Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum

Abstract Endoglucanase (EC 3.2.1.4) catalysing the hydrolysis of β-1.4-glycosidic linkage of cellulose molecules is an enzyme of tremendous industrial importance. The present study describes a response surface methodology based predicted model to deduce a set of fermentation conditions for optimum g...

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Autores principales:	Iram Shahzadi, Maryam A. Al-Ghamdi, Muhammad Shahid Nadeem, Muhammad Sajjad, Asif Ali, Jalaluddin Azam Khan, Imran Kazmi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/941e25ea49f64d738bb6bee1184861d2
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spelling	oai:doaj.org-article:941e25ea49f64d738bb6bee1184861d22021-12-02T13:27:08ZScale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum10.1038/s41598-021-86000-z2045-2322https://doaj.org/article/941e25ea49f64d738bb6bee1184861d22021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86000-zhttps://doaj.org/toc/2045-2322Abstract Endoglucanase (EC 3.2.1.4) catalysing the hydrolysis of β-1.4-glycosidic linkage of cellulose molecules is an enzyme of tremendous industrial importance. The present study describes a response surface methodology based predicted model to deduce a set of fermentation conditions for optimum growth and activity of recombinant endoglucanase in E. coli BL21 (DE3). Numerous significant parameters including fermentation media composition, temperature (Celsius), pH and agitation rate (rpm) were analysed systemically by employing central composite design. This effort reports highly efficient recombinant endoglucanase overproduction (6.9 gl−1 of biomass) with 30% expression by E. coli in modified M9NG media incubated at 37 °C and pH 7 agitated at 200 rpm. Addition of 3 mM glucose and 24 mM glycerol in the M9NG media has shown positive effect on the enzyme yield and activity. The CMCase activity experimentally estimated was found to be 1185 U/mg with the optimized parameters. The outcomes of both the responses by the predicted quadratic model were found in consensus with the obtained values. Our results well depicted the favourable conditions to further scale-up the volumetric yield of other relevant recombinant enzymes and proteins.Iram ShahzadiMaryam A. Al-GhamdiMuhammad Shahid NadeemMuhammad SajjadAsif AliJalaluddin Azam KhanImran KazmiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Iram Shahzadi Maryam A. Al-Ghamdi Muhammad Shahid Nadeem Muhammad Sajjad Asif Ali Jalaluddin Azam Khan Imran Kazmi Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum
description	Abstract Endoglucanase (EC 3.2.1.4) catalysing the hydrolysis of β-1.4-glycosidic linkage of cellulose molecules is an enzyme of tremendous industrial importance. The present study describes a response surface methodology based predicted model to deduce a set of fermentation conditions for optimum growth and activity of recombinant endoglucanase in E. coli BL21 (DE3). Numerous significant parameters including fermentation media composition, temperature (Celsius), pH and agitation rate (rpm) were analysed systemically by employing central composite design. This effort reports highly efficient recombinant endoglucanase overproduction (6.9 gl−1 of biomass) with 30% expression by E. coli in modified M9NG media incubated at 37 °C and pH 7 agitated at 200 rpm. Addition of 3 mM glucose and 24 mM glycerol in the M9NG media has shown positive effect on the enzyme yield and activity. The CMCase activity experimentally estimated was found to be 1185 U/mg with the optimized parameters. The outcomes of both the responses by the predicted quadratic model were found in consensus with the obtained values. Our results well depicted the favourable conditions to further scale-up the volumetric yield of other relevant recombinant enzymes and proteins.
format	article
author	Iram Shahzadi Maryam A. Al-Ghamdi Muhammad Shahid Nadeem Muhammad Sajjad Asif Ali Jalaluddin Azam Khan Imran Kazmi
author_facet	Iram Shahzadi Maryam A. Al-Ghamdi Muhammad Shahid Nadeem Muhammad Sajjad Asif Ali Jalaluddin Azam Khan Imran Kazmi
author_sort	Iram Shahzadi
title	Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum
title_short	Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum
title_full	Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum
title_fullStr	Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum
title_full_unstemmed	Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum
title_sort	scale-up fermentation of escherichia coli for the production of recombinant endoglucanase from clostridium thermocellum
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/941e25ea49f64d738bb6bee1184861d2
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Scale-up fermentation of Escherichia coli for the production of recombinant endoglucanase from Clostridium thermocellum

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