Mn. Coello et al., Effect of the growth rate on the enzymatic activities of L-lysine-producing cells of Corynebacterium glutamicum, WORLD J MIC, 17(4), 2001, pp. 337-341
The activity of 6-phosphogluconate dehydrogenase, aspartate kinase and phos
phoenolpyruvate carboxylase has been studied at different dilution rates in
aerobic continuous culture of Corynebacterium glutamicum. 6-Phosphoglucona
te dehydrogenase and aspartate kinase reached their maximum values at the l
ower dilution rates (0.02-0.06 h(-1)), when L-lysine was produced. The phos
phoenolpyruvate carboxylase activity seemed to be independent of metabolite
synthesis. The production of L-lysine was also studied in non-growing cell
s in batch cultures. In these conditions, statistical analysis revealed sig
nificant differences in L-lysine titres when glucose or gluconic acid were
used as carbon sources. Higher L-lysine concentration obtained with gluconi
c acid was found to be associated with a high 6-phosphogluconate dehydrogen
ase activity.