Large scale production of biologically active Escherichia coli glutamyl-tRNA reductase from inclusion bodies

2003 ◽  
Vol 31 (2) ◽  
pp. 271-275 ◽  
Author(s):  
Stefan Schauer ◽  
Corinna Lüer ◽  
Jürgen Moser
Keyword(s):  
Escherichia Coli ◽  
Inclusion Bodies ◽  
Large Scale ◽  
Biologically Active ◽  
Scale Production ◽  
Large Scale Production

Mammalian G-protein-coupled receptor expression in Escherichia coli: I. High-throughput large-scale production as inclusion bodies

2009 ◽  
Vol 386 (2) ◽  
pp. 147-155 ◽  
Author(s):  
Kerstin Michalke ◽  
Marie-Eve Gravière ◽  
Céline Huyghe ◽  
Renaud Vincentelli ◽  
Renaud Wagner ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
G Protein ◽  
High Throughput ◽  
Inclusion Bodies ◽  
Large Scale ◽  
Receptor Expression ◽  
Scale Production ◽  
Expression In Escherichia Coli ◽  
Large Scale Production ◽  
G Protein Coupled

Large-scale production of citrate synthase from a cloned gene

1982 ◽  
Vol 60 (12) ◽  
pp. 1143-1147 ◽  
Author(s):  
Harry W. Duckworth ◽  
Alexander W. Bell
Keyword(s):  
Escherichia Coli ◽  
Large Scale ◽  
Citrate Synthase ◽  
Specific Activity ◽  
Tetracycline Resistance ◽  
Scale Production ◽  
Ampicillin Resistance ◽  
Colicin E1 ◽  
Large Scale Production ◽  
Cloned Gene

Starting with a colicin E1 resistance recombinant plasmid which contains gltA, the gene for citrate synthase in Escherichia coli, we have constructed an ampicillin-resistance plasmid containing the gltA region as a 2.9-kilobase-pair insert in the tetracycline-resistance region of pBR322. Escherichia coli HB101 harbouring this plasmid, when grown on rich medium containing ampicillin, contains citrate synthase as about 8% of its soluble protein. The enzyme has been purified from this rich source and is identical to the chromosomal enzyme prepared previously in every property tested, except for specific activity, which is 64 U∙mg−1 as compared with 45–50 U∙mg−1 previously obtained. The N-terminal sequences of both enzymes are reported, and they are identical up to residue 16 at least. The overall yield of pure enzyme, starting with the cells grown in 15 L of medium, is 600–800 mg.

scholarly journals Plant expression systems for production of hemagglutinin as a vaccine against influenza virus.

2014 ◽  
Vol 61 (3) ◽  
Author(s):  
Patrycja Redkiewicz ◽  
Agnieszka Sirko ◽  
Katarzyna Anna Kamel ◽  
Anna Góra-Sochacka
Keyword(s):  
Influenza Virus ◽  
Large Scale ◽  
Immunological Response ◽  
Biologically Active ◽  
Scale Production ◽  
Expression Systems ◽  
Lethal Challenge ◽  
Subunit Vaccines ◽  
Large Scale Production ◽  
Major Surface

Many examples of a successful application of plant-based expression systems for production of biologically active recombinant proteins exist in the literature. These systems can function as inexpensive platforms for the large scale production of recombinant pharmaceuticals or subunit vaccines. Hemagglutinin (HA) is a major surface antigen of the influenza virus, thus it is in the centre of interests of various subunit vaccine engineering programs. Large scale production of recombinant HA in traditional expression systems, such as mammalian or insect cells, besides other limitations, is expensive and time-consuming. These difficulties stimulate an ever-increasing interest in plant-based production of this recombinant protein. Over the last few years many successful cases of HA production in plants, using both transient and stable expression systems have been reported. Various forms of recombinant HA, including monomers, trimers, virus like particles (VLPs) or chimeric proteins containing its fusion with other polypeptides were obtained and shown to maintain a proper antigenicity. Immunizations of animals (mice, ferrets, rabbits or chickens) with some of these plant-derived hemagglutinin variants were performed, and their effectiveness in induction of immunological response and protection against lethal challenge with influenza virus demonstrated. Plant-produced recombinant subunit vaccines and plant-made VLPs were successfully tested in clinical trials (Phase I and II) that confirmed their tolerance and immunogenicity.

scholarly journals Efficient Production of l-Ribose with a Recombinant Escherichia coli Biocatalyst

2008 ◽  
Vol 74 (10) ◽  
pp. 2967-2975 ◽  
Author(s):  
Ryan D. Woodyer ◽  
Nathan J. Wymer ◽  
F. Michael Racine ◽  
Shama N. Khan ◽  
Badal C. Saha
Keyword(s):  
Escherichia Coli ◽  
Large Scale ◽  
Active Form ◽  
Apium Graveolens ◽  
Efficient Production ◽  
Scale Production ◽  
Gene Encoding ◽  
Large Scale Production ◽  
One Step ◽  
Rare Sugars

ABSTRACT A new synthetic platform with potential for the production of several rare sugars, with l-ribose as the model target, is described. The gene encoding the unique NAD-dependent mannitol-1-dehydrogenase (MDH) from Apium graveolens (garden celery) was synthetically constructed for optimal expression in Escherichia coli. This MDH enzyme catalyzes the interconversion of several polyols and their l-sugar counterparts, including the conversion of ribitol to l-ribose. Expression of recombinant MDH in the active form was successfully achieved, and one-step purification was demonstrated. Using the created recombinant E. coli strain as a whole-cell catalyst, the synthetic utility was demonstrated for production of l-ribose, and the system was improved using shaken flask experiments. It was determined that addition of 50 to 500 μM ZnCl2 and addition of 5 g/liter glycerol both improved production. The final levels of conversion achieved were >70% at a concentration of 40 g/liter and >50% at a concentration of 100 g/liter. The best conditions determined were then scaled up to a 1-liter fermentation that resulted in 55% conversion of 100 g/liter ribitol in 72 h, for a volumetric productivity of 17.4 g liter−1 day−1. This system represents a significantly improved method for the large-scale production of l-ribose.

Dimroth´s Rearrangement as a Synthetic Strategy Towards New Heterocyclic Compounds

2020 ◽  
Vol 24 (17) ◽  
pp. 1999-2018
Author(s):  
Vitor F. Ferreira ◽  
Thais de B. da Silva ◽  
Fernanda P. Pauli ◽  
Patricia G. Ferreira ◽  
Luana da S. M. Forezi ◽  
...  
Keyword(s):  
Bioactive Compounds ◽  
Heterocyclic Compounds ◽  
Large Scale ◽  
Molecular Diversity ◽  
Biologically Active ◽  
Scale Production ◽  
Dimroth Rearrangement ◽  
Synthetic Strategy ◽  
Large Scale Production ◽  
Synthetic Approaches

Molecular rearrangements are important tools to increase the molecular diversity of new bioactive compounds, especially in the class of heterocycles. This review deals specifically with a very famous and widely applicable rearrangement known as the Dimroth Rearrangement. Although it has originally been observed for 1,2,3-triazoles, its amplitude was greatly expanded to other heterocycles, as well as from laboratory to large scale production of drugs and intermediates. The reactions that were discussed in this review were selected with the aim of demonstrating the windows that may be open by the Dimroth's rearrangement, especially in what regards the development of new synthetic approaches toward biologically active compounds.

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