Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation

Xylan, extracted from oat spelts in a previous work, was assayed by HPLC and used as carbon source for the production of xylanase from Aspergillus flavus AUMC 10331. The produced xylanase was purified using ion exchange resin (IR-120 EP) and gel filtration column of Sephadex G-75 and Sephadex G-100...

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Main Authors: AH Moubasher, Mady Ismail, Ramadan Mohamed, Osama Al-Bedak
Format: Article
Language:English
Published: TMKarpinski Publisher, Tomasz M. Karpiński 2019-03-01
Series:European Journal of Biological Research
Subjects:
Online Access:http://www.journals.tmkarpinski.com/index.php/ejbr/article/view/111
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spelling doaj-bc8dd6ee2b2c48cfa5a4bd04f0deb6d12021-08-02T17:49:59ZengTMKarpinski Publisher, Tomasz M. KarpińskiEuropean Journal of Biological Research2449-89552019-03-0191Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentationAH Moubasher0Mady Ismail1Ramadan Mohamed2Osama Al-Bedak3Botany and Microbiology Department, Faculty of Science, Assiut University, Assiut 71511, Egypt; Assiut University Mycological Centre (AUMC), Assiut University, Assiut 71511, EgyptBotany and Microbiology Department, Faculty of Science, Assiut University, Assiut 71511, Egypt; Assiut University Mycological Centre (AUMC), Assiut University, Assiut 71511, EgyptBotany and Microbiology Department, Faculty of Science, Assiut University, Assiut 71511, EgyptAssiut University Mycological Centre (AUMC), Assiut University, Assiut 71511, Egypt Xylan, extracted from oat spelts in a previous work, was assayed by HPLC and used as carbon source for the production of xylanase from Aspergillus flavus AUMC 10331. The produced xylanase was purified using ion exchange resin (IR-120 EP) and gel filtration column of Sephadex G-75 and Sephadex G-100. The purified xylanase showed total activity of 5.5 IU/ml and specific activity of 687.5 IU/mg, and the enzyme purified 156.75 fold with 4.43 % yield. The highest activity at pH 7.0 and 10.5 indicating two xylanases with the most interesting one with a maximum activity at pH 10.5 and 65 °C. The enzyme activity was greatly stimulated by 5 mM of FeSO4 and CuSO4, while slightly inhibited by other metal ions. Km and Vmax were determined as 8.36 mg/ml and 172.4 IU/min respectively. DOI: http://dx.doi.org/10.5281/zenodo.2586103 http://www.journals.tmkarpinski.com/index.php/ejbr/article/view/111XylanaseAspergillus flavusFermentation
collection DOAJ
language English
format Article
sources DOAJ
author AH Moubasher
Mady Ismail
Ramadan Mohamed
Osama Al-Bedak
spellingShingle AH Moubasher
Mady Ismail
Ramadan Mohamed
Osama Al-Bedak
Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation
European Journal of Biological Research
Xylanase
Aspergillus flavus
Fermentation
author_facet AH Moubasher
Mady Ismail
Ramadan Mohamed
Osama Al-Bedak
author_sort AH Moubasher
title Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation
title_short Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation
title_full Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation
title_fullStr Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation
title_full_unstemmed Production and purification of extreme xylanase from Aspergillus flavus AUMC 10331 in sub-merged fermentation
title_sort production and purification of extreme xylanase from aspergillus flavus aumc 10331 in sub-merged fermentation
publisher TMKarpinski Publisher, Tomasz M. Karpiński
series European Journal of Biological Research
issn 2449-8955
publishDate 2019-03-01
description Xylan, extracted from oat spelts in a previous work, was assayed by HPLC and used as carbon source for the production of xylanase from Aspergillus flavus AUMC 10331. The produced xylanase was purified using ion exchange resin (IR-120 EP) and gel filtration column of Sephadex G-75 and Sephadex G-100. The purified xylanase showed total activity of 5.5 IU/ml and specific activity of 687.5 IU/mg, and the enzyme purified 156.75 fold with 4.43 % yield. The highest activity at pH 7.0 and 10.5 indicating two xylanases with the most interesting one with a maximum activity at pH 10.5 and 65 °C. The enzyme activity was greatly stimulated by 5 mM of FeSO4 and CuSO4, while slightly inhibited by other metal ions. Km and Vmax were determined as 8.36 mg/ml and 172.4 IU/min respectively. DOI: http://dx.doi.org/10.5281/zenodo.2586103
topic Xylanase
Aspergillus flavus
Fermentation
url http://www.journals.tmkarpinski.com/index.php/ejbr/article/view/111
work_keys_str_mv AT ahmoubasher productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation
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AT ramadanmohamed productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation
AT osamaalbedak productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation
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