ISSN: 0973-7510

E-ISSN: 2581-690X

Research Article | Open Access
Lindelwa Mpaka , Nonso E. Nnolim and Uchechukwu U. Nwodo
Patho-Biocatalysis Group (PBG), Department of Biotechnology and Biological Sciences, University of Fort Hare, Private Bag X1314, Alice 5700, South Africa.
Article Number: 10474 | © The Author(s). 2025
J Pure Appl Microbiol. 2025;19(3):2001-2012. https://doi.org/10.22207/JPAM.19.3.26
Received: 14 April 2025 | Accepted: 05 June 2025 | Published online: 23 August 2025
Issue online: September 2025
Abstract

The manipulation of keratinolytic determinants provides an avenue for enhancing keratinase output, thereby facilitating the conversion of wasted chicken feathers into valuable products. Thus, this study investigated the keratinolytic determinants expressed by Chryseobacterium proteolyticum during the degradation of chicken feathers. The bacterial genome was sequenced using the Ion GeneStudio™ S5 Prime System, and SPAdes was used to assemble the raw sequences, while Prokka was used to annotate the obtained sequences. The keratinolytic genes were amplified by polymerase chain reaction (PCR). A total of 4.84 Mb bases were generated from the bacterial genome, which yielded thirty-seven contigs ranging between 165 bp and 1242714 bp when assembled by SPAdes. Prokka annotated 4798 genes, of which thirty-eight were identified as keratinolytic enzyme-coding genes. The resA coding for thiol-disulfide oxidoreductase was the most occurring keratinolytic determinant with a proportion of 26.3% (10/38), followed by dap coding for D-aminopeptidase (13.2%; 5/38). PCR revealed that resA exhibited a band size of 646 bp. The successful amplification of the keratinolytic determinants from this potent keratin degrader, C. proteolyticum, confirms its dexterity for keratinolysis and may pave the way for genetic engineering to enhance keratinase output.

Keywords

Keratinase, Chicken Feathers, Disulfide Reductase, Aminopeptidases, Chryseobacterium proteolyticum

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