In nature, enzymes are often assembled into complex structures that are more effective than individual enzymes in converting raw materials into useful products. Many biologically-derived scaffolds have been used for single and multi-enzyme assembly and have shown increased overall reaction rates in one- or two-dimensional configurations. Analogously, we hypothesize that the use of three-dimensional scaffolds could further enhance the performance of biocatalysts. The E2 core of the pyruvate dehydrogenase complex from Bacillus stearothermophilus is a genetically-modifiable 60-mer protein nanocage that is thermally stable at temperatures as high as 70�C. In this talk, we will discuss combining the E2 nanocage with a thermophilic endoglucanase, CelA from Clostridium thermocellum, resulting an enzyme assembly that benefit from both the synergy gained from clustering and stability at more enzymatically favorable high reaction temperatures. This E2-based approach offers a flexible platform upon which multi-enzyme cascade reactions can be assembled and studied at the nanoscale.

Engineering 3D protein scaffolds for biocatalysts assembly

247th National Meeting (2014)

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