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- W4320498766 endingPage "e13635" @default.
- W4320498766 startingPage "e13635" @default.
- W4320498766 abstract "In recent times, robust green technological developments have advanced the goal of a circular economy by minimizing waste generation. The study was undertaken to explore the keratinolytic activity of chicken feather-degrading bacteria from South African soil. Isolates coded as SSN-01 and HSN-01 were identified as Bacillus sp. NFH5 and Bacillus sp. FHNM and their sequences were deposited in GenBank, with accession numbers MW165830.1 and MW165831.1, respectively. Extracellular enzyme production and thiol group generation by Bacillus sp. NFH5 peaked at 120 h with 1879.09 ± 88.70 U/mL and 9.49 ± 0.78 mM, respectively. Glutamic acid (4.44%), aspartic acid (3.50%), arginine (3.23%), glycine (2.61%), serine (2.08%), and proline (2.08%) were relatively higher in concentration. Keratinase (KerBAN) activity was highest at pH 8.0 and 90 °C but was inhibited by both EDTA and 1,10-phenanthroline. In addition, the keratinase-encoding gene (kerBAN) accessioned OK033360 had 362 amino acid residues, with molecular weight and theoretical isoelectric point of 39 kDa and 8.81, respectively. Findings from this study highlight the significance of Bacillus sp. NFH5 in the bio-recycling of recalcitrant keratinous wastes to protein hydrolysates – potential dietary supplements for livestock feeds. The properties of KerBAN underscore its application potential in green biotechnological processes." @default.
- W4320498766 created "2023-02-14" @default.
- W4320498766 creator A5031062826 @default.
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- W4320498766 creator A5081428588 @default.
- W4320498766 date "2023-02-01" @default.
- W4320498766 modified "2023-10-05" @default.
- W4320498766 title "Thermoactive metallo-keratinase from Bacillus sp. NFH5: Characterization, structural elucidation, and potential application as detergent additive" @default.
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- W4320498766 doi "https://doi.org/10.1016/j.heliyon.2023.e13635" @default.
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- W4320498766 hasPublicationYear "2023" @default.
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