Protein engineering has developed in the past decade to a highly important technology as it is a useful tool to create enzymes with desired properties but also helps to understand how proteins evolved and how they function. Whereas initially rational protein design based on detailed analysis of three-dimensional structures was the method of choice, directed evolution became an important alternative. In this lecture, the principle strategies and current challenges in protein engineering will be highlighted. We used an „in silico neutral drift“ based on the analysis of >2.800 sequences of enzymes from the a/b-hydrolase fold family to yield enzyme variants with substantially enhanced thermostability, enantioselectivity and altered substrate range. Novel transaminases with distinct selectivities were identified by a detailed in silico analysis.
Uwe T. Bornscheuer (*1964 in Frankenhain) is professor for biotechnology and enzyme catalysis at the Institute for Biochemistry at the University of Greifswald. He studied chemistry at the University of Hannover and received several stipends of the ‘Fonds der Chemischen Industrie’ (FCI, Germany), fellowships of the Japanese Society for the Promotion of Science (JSPS) and in 2008 the Biocat Award. His main research interest is the application of biocatalysts in the synthesis of optically active compounds and in lipid modification.
Moderation: Professor Dr. Barbara M. Bröker