Expression of an anaplerotic enzyme, pyruvate carboxylase, improves recombinant protein production in Escherichia coli

dc.contributor.author	March, JC	en
dc.contributor.author	Eiteman, MA	en
dc.contributor.author	Altman, E	en
dc.date.accessioned	2014-06-06T06:44:48Z
dc.date.available	2014-06-06T06:44:48Z
dc.date.issued	2002	en
dc.identifier.issn	00992240	en
dc.identifier.uri	http://62.217.125.90/xmlui/handle/123456789/2080
dc.relation.uri	http://www.scopus.com/inward/record.url?eid=2-s2.0-0036841201&partnerID=40&md5=f0e07ba65926be536f3fedee81a3536c	en
dc.subject.other	Batch cell culture	en
dc.subject.other	Biomass	en
dc.subject.other	Carboxylic acids	en
dc.subject.other	Enzymes	en
dc.subject.other	Fermentation	en
dc.subject.other	Genetic engineering	en
dc.subject.other	Glucose	en
dc.subject.other	Cell yields	en
dc.subject.other	Escherichia coli	en
dc.subject.other	acetic acid	en
dc.subject.other	beta galactosidase	en
dc.subject.other	carbon	en
dc.subject.other	glucose	en
dc.subject.other	pyruvate carboxylase	en
dc.subject.other	recombinant protein	en
dc.subject.other	tricarboxylic acid	en
dc.subject.other	enzyme	en
dc.subject.other	article	en
dc.subject.other	batch fermentation	en
dc.subject.other	biomass	en
dc.subject.other	cell growth	en
dc.subject.other	chemical reaction	en
dc.subject.other	concentration (parameters)	en
dc.subject.other	enzyme activity	en
dc.subject.other	Escherichia coli	en
dc.subject.other	nonhuman	en
dc.subject.other	protein expression	en
dc.subject.other	protein synthesis	en
dc.subject.other	beta-Galactosidase	en
dc.subject.other	Biotechnology	en
dc.subject.other	Escherichia coli	en
dc.subject.other	Pyruvate Carboxylase	en
dc.subject.other	Recombinant Proteins	en
dc.subject.other	Escherichia coli	en
dc.subject.other	Negibacteria	en
dc.title	Expression of an anaplerotic enzyme, pyruvate carboxylase, improves recombinant protein production in Escherichia coli	en
heal.type	journalArticle	en
heal.publicationDate	2002	en
heal.abstract	Anaplerotic enzyme reactions are those which replenish tricarboxylic acid intermediates that are withdrawn for the synthesis of biomass. In this study, we examined recombinant protein production in Escherichia coli containing activity in an additional anaplerotic enzyme, pyruvate carboxylase. In batch fermentations, the presence of pyruvate carboxylase resulted in 68% greater production of the model protein, β-galactosidase, 41% greater cell yield, and 57% lower acetate concentration. We discuss why these results indicate that acetate concentration does not limit cell growth and protein synthesis, as predicted by other researchers, and suggest instead that the rate of acetate formation represents an inefficient consumption of glucose carbon, which is reduced by the presence of pyruvate carboxylase.	en
heal.journalName	Applied and Environmental Microbiology	en
dc.identifier.issue	11	en
dc.identifier.volume	68	en
dc.identifier.spage	5620	en
dc.identifier.epage	5624	en