Range: Table - link mg/L
||Bacteria Escherichia coli
||Lendenmann U, Snozzi M, Egli T. Growth kinetics of Escherichia coli with galactose and several other sugars in carbon-limited chemostat culture. Can J Microbiol. 2000 Jan46(1):72-80. doi 10.1139/w99-113 p.79 table 6PubMed ID10696473
||Dykhuizen, D., and Davies, M. 1980. An experimental model: bacterial specialists and generalists competing in chemostats. Ecology, 61: 1213–1227. DOI: 10.2307/1936839 Stable URL: link
||p.79 caption to table 6(13):"Determined in chemostat culture. Steady-state substrate concentrations (s) were estimated from yield data of two identical chemostat runs with different maltose feed concentrations."
||P.78 left column bottom paragraph:"A comparison of Ks values for individual sugars obtained here (Table 5) with published Michaelis–Menten parameters for uptake of these sugars (Km) or affinity constants for sugar-binding proteins (Kd) (Table 6) show little agreement. Km and Kd values for maltose transport systems were approximately three times higher than Ks for growth. In contrast, Km and Kd values for ribose were 3–5 times smaller than Ks. Only for growth with galactose a clear correlation between the measured Ks value and the high affinity Km and Kd values for the binding-protein system (Mgl) were observed. The range of published Km values for the low-affinity proton-driven galactose permease (GalP) is between 0.7 and 16 mg/L for wild type strains of E. coli (Table 6). For the high-affinity transport system (Mgl) the corresponding value is 0.09 mg/L (Table 6). The Ks value determined in this study for growing cells was similar to the published Km values of the high-affinity galactose transport system, which suggests that during growth in continuous culture, up to a dilution rate of approximately 0.7/h, the binding-protein transport system was mainly responsible for galactose uptake. Unfortunately, [investigators] are not aware of published kinetic data for the utilisation of fructose by E. coli." See notes beneath table