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Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss

This paper assesses the ability of strains of Aphanoascus fulvescens and Chrysosporium articulatum isolated from soil (phaesol) to degrade native feather keratin. Strains were identified based on phenotypic traits and nucleotide sequencing. Response Surface Methodology was used to optimize cultivati...

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Autor principal: Bohacz, Justyna
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5122606/
https://www.ncbi.nlm.nih.gov/pubmed/27885567
http://dx.doi.org/10.1007/s11274-016-2177-2
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author Bohacz, Justyna
author_facet Bohacz, Justyna
author_sort Bohacz, Justyna
collection PubMed
description This paper assesses the ability of strains of Aphanoascus fulvescens and Chrysosporium articulatum isolated from soil (phaesol) to degrade native feather keratin. Strains were identified based on phenotypic traits and nucleotide sequencing. Response Surface Methodology was used to optimize cultivation conditions exhibiting the highest keratinolytic activity. The experiments were based on Box-Behnken designs for the loss of substrate mass (chicken feathers). While substrate mass loss is an “economic coefficient” that reliably indicates feather keratin degradation, it has not been studied before. Stationary liquid cultures of five selected strains were conducted in laboratory conditions at 28 °C using poultry feathers (1 g) as the sole source of carbon, nitrogen and energy. Enzymatic activities, keratin mineralization products and substrate mass loss were determined periodically. The mineralization of keratin proteins by strains yielded a high number of ammonium ions alkalinizing the medium. Increased ammonium ions inhibited the activity of caseinian protease and keratinase. A decrease in the concentration of these ions induced proteolytic enzymes, chiefly the activity of keratinase, at the end of fungal cultivation. Keratinase activity was related to protein- and peptide release and that of caseinian protease to sulfate ions. The highest loss of substrate mass in comparison to the reference strain CBS104.62 (35.4%) was recorded for Aphanoascus fulvescens B21/4-5 (65.9%). Based on a Box-Behnken design, the maximum loss of substrate mass for the Aphanoascus fulvescens strain (71.08%) can be achieved at pH 7.58 and temperature 28.7 °C.
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spelling pubmed-51226062016-12-09 Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss Bohacz, Justyna World J Microbiol Biotechnol Original Paper This paper assesses the ability of strains of Aphanoascus fulvescens and Chrysosporium articulatum isolated from soil (phaesol) to degrade native feather keratin. Strains were identified based on phenotypic traits and nucleotide sequencing. Response Surface Methodology was used to optimize cultivation conditions exhibiting the highest keratinolytic activity. The experiments were based on Box-Behnken designs for the loss of substrate mass (chicken feathers). While substrate mass loss is an “economic coefficient” that reliably indicates feather keratin degradation, it has not been studied before. Stationary liquid cultures of five selected strains were conducted in laboratory conditions at 28 °C using poultry feathers (1 g) as the sole source of carbon, nitrogen and energy. Enzymatic activities, keratin mineralization products and substrate mass loss were determined periodically. The mineralization of keratin proteins by strains yielded a high number of ammonium ions alkalinizing the medium. Increased ammonium ions inhibited the activity of caseinian protease and keratinase. A decrease in the concentration of these ions induced proteolytic enzymes, chiefly the activity of keratinase, at the end of fungal cultivation. Keratinase activity was related to protein- and peptide release and that of caseinian protease to sulfate ions. The highest loss of substrate mass in comparison to the reference strain CBS104.62 (35.4%) was recorded for Aphanoascus fulvescens B21/4-5 (65.9%). Based on a Box-Behnken design, the maximum loss of substrate mass for the Aphanoascus fulvescens strain (71.08%) can be achieved at pH 7.58 and temperature 28.7 °C. Springer Netherlands 2016-11-24 2017 /pmc/articles/PMC5122606/ /pubmed/27885567 http://dx.doi.org/10.1007/s11274-016-2177-2 Text en © The Author(s) 2016 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Original Paper
Bohacz, Justyna
Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss
title Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss
title_full Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss
title_fullStr Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss
title_full_unstemmed Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss
title_short Biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus Chrysosporium and statistical optimization of feather mass loss
title_sort biodegradation of feather waste keratin by a keratinolytic soil fungus of the genus chrysosporium and statistical optimization of feather mass loss
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5122606/
https://www.ncbi.nlm.nih.gov/pubmed/27885567
http://dx.doi.org/10.1007/s11274-016-2177-2
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