH:D004229), metal (MESH:D008670), salt (MESH:D012492), lanolin (MESH:D007809), acids (MESH:D000143), sodium sulfite (MESH:C025026), sulfide (MESH:D013440), sulfate (MESH:D013431), oxygen (MESH:D010100), graphene oxide (MESH:C000628730), lactic acid (MESH:D019344), beta-cyclodextrin (MESH:C031215), nitrogen (MESH:D009584), EDTA (MESH:D004492), methane (MESH:D008697), polymer (MESH:D011108), carbon (MESH:D002244)
- **Species:** Fusarium oxysporum (species) [taxon 5507], Stenotrophomonas sp. (species) [taxon 69392], Bos taurus (bovine, species) [taxon 9913], Pseudomonas (RNA similarity group I, genus) [taxon 286], Gallus gallus (bantam, species) [taxon 9031], Streptomyces pactum (species) [taxon 68249], Arthrobacter sp. (species) [taxon 1667], Bacillus subtilis subsp. subtilis (subspecies) [taxon 135461], Escherichia coli BL21(DE3) (strain) [taxon 469008], Pseudogymnoascus pannorum (species) [taxon 79858], Penicillium oxalicum (species) [taxon 69781], Homo sapiens (human, species) [taxon 9606], Aspergillus clavatus (species) [taxon 5057], Nectria haematococca [taxon 140110], Komagataella pastoris (species) [taxon 4922], Bacillus licheniformis (species) [taxon 1402], Parastagonospora nodorum (species) [taxon 13684], Ovis aries (domestic sheep, species) [taxon 9940], Sus scrofa (pig, species) [taxon 9823], Bacillus zhangzhouensis (species) [taxon 1178540], Bacillus sp. (in: firmicutes) (species) [taxon 1409], Chryseobacterium (genus) [taxon 59732], Lysinibacillus (genus) [taxon 400634], Bacillus subtilis (species) [taxon 1423], Escherichia coli (E. coli, species) [taxon 562], Thermoactinomyces vulgaris (species) [taxon 2026], Purpureocillium lilacinum (species) [taxon 33203], Geoglobus acetivorans (species) [taxon 565033]
- **Mutations:** C) for 12-24, N122, N122Y

## Full text

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## Figures

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## References

101 references — full list in the complete paper: https://tomesphere.com/paper/PMC12968019/full.md

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Source: https://tomesphere.com/paper/PMC12968019