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Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation
Chicken feathers are predominantly composed of keratin; hence, valorizing the wastes becomes an imperative. In view of this, we isolated keratinase-producing bacteria and identified them through the 16S rDNA sequence. The process condition for keratinase activity was optimized, and electron microgra...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7180861/ https://www.ncbi.nlm.nih.gov/pubmed/32225031 http://dx.doi.org/10.3390/molecules25071505 |
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author | Nnolim, Nonso E. Okoh, Anthony I. Nwodo, Uchechukwu U. |
author_facet | Nnolim, Nonso E. Okoh, Anthony I. Nwodo, Uchechukwu U. |
author_sort | Nnolim, Nonso E. |
collection | PubMed |
description | Chicken feathers are predominantly composed of keratin; hence, valorizing the wastes becomes an imperative. In view of this, we isolated keratinase-producing bacteria and identified them through the 16S rDNA sequence. The process condition for keratinase activity was optimized, and electron micrography of the degradation timelines was determined. Keratinolytic bacteria were isolated and identified as Bacillus sp. FPF-1, Chryseobacterium sp. FPF-8, Brevibacillus sp. Nnolim-K2, Brevibacillus sp. FPF-12 and Brevibacillus sp. FSS-1; and their respective nucleotide sequences were deposited in GenBank, with the accession numbers MG214993, MG214994, MG214995, MG214996 and MG214999. The degree of feather degradation and keratinase concentration among the isolates ranged from 62.5 ± 2.12 to 86.0 ± 1.41(%) and 214.55 ± 5.14 to 440.01 ± 20.57 (U/mL), respectively. In the same vein, 0.1% (w/v) xylose, 0.5% (w/v) chicken feather, an initial fermentation pH of 5.0, fermentation temperature of 25 °C and an agitation speed of 150 rpm, respectively, served as the optimal physicochemical conditions for keratinase activity by Bacillus sp. FPF-1. The time course showed that Bacillus sp. FPF-1 yielded a keratinase concentration of 1698.18 ± 53.99(U/mL) at 120 h. The electron microscopic imaging showed completely structural dismemberment of intact chicken feather. Bacillus sp. FPF-1 holds great potential in the valorization of recalcitrant keratinous biomass from the agro sector into useful products. |
format | Online Article Text |
id | pubmed-7180861 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-71808612020-05-01 Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation Nnolim, Nonso E. Okoh, Anthony I. Nwodo, Uchechukwu U. Molecules Article Chicken feathers are predominantly composed of keratin; hence, valorizing the wastes becomes an imperative. In view of this, we isolated keratinase-producing bacteria and identified them through the 16S rDNA sequence. The process condition for keratinase activity was optimized, and electron micrography of the degradation timelines was determined. Keratinolytic bacteria were isolated and identified as Bacillus sp. FPF-1, Chryseobacterium sp. FPF-8, Brevibacillus sp. Nnolim-K2, Brevibacillus sp. FPF-12 and Brevibacillus sp. FSS-1; and their respective nucleotide sequences were deposited in GenBank, with the accession numbers MG214993, MG214994, MG214995, MG214996 and MG214999. The degree of feather degradation and keratinase concentration among the isolates ranged from 62.5 ± 2.12 to 86.0 ± 1.41(%) and 214.55 ± 5.14 to 440.01 ± 20.57 (U/mL), respectively. In the same vein, 0.1% (w/v) xylose, 0.5% (w/v) chicken feather, an initial fermentation pH of 5.0, fermentation temperature of 25 °C and an agitation speed of 150 rpm, respectively, served as the optimal physicochemical conditions for keratinase activity by Bacillus sp. FPF-1. The time course showed that Bacillus sp. FPF-1 yielded a keratinase concentration of 1698.18 ± 53.99(U/mL) at 120 h. The electron microscopic imaging showed completely structural dismemberment of intact chicken feather. Bacillus sp. FPF-1 holds great potential in the valorization of recalcitrant keratinous biomass from the agro sector into useful products. MDPI 2020-03-26 /pmc/articles/PMC7180861/ /pubmed/32225031 http://dx.doi.org/10.3390/molecules25071505 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Nnolim, Nonso E. Okoh, Anthony I. Nwodo, Uchechukwu U. Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation |
title | Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation |
title_full | Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation |
title_fullStr | Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation |
title_full_unstemmed | Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation |
title_short | Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation |
title_sort | bacillus sp. fpf-1 produced keratinase with high potential for chicken feather degradation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7180861/ https://www.ncbi.nlm.nih.gov/pubmed/32225031 http://dx.doi.org/10.3390/molecules25071505 |
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