Production from E. coli

RecA gene product from E. coli which cleaves bacteriophage A repressor The acid proteinase, renin, which cleaves angiotenginogen to ansiotensin... 

C. Example 6 An Economic Analysis for Heparinase I Production from E. coli... 

The next two examples pursue this line of thought further wherein we analyze a computer-aided process of human insulin production.15 This is then followed by an analysis of process simulation of heparinase I production from E. coli.5... 

Expression of plant genes involved in flavonoid biosynthesis is not easy in E. coli, but the ability of yeast S. cerevisiae to express such genes makes it an attractive production platform. However, the functional expression of many plant genes has recently been reported for the heterologous production of value-added products from E. coli. 

Agarwal L, Isar J, Dutt K, Saxena RK (2007a) Statistical optimization for succinic acid production from E. coli in a cost-effective medium. Appl Biochem Biotechnol 142 158-167... 

Rasor and Tischer (1998) have brought out the advantages of enzyme immobilization. Examples of penicillin-G to 6-APA, hydrolysis of cephalospwrin C into 7-ACA, hydrolysis of isosorbide diacetate and hydrolysis of 5-(4-hydroxy phenyl) hydantom are cited. De Vroom (1998) has reported covalent attachment of penicillin acylase (EC 3.51.11) from E.Coli in a gelatine-based carrier to give a water insoluble catalyst assemblase which can be recycled many times, and is suitable for the production of semi-synthetic antibiotics in an aqueous environment. The enzyme can be applied both in a hydrolytic fashion and a synthetic fashion. 6-APA was produced from penicillin-G similarly, 7-ADCA was produced from desa acetoxycephalosporin G, a ring expansion product of penicillin G. 

Production of laboratory and pilot scale quantities of a newly identified enzyme (either naturally occurring or engineered) can be facilitated by cloning and expressing the gene in an alternate host system. This host may be different from the host for final product of the commercial product (ie. E.coli vs Bacillus spp.). 

In an interesting extension of this work, the Neu5Ac aldolase from E. coli was subjected to directed evolution to expand its catalytic activity for enantiomeric forms of the usual substrates to include A -acetyl-L-mannosamine and L-arabinose with formation of the synthetically important products L-sialic add and L-3-deoxy-L-manno-oct-2-ulosonic add (l-KDO) (163). The evolved Neu5Ac aldolases were characterized by sequence analysis, kinetics, stereoselectivity, and in one case even by an X-ray structure analysis. Again, remote mutations were identified. It is significant... 

A single enzyme, L-aspartate ammonia lyase obtained from E. coli is used acting on ammonium fumarate substrate. Little cell activity was lost upon immobilisation. Initially polyacrylamide was used as the immobilisation medium, and later cross-linked K-carrageenan was used, as higher operational life-times for the biocatalyst were obtained. The immobilized cell activity is very stable with a half-life of 120 days, while achieving 95% conversion of substrate into product. 

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