Evidence map›Paper›PMID 40696551›Full record

ArticleProtein and peptide letters2025

Unlocking the Keratinolytic Potential of

Hira Batool, Beenish Maqsood, Hira Muzzamal, Hamama Islam Butt, Roquyya Gul, Farooq Latif, Mahjabeen Saleem

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Article in Protein and peptide letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Hira BatoolSchool of Biochemistry and Biotechnology, University of the Punjab, Lahore-54590, Pakistan.
Beenish MaqsoodSchool of Biochemistry and Biotechnology, University of the Punjab, Lahore-54590, Pakistan.
Hira MuzzamalSchool of Medical Lab Technology, Minhaj University Lahore, Lahore-54770, Pakistan.
Hamama Islam ButtSchool of Medical Lab Technology, Minhaj University Lahore, Lahore-54770, Pakistan.
Roquyya GulFaculty of Life Sciences, Gulab Devi Educational Complex, Lahore, Pakistan.
Farooq LatifSchool of Biochemistry, Minhaj University Lahore, Lahore-54770, Pakistan.
Mahjabeen SaleemSchool of Biochemistry and Biotechnology, University of the Punjab, Lahore-54590, Pakistan.ORCID 0000-0001-8944-8714

Funding

Higher Education Commission (HEC) of Pakistan 213-59672-2BM2-022
6 · The paper itself

Abstract

backgroundKeratinases have an established role in degrading highly stable and insoluble fibers of keratin proteins, which are otherwise difficult to be hydrolyzed by conventional proteases. Keratinases find promising application in degrading poultry waste to valuable products. Moreover, their role in cosmetics, detergents, agriculture and the leather industry is well recognized.

objectivesIn this study, the keratinase gene from locally isolated

methods1300 bp amplified gene from

resultsThe blast analysis and homologous sequences in the NCBI database established a close link to Brevibacillus agri. The highest expression from transformed E. coli BL21 was achieved with 0.8 mM IPTG following 6 hours of induction. The resulting recombinant keratinase (KerH), purified by Ni-affinity chromatography, possessed 283 U/mg specific activity and displayed ~45 kDa band on SDS-PAGE and zymogram. Secondary structure analysis and active site prediction was performed computationally. Considering the extensive applications of keratinase, KerH was found to be useful in dehairing animal skin surfaces without any damage. The encapsulated KerH possessed improved stability and better compatibility with commercial detergents. It efficiently removed blood, turmeric, strawberry, and egg yolk stains from the fabric. Furthermore, KerH significantly degraded the poultry feathers and provided a protein hydrolysate that helped in converting damaged, dull and curly hair into healthier, shiny and straightened hair. DISCUSSION: These key findings highlight that KerH is a robust keratinase with significant potential as an environmental-friendly alternative to the prevailing harsh chemical treatments in various industries. Encapsulation enhanced its suitability by improving its stability and shelf-life. Its broader substrate specificity, stability and application in detergents and cosmetics underline its commercial importance.

conclusionThe recombinant KerH from Brevibacillus agri can be considered as a valuable microbial keratinase that can be used as an alternative to the eco hazardous chemicals used in commercial applications of feather degradation, hair protein treatment, feather keratin hydrolysate production and hide dehairing.

Indexed as

Bacterial ProteinsBrevibacillusKeratinsPeptide HydrolasesAnimalsCloning, MolecularEscherichia coliRecombinant ProteinsBacterial ProteinskeratinaseKeratinsPeptide HydrolasesRecombinant ProteinsBrevibacillus agricloning and expressiondehairingkeratinaseprotein hydrolysate.purification

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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.