Recombinant bacterium

A BDS process in the presence of a recombinant bacterium [105], which was not identified in the patent abstract, was awarded in 2002 to NIAIST in cooperation with... 

The first field test of a recombinant bacterium, Frostban, engineered to inhibit ice formation... 

Gu, M.B. Chang, S. X Soil biosensor for the detection of PAH toxicity using an immobilized recombinant bacterium and a biosurfactant. Biosens Bioelectron. December 2001, 16(9-12), 667-674 [pah]. 

Gene cloning is a method that uses recombinant technology to insert a gene into a vector DNA (plasmid obtained from a bacterium). The modified vector is put back into the bacterium, which then reproduces endlessly (clones) the new gene as well as the others in the vector. 

A fermentation route to 1-butanol based on carbon monoxide employing the anaerobic bacterium, Butyribacterium methjlotrophicum has been reported (14,15). In contrast to other commercial catalytic processes for converting synthesis gas to alcohols, the new process is insensitive to sulfur contaminants. Current productivities to butanol are 1 g/L, about 10% of that required for commercial viabiUty. Researchers hope to learn enough about the bacteria s control mechanisms to be able to use recombinant DNA to make the cells produce more butanol. 

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). 

Paracoccus denitrificans, a facultatively methylotrophic bacterium, is able to grow and accumulate PHAs on methanol. Recombinant P. denitrificans strains with increased expression levels of all PHA synthetic enzymes were investigated for the enhanced production of PHA. The PHA content and PHA accumulation rate of recombinant P. denitrificans with homologous overexpression of PHA synthase were 2 and 2.7 times higher, respectively, than those of the wild strain, suggesting that the step of PHA synthase was limited in PHA biosynthesis [111]. 

Many of the initial biopharmaceuticals approved were simple replacement proteins (e.g. blood factors and human insulin). The ability to alter the amino acid sequence of a protein logically coupled to an increased understanding of the relationship between protein structure and function (Chapters 2 and 3) has facilitated the more recent introduction of several engineered therapeutic proteins (Table 1.3). Thus far, the vast majority of approved recombinant proteins have been produced in the bacterium E. coli, the yeast S. cerevisiae or in animal cell lines (most notably Chinese hamster ovary (CHO) cells or baby hamster kidney (BHK) cells. These production systems are discussed in Chapter 5. 

The concept of recombinant DNA technology is based on the premise that a gene sentence may be taken from an animal or human gene responsible for the production of a particular protein and inserted into the DNA of Escherichia coli, a single-cell bacterium. The bacterial cells then divide very rapidly, making billions of copies of themselves, including a rephea of the gene that has been inserted. 

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