Evidence map›Paper›PMID 41809600›Full record

ReviewFrontiers in microbiology2026

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

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

Abstract readReview
In one paragraph

Review in Frontiers in microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Yuqing ChuCollege of Medical Engineering, Jining Medical University, Jining, China.
Shan ChuCollege of Medical Engineering, Jining Medical University, Jining, China.
Fengna HuAffiliated Hospital of Jining Medical University, Jining, China.
Mohan HuangCollege of Medical Engineering, Jining Medical University, Jining, China.
Haoran LuCollege of Medical Engineering, Jining Medical University, Jining, China.
Zhiqiao LiuCollege of Medical Engineering, Jining Medical University, Jining, China.
Fenglian ShanAffiliated Hospital of Jining Medical University, Jining, China.
Xiaotang ChenCollege of Medical Engineering, Jining Medical University, Jining, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

biocatalysisdegradation mechanismenzymatic propertiesindustrial applicationskeratinaseprotein engineeringwaste valorization

Identifiers

PMID41809600
PMCPMC12968019

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.