Fed-batch cultures of Escherichia coli cells with oxygen-dependent nar promoter systems.
The recombinant proteins produced from Escherichia coli as a host cell need to be made at as low a cost as possible because of the end of the monopoly following expiry of the patent on early pharmaceutical proteins, and thus expanding applications to non-pharmaceutical large-scale products. We review in this article how the various promoters used in recombinant E. coli could affect its protein products, especially with emphasis on relatively new oxygen-dependent nar promoters for beta-galactosidase production. Several studies carried out in the authors' laboratory show that the nar promoter does not require any chemicals except 1% nitrate and oxygen for protein production. And according to recent work with the modified strains it is possible to produce the enzyme (beta-galactosidase) even without the nitrate ions at 45% of its total protein content when its cell density reached OD = 176.
Chang
Ho Nam
HN
Department of Chemical Engineering, KAIST, Taejon, Korea. hmchang@mail.kaist.ac.kr
Han
Se Jong
SJ
Yim
Seong-Chun
SC
Han
Mu-ri
MR
Lee
Jongwon
J
D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics / Q000378:metabolism; D005798:Genes, Bacterial; D010100:Oxygen / Q000378:metabolism*; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis; D001616:beta-Galactosidase / Q000096:biosynthesis
D011994:Recombinant Proteins; D001616:beta-Galactosidase; D010100:Oxygen