Gschaedler A, Thi Le N, Boudrant J
Laboratoire des Sciences du Génie Chimique, CNRS, ENSAIA, Vandoeuvre-les-Nancy, France.
J Ind Microbiol. 1994 Jul;13(4):225-32. doi: 10.1007/BF01569753.
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.
本研究突出了大肠杆菌HB 101（甘油醛-3-磷酸脱氢酶，GAPDH）在复杂培养基中的分批发酵和补料分批发酵过程中重组蛋白（甘油醛-3-磷酸脱氢酶）的生产数据。通过少量实验，已对该菌株在蛋白质生产性能以及葡萄糖和乙酸盐对生长和重组蛋白生产的影响方面进行了表征。目前的结果表明，该菌株适合用于重组蛋白生产，在补料分批培养中可获得55 g L-1的生物量和6 g L-1的GAPDH。然而，该菌株，尤其是GAPDH的过量生产对葡萄糖的可利用性敏感。在发酵过程中，分批实验中葡萄糖浓度为10 g L-1时以及补料分批实验中葡萄糖供应速率为10 g h-1（初始体积1.5 L）时，可获得GAPDH生产的最大产量。该菌株的生长和GAPDH的过量生产也受到乙酸盐的抑制。此外，乙酸盐已被认为是其自身形成的激活剂。
