Expanding the horizon of biodiesel production via enzyme engineering

Biodiesel generated from oils and fats composed of fatty acid alkyl esters is a potential substitution for fossil fuels. This alternative fuel has become more prevalent as the demand for sustainable energy increases. Enzymatic transesterification has attracted special attention as an alternative method to conventional chemical processes in biodiesel production as it requires less energy and allows for the easy recovery of glycerol and also compatible with various feedstocks, high specificity, and requires mild reaction conditions. However, limitations such as enzyme production cost, low product yield, and low stability against high temperature and organic solvents in the reaction mixture, have hindered the progress of biocatalysis. Protein engineering has emerged as an important strategy in tailoring enzymes to serve as biocatalysts across a broad range of industrial applications. Recent developments in protein engineering suggest that rational design approaches are more advantageous in lipase engineering, due to easily accessible experimental tools and prior knowledge of the structure and function of lipase. Site-directed mutagenesis has been applied to improve stability, substrate specificity, methanol tolerance, and catalytic efficiency of lipase by the introduction of molecular interactions such as hydrogen bonds and disulfide bridges as well as improved lid flexibility by mutations at the lid or lid swapping. Moreover, site directed mutagenesis provides a targeted approach to introduce specific mutations into gene sequences allowing for the precise modification of amino acid residues for certain characteristics. By strategically designing mutations, researchers can tailor lipases to exhibit the desired characteristics, which are crucial for efficient biodiesel production.

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