Yeast cell surface display for lipase whole cell catalyst and its applications

• This review summarized the matching rule of lipase surface display technique.
• Some novel strategies were evaluated to improve the lipase whole cell catalyst.
• Applications of lipase whole cell catalyst based on surface display technique were addressed.
• Conclusions and prospects of lipase whole cell catalyst were put forward.

The cell surface display technique allows for the expression of target proteins or peptides on the microbial cell surface by fusing an appropriate protein as an anchoring motif. Yeast display systems, such as Pichia pastoris, Yarowia lipolytica and Saccharomyces cerevisiae, are ideal, alternative and extensive display systems with the advantage of simple genetic manipulation and post-translational modification of expressed heterologous proteins. Engineered yeasts show high performance characteristics and variant utilizations. Herein, we comprehensively summarize the variant factors affecting lipase whole cell catalyst activity and display efficiency, including the structure and size of target proteins, screening anchor proteins, type and chain length of linkers, and the appropriate matching rules among the above-mentioned display units. Furthermore, we also address novel approaches to enhance stability and activity of recombinant lipases, such as VHb gene co-expression, multi-enzyme co-display technique, and the micro-environmental interference and self-assembly techniques. Finally, we represent the variety of applications of whole cell surface displayed lipases on yeast cells in non-aqueous phases, including synthesis of esters, PUFA enrichment, resolution of chiral drugs, organic synthesis and biofuels. We demonstrate that the lipase surface display technique is a powerful tool for functionalizing yeasts to serve as whole cell catalysts, and increasing interest is providing an impetus for broad application of this technique.

The displaying structural units of surface display system, including target protein, anchor protein and host cell, as well as two ways of the fusion between target protein and anchor protein. Sometimes histidine acid (HA) tag was added with the gene C terminal of target protein in order to purify the protein.Figure optionsDownload as PowerPoint slide