Evidence map›Paper›PMID 40308531›Full record

ReviewBiochemistry research international2025

Current Understanding of Feather Keratin and Keratinase and Their Applications in Biotechnology.

Thanakorn Moktip, Lakha Salaipeth, Ana Eusebio Cope, Mohammad J Taherzadeh, Takashi Watanabe, Paripok Phitsuwan

Abstract readReview
In one paragraph

Review in Biochemistry research international, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Reengineering a thermostable keratinase past the boiling point.Applied and environmental microbiology · 2026
    Article
  3. Review
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

6 authors.

Thanakorn MoktipLigniTech-Lignin Technology Research Group, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand.ORCID https://orcid.org/0009-0007-6820-3057
Lakha SalaipethLigniTech-Lignin Technology Research Group, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand.ORCID https://orcid.org/0000-0002-2888-8828
Ana Eusebio CopeFuture Genetic Resources Cluster, Rice Breeding Innovation Platform, IRRI, Los Banos, Philippines.
Mohammad J TaherzadehSwedish Centre for Resource Recovery, University of Borås, Borås 50190, Sweden.ORCID https://orcid.org/0000-0003-4887-2433
Takashi WatanabeResearch Institute for Sustainable Humanosphere, Kyoto University, Kyoto 611-0011, Japan.ORCID https://orcid.org/0000-0003-0220-4157
Paripok PhitsuwanLigniTech-Lignin Technology Research Group, School of Bioresources and Technology, King Mongkut's University of Technology Thonburi, Bangkuntien, Bangkok 10150, Thailand.ORCID https://orcid.org/0000-0002-2875-1530

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The food industry generates substantial keratin waste, particularly chicken feathers, which are rich in amino acids and essential nutrients. However, the insolubility of keratin presents a significant challenge to its conversion. Keratinase, an enzyme produced by certain fungi and bacteria, offers a promising solution by degrading feather keratin into amino acids and soluble proteins. Among these, bacterial keratinase is notable for its superior stability and activity, although its production remains constrained, necessitating continued research to identify efficient microbial strains. Keratin-derived hydrolyzates, recognized for their biological and immunological properties, have garnered significant research interest. This review examines the structural characteristics of chicken feather keratin, its resistance to conventional proteases, and advances in keratinase production and purification techniques. Additionally, the keratin degradation mechanism and the adoption of environmentally friendly technologies for managing feather waste are explored. Finally, the review highlights the potential applications of keratinase across diverse industries, including animal feed and cosmetics.

Indexed as

bioactive peptidechicken featherkeratinasekeratin degradationprotease

Identifiers

PMID40308531
PMCPMC12041636

What OpenQuestion 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 OpenQuestion graph.