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Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation
Xylanase breaks xylan down to xylose, which is used in industries such as pulp and paper, food and feed, among others. The utilization of wastes for xylanase production is economical, hence this work aimed at producing xylanase through solid-state fermentation and characterizing the enzyme. Xylanase...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Microbiology Society
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10323791/ https://www.ncbi.nlm.nih.gov/pubmed/37424564 http://dx.doi.org/10.1099/acmi.0.000506.v5 |
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author | Fasiku, Samuel Adedayo Bello, Mobolaji Akeem Odeniyi, Olubusola Ayoola |
author_facet | Fasiku, Samuel Adedayo Bello, Mobolaji Akeem Odeniyi, Olubusola Ayoola |
author_sort | Fasiku, Samuel Adedayo |
collection | PubMed |
description | Xylanase breaks xylan down to xylose, which is used in industries such as pulp and paper, food and feed, among others. The utilization of wastes for xylanase production is economical, hence this work aimed at producing xylanase through solid-state fermentation and characterizing the enzyme. Xylanase-producing strains of Bacillus megaterium and Aspergillus niger GIO were inoculated separately in a 5 and 10 day solid fermentation study on maize straw, rice straw, sawdust, corn cob, sugarcane bagasse, conifer litters, alkaline-pretreated maize straw (APM) and combined alkaline and biological-pretreated maize straw, respectively. The best substrate was selected for xylanase production. The crude enzyme was extracted from the fermentation medium and xylanase activity was characterized using parameters such as temperature, cations, pH and surfactants. Among different substrates, the highest xylanase activity of 3.18 U ml(−1) was recorded when A. niger GIO was grown on APM. The xylanase produced by A. niger GIO and B. megaterium had the highest activities (3.67 U ml(−1) and 3.36 U ml(−1)) at 40 °C after 30 and 45 min of incubation, respectively. Optimal xylanase activities (4.58 and 3.58 U ml(−1)) of A. niger GIO and B. megaterium , respectively, were observed at pH 5.0 and 6.2. All cations used enhanced xylanase activities except magnesium ion. Sodium dodecyl sulfate supported the highest xylanase activity of 6.13 and 6.90 U ml(−1) for A. niger GIO and B. megaterium , respectively. High yields of xylanase were obtained from A. niger GIO and B. megaterium cultivated on APM. The xylanase activities were affected by pH, temperature, surfactants and cations. |
format | Online Article Text |
id | pubmed-10323791 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Microbiology Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-103237912023-07-07 Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation Fasiku, Samuel Adedayo Bello, Mobolaji Akeem Odeniyi, Olubusola Ayoola Access Microbiol Research Articles Xylanase breaks xylan down to xylose, which is used in industries such as pulp and paper, food and feed, among others. The utilization of wastes for xylanase production is economical, hence this work aimed at producing xylanase through solid-state fermentation and characterizing the enzyme. Xylanase-producing strains of Bacillus megaterium and Aspergillus niger GIO were inoculated separately in a 5 and 10 day solid fermentation study on maize straw, rice straw, sawdust, corn cob, sugarcane bagasse, conifer litters, alkaline-pretreated maize straw (APM) and combined alkaline and biological-pretreated maize straw, respectively. The best substrate was selected for xylanase production. The crude enzyme was extracted from the fermentation medium and xylanase activity was characterized using parameters such as temperature, cations, pH and surfactants. Among different substrates, the highest xylanase activity of 3.18 U ml(−1) was recorded when A. niger GIO was grown on APM. The xylanase produced by A. niger GIO and B. megaterium had the highest activities (3.67 U ml(−1) and 3.36 U ml(−1)) at 40 °C after 30 and 45 min of incubation, respectively. Optimal xylanase activities (4.58 and 3.58 U ml(−1)) of A. niger GIO and B. megaterium , respectively, were observed at pH 5.0 and 6.2. All cations used enhanced xylanase activities except magnesium ion. Sodium dodecyl sulfate supported the highest xylanase activity of 6.13 and 6.90 U ml(−1) for A. niger GIO and B. megaterium , respectively. High yields of xylanase were obtained from A. niger GIO and B. megaterium cultivated on APM. The xylanase activities were affected by pH, temperature, surfactants and cations. Microbiology Society 2023-06-14 /pmc/articles/PMC10323791/ /pubmed/37424564 http://dx.doi.org/10.1099/acmi.0.000506.v5 Text en © 2023 The Authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License. |
spellingShingle | Research Articles Fasiku, Samuel Adedayo Bello, Mobolaji Akeem Odeniyi, Olubusola Ayoola Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation |
title | Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation |
title_full | Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation |
title_fullStr | Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation |
title_full_unstemmed | Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation |
title_short | Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation |
title_sort | production of xylanase by aspergillus niger gio and bacillus megaterium through solid-state fermentation |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10323791/ https://www.ncbi.nlm.nih.gov/pubmed/37424564 http://dx.doi.org/10.1099/acmi.0.000506.v5 |
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