 This work is a collaboration between the advanced centre for my chemical engineering at UCL and the School of Life Sciences at the University of Warwick. We have successfully assessed and then demonstrated the benefits of microbial cell engineering in the context of whole integrated processing using ultra-scale down tools devised at UCL. This allowed a rapid turnaround of process data to inform early stage development and optimisation of the engineered cells. Here we investigated the processability of E. coli cells, which over expressed and then used an alternative secretion pathway known as twin arginine translocation pathway to secret the protein. This pathway is potentially attractive commercially as it can export folded soluble proteins of interest into the periplasm of the cells. In the results you see we begin by comparing fermentation growth profiles of three coli strains. We'll type MC4100, MC4100 over expressing the TAP pathway 20 fold and cells with the TAP machinery disabled entirely. We show that there's no effect from TAP over expression. We then compared the same strains but now exporting protein into the periplasmic space. The best growth rate occurred when cells over expressed the TAP pathway a result of removing the capacity bottleneck. Overall we saw a 25% increase in growth rates. Using Western blots to detect the quantity of protein exported we see that the world type TAP pathway showed poor FHUD accumulation reaching a periplasmic maximum of only half a meg per litre of growth medium. In contrast over expressed in TAP pathway gave a 40 fold higher periplasmic accumulation. Now these performance improvements are useless if cells are less robust to downstream processing and this is why we analyse their robustness. We show that the integrative cells over expressing TAP was conserved and it's not only intact cells that we need to be concerned about. Further down the DSP route we need to remove spheroplasts from the process stream which are cells which have a selectively ruptured outer membrane to release the periplasmic protein. Here we show similar robustness between the strains. Finally a scaled-down model of continuous disk duck centrifugation predicted clarifications in excess of 90% for both intact cells and spheroplasts. Cells over expressed in the TAP pathway performed comparably to cells with a world type system. Overall our work shows that engineering E.coli cells to over express the TAP pathway not only allows for greater yield of soluble protein in the periplasa but also this can be achieved without compromising downstream processing performance. We would like to acknowledge the financial support of the Bioprocessing Research Industry Club in the UK for their financial support.