To pave the way for an industrial process, we need to modify ''E.&nbsp;coli'' to produce high concentrations of glycogen. It has previously been shown that a knockout of one glycogen degradation enzyme leads to the accumulation of glycogen in the cells (Fig. 2)<ref name="2"> Alonso-Casaju´s Nora et al. 2006. Glycogen Phosphorylase, the Product of the glgP Gene, Catalyzes Glycogen Breakdown by Removing Glucose Units from the Nonreducing Ends in Escherichia coli<ref name="2" />. To further improve the production of glycogen in ''E.&nbsp;coli'', we approached this problem in our project in two ways:  

{{Team:Aachen/DoubleFigure|Aachen_glycogen metabolism adjusted.png|Aachen Glyogen accumulation of ∆glgP.png|title1= Figure 1 - Glycogen enzymes in ''E. coli'' |title2=Figure 2 - ∆''glgP'' ''E. coli'' cells|subtitle1=GlgC forms ADP-glucose from ATP and glucose-1-phosphate. The ADP-glucose is then used by GlgA which also serves as the starting particle through autophosphorylation. GlgB adds branches to the existing chains forming α-1,6-glycosidic bonds. GlgX degrades glycogen by cleaving α-1,6-glycosidic bonds whereas GlgP removes glucose units from the end of linear chains.|subtitle2= ''E. coli'' cells lacking ''glgP'' are shown. They accumulated glycogen in granules. By Alonso-Casaju´s Nora et al. 2006 <ref name="2">Alonso-Casaju´s Nora et al. 2006. Glycogen Phosphorylase, the Product of the glgP Gene, Catalyzes Glycogen Breakdown by Removing Glucose Units from the Nonreducing Ends in Escherichia coli<ref name="2" />|size=large}}