Escherichia coli production

Swartz, J. R. Advances in Escherichia Coli Production of Therapeutic Proteins. Current Opinion in BiotechnologyYol. 12 no. 2 (2001) 195-201. 

Macaloney, G. Hall, J.W. Rollins, M.J. Draper, I. Anderson, K.B. Preston, J. Thompson, B.G. McNeil, B., The utility and performance of near-infrared spectroscopy in simultaneous monitoring of multiple components in a high cell density recombinant Escherichia coli production process Bioprocess Eng. 1997, 17, 157-167. 

Hakansson K, Changgoo H, Anders G et al. (1996) Mouse and rat cystatin C Escherichia coli production, characterization, and tissue distribution. Comp Biochem Physiol - B Comp Biochem 114 303-311... 

This work was followed by the detection of an aldoheptose in Escherichia coli products and the subsequent isolation of jj-glycero-i>-manno-heptoee by Weidel, again in connection with phage-receptor studies. The sugar was obtained from the lipocarbohydrate fraction of Escherichia coli B cell-membranes and was isolated, after acid hydrolysis, on a cellulose-powder column. In this case, sufficient of the product was obtained to show that the diethyl dithioacetal and its hexaacetate had equal but opposite optical rotations, as compared with those of the same derivatives prepared from authentic D-glyc o-n-manno-heptose. 

Belloc, C., Baird, S., Cosme, J., Lecoeur, S., Gautier, J.-C., Challine, D., de Waziers, I., Flinois J.-P., and Beaune, P.H. (1996) Human cytochrome P450 expressed in Escherichia coli production of spedfic antibodies. Toxicology, 106, 207-219. 

Swartz J R (2001). Advances in Escherichia coli production of therapeutic proteins. Curr. Opin. Biotechnol. 12 195-201. 

Escherichia coli Product Bacteria oxidize glucose ... 

Penicillin amidase) Escherichia coli production of semisynthetic pencillins. 

Escherichia coli. The genetics of this gram-negative bacterium are very well known. For this reason, many of the first efforts to produce recombinant products from this microorganism were successful. However, because of the importance of the other criteria Hsted above, many efforts failed. E. co/i is only used to produce the milk-clotting mammalian protease chymosin [9001-98-3] (rennin). 

Polyunsaturated fatty acids pose a slightly more complicated situation for the cell. Consider, for example, the case of linoleic acid shown in Figure 24.24. As with oleic acid, /3-oxidation proceeds through three cycles, and enoyl-CoA isomerase converts the cA-A double bond to a trans-b double bond to permit one more round of /3-oxidation. What results this time, however, is a cA-A enoyl-CoA, which is converted normally by acyl-CoA dehydrogenase to a trans-b, cis-b species. This, however, is a poor substrate for the enoyl-CoA hydratase. This problem is solved by 2,4-dienoyl-CoA reductase, the product of which depends on the organism. The mammalian form of this enzyme produces a trans-b enoyl product, as shown in Figure 24.24, which can be converted by an enoyl-CoA isomerase to the trans-b enoyl-CoA, which can then proceed normally through the /3-oxidation pathway. Escherichia coli possesses a... 

Benzyl- and Phenoxymethylpenicillins, Ampidllin, Carbenicillin Cephalosporin C Cephaloglycine, Cephaloridine, Cephalothin Hydrolysis Corresponding p-lactam ring cleavage products Escherichia coli Streptomyces aibus Pseudomonas aeruginosa Enterobacter cloacae Streptomyces sp. 

Another way to enhance the production of an amino acid is to make use of DNA-recombinant technology, often in combination with foe mutations already described. In this way foe negative features of foe micro-organisms are avoided. To help explain this, we will consider a well known fermentation of L-phenylalanine using Escherichia coli. We have already seen foe metabolic pathway leading to foe production of L-phenylalanine in Figure 8.4. 

One of the commercial methods for production of lysine consists of a two-stage process using two species of bacteria. The carbon sources for production of amino acids are corn, potato starch, molasses, and whey. If starch is used, it must be hydrolysed to glucose to achieve higher yield. Escherichia coli is grown in a medium consisting of glycerol, corn-steep liquor and di-ammonium phosphate under aerobic conditions, with temperature and pH controlled. 

Since 1978, several papers have examined the potential of using immobilised cells in fuel production. Microbial cells are used advantageously for industrial purposes, such as Escherichia coli for the continuous production of L-aspartic acid from ammonium fur-marate.5,6 Enzymes from microorganisms are classified as extracellular and intracellular. If whole microbial cells can be immobilised directly, procedures for extraction and purification can be omitted and the loss of intracellular enzyme activity can be kept to a minimum. Whole cells are used as a solid catalyst when they are immobilised onto a solid support. 

Philips, T.A., Van Bogelen, R.A. Neidhardt, F.C. (1984). Ion gene product of Escherichia coli is a heat-shock protein. Journal of Bacteriology, 159, 283-7. 

Recombinant resilin production was induced, with the nonmetabolizable lactose analogue IPTG, in the Escherichia coli bacterial strain BL21(DE3)/pLysS. Cells were collected by centrifugation (10,000 g, 20 min at 4°C) and the cell pellet frozen at 80°C. 

Recently, recombinant biocatalysts obtained using Escherichia coli cells were designed for this process. The overexpression of all enzymes required for the process, namely, hydantoinase, carbamoylase, and hydantoin racemase from Arthrobacter sp. DSM 9771 was achieved. These cells were used for production of a-amino acids at the concentration of above 50 g 1 dry cell weight [37]. This is an excellent example presenting the power of biocatalysis with respect to classical catalysis, since a simultaneous use of three different biocatalysts originated from one microorganism can be easily achieved. 

Research into elastin, its properties, and the fiber formation was for a considerable period of time hindered due to its insolubihty. However, discovery of the soluble tropoelastin precursor made new investigations possible. The tropoelastin protein can be isolated from copper-deficient animals. However, this is a very animal-unfriendly and low yielding process [2]. Therefore, it is preferred to obtain tropoelastin from overexpression in microbial hosts such as Escherichia coli (E. coli). Most studies are thus based on tropoelastin obtained via bacterial production. 

Recombinant DNA technology can also be used to design genes that encode for proteins with desired features [34]. The gene can be incorporated into a plasmid, which is then used to transform a bacterial host such as Escherichia coli. Finally, the production of the desired amino acid polymer is performed by the host with a precisely defined sequence and near absolute monodispersity [29, 35]. 

Misawa, N. et al.. Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by functional analysis of gene products expressed in Escherichia coli, J. Bacteriol. 172, 6704, 1990. 

Misawa, N. et al.. Expression of a tomato cDNA coding for phytoene synthase in Escherichia coli, phytoene formation in vivo and in vitro, and functional analysis of the various truncated gene products, J. Biochem. (Tokyo) 116, 980, 1994. 

Wang, C., Oh, M.K., and Liao, J.C., Directed evolntion of metabolically engineered Escherichia coli for carotenoid production, Biotechnol. Progr. 16, 922, 2000. 

Lee, PC., Mijts, B.N., and Schmidt-Dannert, C., Investigation of factors influencing production of the monocyclic carotenoid torulene in metahohcaUy engineered Escherichia coli, Appl. Microbiol. Biotechnol. 65, 538, 2004. 

Ruther, A. et al., Production of zeaxanthin in Escherichia coli hansformed with different carotenogenic plasmids, Appl. Microbiol. Biotechnol. 48, 162, 1997. 

Kim, S.W. et al.. Over-production of beta-carotene from metabolicaUy engineered Escherichia coli, Biotechnol. Lett. 28, 897, 2006. 

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