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Develops a system using yeast surface display to bind and degrade petroporphyrins in crude oil, addressing a challenge in the petroleum industry. This innovative approach aims to facilitate the removal of these compounds, which can foul catalyst beds and increase refining costs. By evolving heme oxygenase (hHO-1) with a directed evolution system, the study enables screening of variants that efficiently target petroporphyrins. The successful display and evolution of hHO-1 on yeast surface show promising results in potentially finding solutions to the petroporphyrin issue in oil refining.
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Engineering Proteins for Facile Removal of Petroporphyrins from Crude Oil Reza A. Ghiladi, Department of Chemistry, North Carolina State University, Raleigh NC 27695-8204 Petroporphyrins are found in all fossil fuels and pose a significant challenge to the petroleum industry as their degradation results in the fouling of the precious-metal catalyst beds utilized in oil refining, thus increasing the cost of petroleum products and/or making certain sources of oil unusable. While removal of petroporphyrins is a conceptually easy solution to this problem, the challenge is that there are no known petroporphyrin-specific binding materials or degradation catalysts to accomplish this. Our primary focus has been the development of a functional Yeast Surface Display (YSD) directed evolution system to evolve heme oxygenase (hHO-1) to specifically bind and catalytically degrade petroporphyrins to facilitate their removal from crude oil. To that end, we have successfully displayed hHO-1 on the surface of yeast, confirmed these results using Fluorescence Activated Cell Sorting (FACS), and employed error prone PCR to evolve hHO-1. Our approach now enables rapid library screening of hHO-1 variants that will be evolved to bind, or catalytically degrade, a variety of petroporphyrins. hHO-1 FACS Evolved hHO-1 YSD of hHO-1
