Reference: Traxlmayr MW and Obinger C (2012) Directed evolution of proteins for increased stability and expression using yeast display. Arch Biochem Biophys 526(2):174-80

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Abstract


The expression of recombinant proteins incorporated into the cell wall of Saccharomyces cerevisiae (yeast surface display) is an important tool for protein engineering and library screening applications. In this review, we discuss the state-of-the-art yeast display techniques used for stability engineering of proteins including antibody fragments and immunoglobulin-like molecules. The paper discusses assets and drawbacks of stability engineering using the correlation between expression density on the yeast surface and thermal stability with respect to the quality control system in yeast. Additionally, strategies based on heat incubation of surface displayed protein libraries for selection of stabilized variants are reported including a recently developed method that allows stabilization of proteins of already high intrinsic thermal stability like IgG1-Fc.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't | Review
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Traxlmayr MW, Obinger C
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