Biomolecular crystallography of the volatile ester synthesizing enzymes of S. cerevisiae combined with computational protein redesign of its substrate specificity

During the fermentation process yeast produces a huge variety of volatile esters that contribute to the aroma of food products such as beer and wine. These variety of esters are produced by only 6 different enzymes which exhibit substrate promiscuity. Currently no crystal structures are available of any of these enzymes to analyze the molecular recognition between the enzyme substrates and the binding site. Therefore the first goal will be to obtain these crystal structures. Furthermore, we have the genomes of more than 150 industrially used yeast strains and the amount of different esters each one of them can produce. Using biomolecular modelling we will then relate the different structures to the different substrate levels explaining how the small variances in active sites may yield different produced esters. In a final work package, it will then be attempted to redesign the enzyme specificity using a molecular modelling procedure in order to create mutant enzymes that are able to produce a desired ester, without any side products. This process will not only allow us to optimize the protein design workflow method which are recently emerging but may also yield novel enzymes which in the future could have an industrial application for the green synthesis of a desired compound.