Glucose and acetate influences on the behavior of the recombinant strain Escherichia coli HB 101 (GAPDH).

This study highlights data about the production of a recombinant protein (glyceraldehyde-3-phosphate dehydrogenase) by E. coli HB 101 (GAPDH) during batch and fed-batch fermentations in a complex medium. From a small number of experiments, this strain has been characterized in terms of protein production performance and glucose and acetate influences on growth and recombinant protein production. The present results show that this strain is suitable for recombinant protein production, in fed-batch culture 55 g L-1 of biomass and 6 g L-1 of GAPDH are obtained. However this strain, and especially GAPDH overproduction is sensitive to glucose availability. During fermentations, maximum yields of GAPDH production have been obtained in batch experiments for glucose concentration of 10 g L-1, and in fed-batch experiments for glucose availability of 10 g h-1 (initial volume 1.5 L). The growth of the strain and GAPDH overproduction are also inhibited by acetate. Moreover acetate has been noted as an activator of its own formation.