초록
<▼1><P>Bacterial microcompartments (BMCs) enhance the breakdown of metabolites such as 1,2-propanediol (1,2-PD) to propionic acid. The encapsulation of proteins within the BMC is mediated by the presence of targeting sequences. In an attempt to redesign the Pdu BMC into a 1,2-PD synthesising factory using glycerol as the starting material we added N-terminal targeting peptides to glycerol dehydrogenase, dihydroxyacetone kinase, methylglyoxal synthase and 1,2-propanediol oxidoreductase to allow their inclusion into an empty BMC. 1,2-PD producing strains containing the fused enzymes exhibit a 245% increase in product formation in comparison to un-tagged enzymes, irrespective of the presence of BMCs. Tagging of enzymes with targeting peptides results in the formation of dense protein aggregates within the cell that are shown by immuno-labelling to contain the vast majority of tagged proteins. It can therefore be concluded that these protein inclusions are metabolically active and facilitate the significant increase in product formation.</P></▼1><▼2><P><B>Highlights</B></P><P>•<P>Fusion of BMC targeting peptides to enzymes has a variable effect on activity.</P>•<P>Tagged enzymes for 1,2-propanediol synthesis are localised to a BMC.</P>•<P>BMC-targeted proteins localised within the BMC are protected from proteases.</P>•<P>TEM reveals tagged enzymes form large intracellular protein aggregates.</P>•<P>Strains with enzyme aggregates are shown to have enhanced 1,2-propanediol production.</P></P></▼2>