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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TMKarpinski Publisher, Tomasz M. Karpiński
2019-03-01
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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
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topic |
Xylanase Aspergillus flavus Fermentation |
url |
http://www.journals.tmkarpinski.com/index.php/ejbr/article/view/111 |
work_keys_str_mv |
AT ahmoubasher productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation AT madyismail productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation AT ramadanmohamed productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation AT osamaalbedak productionandpurificationofextremexylanasefromaspergillusflavusaumc10331insubmergedfermentation |
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