Enzymes in Biocatalysis

Over the past decades enzymes established as a new class of catalysts in the field of modern synthetic chemistry und continue to gain in importance through discovery of new applications and development of even more efficient systems. The tremendously fast progression of these ꞌꞌnature’s toolsꞌꞌ has numerous reasons of which the uniqueness of the catalyzed reactions, progresses in the field of molecular biology and protein science as well as development of convenient assay systems are probably the most striking. Enzymes catalyze transformations and offer selectivities that – though synthetically desired - are hard or impossible to achieve through traditional chemical methods. In addition to the often studied and frequently applied enzyme family of hydrolases, especially oxidoreduktases, transferases and lyases are the center of attention for synthetic applications. By including the possibility of biocatalytic steps in the retrosynthetic analysis of numerous natural product syntheses, we establish novel biocatalytic applications und show how biocatalysis can complement classical chemical tools. In our projects we focus on both, the ꞌꞌwell-triedꞌꞌ biocatalysts such as lipases and alcohol dehydrogenases as well as ꞌꞌmodernꞌꞌ catalysts such as enoate-reductases, aldolases, monooxygenases, glucosidases and laccases and this list is continuously expanded due to new synthetic challenges.

In addition to the characterization and application of these biocatalysts, the production of these enzymes is another central task in the IBOC. Both classical methods and innovative approaches such as optogentic “switches” for light-mediated control of gene expression in yeast and other host organisms were established for the expression of genes encoding relevant enzymes.