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Thermoactive metallo-keratinase from sp. NFH5: Characterization, structural elucidation, and potential application as detergent additive.

作者信息

Kokwe Lupho, Nnolim Nonso E, Ezeogu Lewis I, Sithole Bruce, Nwodo Uchechukwu U

机构信息

SAMRC Microbial Water Quality Monitoring Centre, University of Fort Hare, Alice, Private Bag X1314, 5700, South Africa.

Applied and Environmental Microbiology Research Group (AEMREG), Department of Biochemistry and Microbiology, University of Fort Hare, Alice, 5700, South Africa.

出版信息

Heliyon. 2023 Feb 13;9(2):e13635. doi: 10.1016/j.heliyon.2023.e13635. eCollection 2023 Feb.


DOI:10.1016/j.heliyon.2023.e13635
PMID:36852054
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9957710/
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 sp. NFH5 and 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 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 () 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 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.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/924bf3dcbf69/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/18d38c247c7f/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/383c2b6731de/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/0002b6405095/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/429f37c3f2a2/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/ee01fdccae6a/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/924bf3dcbf69/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/18d38c247c7f/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/383c2b6731de/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/0002b6405095/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/429f37c3f2a2/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/ee01fdccae6a/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9e8/9957710/924bf3dcbf69/gr6.jpg

相似文献

[1]
Thermoactive metallo-keratinase from sp. NFH5: Characterization, structural elucidation, and potential application as detergent additive.

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[2]
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[3]
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[4]
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[7]
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[10]
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引用本文的文献

[1]
Sustainable exploitation of high-protein feather waste for green production of cold-adapted and detergent-stable keratinase by Penicillium oxalicum AUMC 15084.

World J Microbiol Biotechnol. 2025-6-5

[2]
An update on thermostable keratinases for protein engineering against feather pollutants.

Appl Microbiol Biotechnol. 2025-3-25

[3]
High keratinase and other types of hydrolase activity of the new strain of Bacillus paralicheniformis.

PLoS One. 2024

[4]
New Bacillus paralicheniformis strain with high proteolytic and keratinolytic activity.

Sci Rep. 2024-9-30

[5]
Partial purification and characterization of protease extracted from .

Heliyon. 2024-2-27

[6]
Strawberry Protease as a Laundry Detergent Additive Candidate: Immobilization, Compatibility Study with Detergent Ingredients, and Washing Performance Test.

Glob Chall. 2023-11-24

[7]
Metal Nanomaterials and Hydrolytic Enzyme-Based Formulations for Improved Antifungal Activity.

Int J Mol Sci. 2023-7-12

本文引用的文献

[1]
Production of surfactant-stable keratinase from Bacillus cereus YQ15 and its application as detergent additive.

BMC Biotechnol. 2022-9-8

[2]
Production and characterization of a new detergent-stable keratinase expressed by Pedobacter sp. 3.14.7, a novel Antarctic psychrotolerant keratin-degrading bacterium.

J Genet Eng Biotechnol. 2022-5-25

[3]
Novel Feather Degrading Keratinases from Group: Biochemical, Genetic and Bioinformatics Analysis.

Microorganisms. 2022-1-1

[4]
Keratinases as Versatile Enzymatic Tools for Sustainable Development.

Biomolecules. 2021-12-18

[5]
keratinase liberated essential and nonessential amino acids from chicken feather degradation.

Environ Technol. 2023-1

[6]
Mutations in the regulatory regions result in increased streptomycin resistance and keratinase synthesis in Bacillus thuringiensis.

Arch Microbiol. 2021-11

[7]
Structure, Application, and Biochemistry of Microbial Keratinases.

Front Microbiol. 2021-6-23

[8]
Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs.

Sci Rep. 2021-6-7

[9]
Comparative Genomics Analysis of Keratin-Degrading Species Reveals Their Keratinolytic Potential for Secondary Metabolite Production.

Microorganisms. 2021-5-12

[10]
Enhanced fusidic acid transdermal delivery achieved by newly isolated and optimized cereus Keratinase.

Biotechnol Rep (Amst). 2021-4-18

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