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Open AccessArticle

Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1

1
SAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Alice 5700, South Africa
2
Applied and Environmental Microbiology Research Group (AEMREG), Department of Biochemistry and Microbiology, University of Fort Hare, Private Bag X1314, Alice 5700, South Africa
*
Author to whom correspondence should be addressed.
Received: 5 June 2020 / Revised: 14 July 2020 / Accepted: 21 July 2020 / Published: 27 August 2020
(This article belongs to the Section Environmental Microbiology)
Keratinases are considerably gaining momentum in green technology because of their endowed robustness and multifaceted application potentials, such as keratinous agro-wastes valorization. Therefore, the production of novel keratinases from relatively nonpathogenic bacteria grown in agro-wastes formulated medium is cost-effective, and also imperative for the sustainability of thriving bioeconomy. In this study, we optimized keratinase production by Bacillus sp. Nnolim-K1 grown in chicken feather formulated medium. The produced keratinase (KerBNK1) was biochemically characterized and also, the keratinase-encoding gene (kerBNK1) was amplified and sequenced. The optimal physicochemical conditions for extracellular keratinase production determined were 0.8% (w/v) xylose, 1.0% (w/v) feather, and 3.0% (v/v) inoculum size, pH 5.0, temperature (25 °C) and agitation speed (150 rpm). The maximum keratinase activity of 1943.43 ± 0.0 U/mL was achieved after 120 h of fermentation. KerBNK1 was optimally active at pH and temperature of 8.0 and 60 °C, respectively; with remarkable pH and thermal stability. KerBNK1 activity was inhibited by ethylenediamine tetra-acetic acid and 1,10-phenanthroline, suggesting a metallo-keratinase. The amplified kerBNK1 showed a band size of 1104 bp and the nucleotide sequence was submitted to the GenBank with accession number MT268133. Bacillus sp. Nnolim-K1 and the keratinase displayed potentials that demand industrial and biotechnological exploitations. View Full-Text
Keywords: Keratinase; chicken feather; biodegradation; thiol group; valorization; bioeconomy; Bacillus sp. Keratinase; chicken feather; biodegradation; thiol group; valorization; bioeconomy; Bacillus sp.
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MDPI and ACS Style

Nnolim, N.E.; Mpaka, L.; Okoh, A.I.; Nwodo, U.U. Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1. Microorganisms 2020, 8, 1304. https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms8091304

AMA Style

Nnolim NE, Mpaka L, Okoh AI, Nwodo UU. Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1. Microorganisms. 2020; 8(9):1304. https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms8091304

Chicago/Turabian Style

Nnolim, Nonso E.; Mpaka, Lindelwa; Okoh, Anthony I.; Nwodo, Uchechukwu U. 2020. "Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1" Microorganisms 8, no. 9: 1304. https://0-doi-org.brum.beds.ac.uk/10.3390/microorganisms8091304

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