beta-Galactosidase and tryptophanase were induced either simultaneously or successively during continuous cultivation of the inducible strain Escherichia coli K 12 in the chemostat. Growth was limited by glycerol and the dilution rate was 0.1 h-1. During both the simultaneous and successive induction specific rates of synthesis, as well as maximum enzyme levels, were identical with those obtained after independent induction of individual enzymes. As compared with batch cultivation, beta-galactosidase reached the same specific rate of synthesis in the chemostat, whereas the specific rate of synthesis of tryptophanase in the chemostat was up to five times higher.

See more in PubMed

Biochim Biophys Acta. 1951 Nov;7(4):585-99 PubMed

Biochem Biophys Res Commun. 1968 Jun 10;31(5):812-7 PubMed

J Mol Biol. 1967 Aug 14;27(3):495-506 PubMed

J Bacteriol. 1950 Oct;60(4):381-92 PubMed

Folia Microbiol (Praha). 1976;21(6):431-7 PubMed

Activity of beta-galactosidase in soil continuously supplemented with lactose

Catabolite repression during single and multiple induction in Escherichia coli

Effect of cyclic adenosine-3',5'-monophosphate on the simultaneous synthesis of beta-galactosidase and tryptophanase in Escherichia coli

Simultaneous induction of three catabolic enzymes in Escherichia coli