Increasing Recombinant Protein Production in E. coli by an Alternative Method to Reduce Acetate

Since the development of recombinant DNA technology (Cohen et al., 1973), it became possible to express heterologous genes in proor eukaryotic hosts, i.e. genes which they naturally not express. This development enabled the production of all kinds of products of which the high-added value recombinant proteins, became increasingly important and as such boosted biopharmaceutical and industrial enzyme applications. Up to now, the FDA (Food and Drug Administration) and EMEA (European Medicines Agency) have licensed the application of more than 150 recombinant proteins to be used as a pharmaceutical (Ferrer-Miralles et al., 2009). Global sales of biopharmaceuticals are estimated to account for US$70–80 Billion today (Walsh, 2010). Industrial enzymes (e.g. proteases, amylases, lipases, cellulases, pullulanases, pectinases) are used in various industrial segments and the industrial enzyme market is still expanding, estimated to reach US$ 3.74 Billion by the year 2015 (Global Industry Analysts, 2011). To date, the majority of this industrial enzyme market value is generated by recombinant processes (Hodgson, 1994; Demain & Vaishnav, 2009).