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Global transcriptome response of recombinant protein xylanase producing E. coli in high cell density fed batch culture

ABSTRACT: Strong production of recombinant proteins interfere with cellular processes in many ways. The extent of the bacterial stress response is determined by the specific properties of the recombinant protein, and by the rates of transcription and translation. The consideration of bacterial stress and starvation responses is of crucial importance for the successful establishment of an industrial large scale bioprocess. Stress genes can be used as marker genes in order to monitor the fitness of industrial bacterial hosts during fermentation processes. For this purpose, here in our study we have applied transcriptome analysis for the description of general and specific stress and starvation responses of Escherichia coli. Producing recombinant protein (Xylanase) in high cell density fed batch culture.

ORGANISM(S): Escherichia coli

PROVIDER: GSE29439 | GEO | 2011/05/24

SECONDARY ACCESSION(S): PRJNA141515

REPOSITORIES: GEO

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Global transcriptome response of recombinant protein xylanase producing E. coli in high cell density fed batch culture

Project description:Strong production of recombinant proteins interfere with cellular processes in many ways. The extent of the bacterial stress response is determined by the specific properties of the recombinant protein, and by the rates of transcription and translation. The consideration of bacterial stress and starvation responses is of crucial importance for the successful establishment of an industrial large scale bioprocess. Stress genes can be used as marker genes in order to monitor the fitness of industrial bacterial hosts during fermentation processes. For this purpose, here in our study we have applied transcriptome analysis for the description of general and specific stress and starvation responses of Escherichia coli. Producing recombinant protein (Xylanase) in high cell density fed batch culture. Cells were grown in batch mode in TB media till an OD600 of 15. The specific growth rate of 0.3 h-1 was maintained by fed batch started at OD600 of 15. Cells were induced at an OD600 of 30 using 1 mM IPTG and the growth and product profile was monitored. Samples at different time points (2hrs, 4hrs, and 6hrs) were taken and frozen in liquid nitrogen quickly for transcriptome analysis.

2011-05-23 | E-GEOD-29439 | biostudies-arrayexpress

Analyzing the metabolic stress response of recombinant Escherichia coli cultures expressing human interferon beta in high cell density fed batch cultures using time course transcriptomic data

2011-04-07 | GSE28412 | GEO

Analyzing the metabolic stress response of recombinant Escherichia coli cultures expressing human interferon beta in high cell density fed batch cultures using time course transcriptomic data

Project description:Over expression of recombinant proteins is known to cause a metabolic burden to the host cells which leads to down regulation of both growth rates and protein expression. Most studies in this regard have been conducted in low density shake flask cultures which does not capture the essential features of an industrial scale bioprocess. In the present work we studied the transcriptomic profiling at different specific growth rates while expressing the recombinant human interferon beta in fed batch cultures with complex media. These conditions mimicked the industrial fermentations for recombinant proteins. To determine the transcriptomic response of E.coli BL21(DE3) to recombinant protein production at three different specific growth rates, samples were collected for four time points (0h, 2h, 4h, 6h) post induction for the fed batch cultivations at specific growth rates 0.2h-1, 0.3h-1, 0.4h-1 respectively and induced at an optical density of 30. 0h (uninduced) sample was taken as control conditions for every run.

2011-04-06 | E-GEOD-28412 | biostudies-arrayexpress

Amino acid supplementation for enhancing recombinant protein production in E. coli

Project description:Amino acid starvation during recombinant protein production (RPP) induces metabolic stress to cellular host which results in reduced productivity of the recombinant bioprocess. In present study, supplementation of amino acids in a chemically defined medium showed several folds increase in recombinant product titers in E. coli BL21 DE3 strain. To understand, the effect of amino acid supplementation in alleviating cellular stress during RPP a deep insight of cellular physiology must be studied. Here, we performed transcriptomic analysis of E. coli expressing a recombinant protein in two different conditions: with (5 mM of all 20 amino acids) as test and without supplementation of amino acids as control. RNA-seq data revealed downregulation of several genes associated with stress in test culture confirming the critical role of amino acids supplementation in improving RPP.

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Comparative genomic, transcriptomic and secretomic profilings of Penicillium oxalicum HP7-1 and its cellulase and xylanase hyper-producing mutant EU2106, and identification of two novel regulators for cellulase and xylanase gene expression

Project description:In this study,comparative genomic, transcriptomic and secretomic profilings of Penicillium oxalicum HP7-1 and its cellulase and xylanase hyper-producing mutant EU2106 were employed to screen for novel regulators for cellulase and xylanase gene expression.

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Effects of transcription factor POX04513 on the transcription of cellulase genes and xylanase genes in Penicillium oxalicum

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Large-scale transcriptomic analyses reveal a global co-expression network of cellulase and xylanase genes in filamentous fungi

Project description:A global co-expression network of cellulase and xylanase genes was identified in P. oxalicum, their transcriptional levels depended on the induction of carbon sources and induction time.

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Induction of CtsR-regulated chaperones improves Xylanase production in Bacillus subtilis

Project description:We examined the effect of high-level expression of the commercially important endo-1,4-β-xylanase XynA on the B. subtilis transcriptome using RNA-seq. Rather unexpectedly, we found a reduced expression of several protein chaperones, including ClpC, ClpE and ClpX, was downregulated when XynA was overproduced. Expression of these proteins is controlled by the transcriptional repressor CtsR. CtsR levels are directly controlled by regulated proteolysis, involving ClpC and its cognate protease ClpP. Preventing this downregulation by knocking out the involved transcriptional repressor CtsR resulted in increased XynA production by more than 25 %.

2023-02-21 | GSE217916 | GEO

Pilot project to determine optimal bioreactor protein glycosylation conditions

Project description:These research areas concentrate on stress induced proteases in recombinant Escherichia coli, glycosylation heterogeneity due to bioprocess conditions produced in mammalian cells, and metabolic engineering of E. coli. The hypothesis of this project is that recombinant protein glycosylation is inefficient under normal bioreactor conditions since the additional glycosylation reactions necessary for the recombinant protein exceed the metabolic capacity of the cells. Normal bioreactor conditions have been optimized for cell growth, and sometimes for protein productivity. Only recently has it been accepted that optimal glycosylation may not occur under optimal growth or protein productivity conditions. Specific Aim: Determine the relationship between bioreactor conditions and glycosylation gene expression in NS0 cells.

2011-04-29 | GSE28920 | GEO

Large scale transcriptome analysis was used to identify the genes most related to the transcription of cellulase genes and/or xylanase genes expression

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2023-07-22 | GSE155790 | GEO

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