Biosketch

Trained in enzymology (PhD in 1998), Marco Fraaije’s research focuses on the discovery and knowledge-based engineering of cofactor-dependent redox enzymes. Through detailed structural and mechanistic studies, new insights into the molecular functioning have been obtained, which has fuelled novel enzyme redesign strategies. In addition, Marco’s research has led to the development of several industrially relevant enzymes. His main current research areas include:

• Enzyme discovery: discovery and functional characterization of novel redox enzymes with emphasis on flavin- and deazaflavin-dependent enzymes;

• Enzyme engineering: a combination of mechanistic studies, structure elucidation and computational analyses & predictions, new insights in enzyme functioning are obtained, leading to effective enzyme engineering;

• Biocatalysis: develop innovative biocatalytic approaches for employing cofactor-dependent enzymes.

Three top publications 2017-2022

1. Guo Y, Alvigini L, ……, & Fraaije MW (2022) Structure- and computational-aided engineering of an oxidase to produce isoeugenol from a lignin-derived compound. Nature Communications 13, 7195; DOI: https://doi.org/10.1038/s41467-022-34912-3

By using structure-based computational predictions, combined with mechanistic studies, a truly novel and industrially applicable biocatalyst was engineered, active on a lignin-derived compound.

2. Tong Y, Lee M, Drenth J & Fraaije MW (2021) Flavin-tag: a facile method for site-specific labeling of proteins with a flavin fluorophore. Bioconjugate Chemistry 32, 1559-1563; DOI: https://doi.org/10.1021/acs.bioconjchem.1c00306

Newly developed method for selective and efficient incorporation of flavins to a short peptide-tag.

3. Aalbers FS, Fürst MJ, ……, & Fraaije MW (2020). Approaching boiling point stability of an alcohol dehydrogenase through computationally-guided enzyme engineering. eLife, 9, e54639; DOI: https://doi.org/10.7554/eLife.54639

Demonstration of the power of computational-assisted enzyme engineering by creating a highly thermostable biocatalyst