Alice Pedroni, PhD student at TU Delft

👩‍🔬 I'm Alice Pedroni, a PhD student at TU Delft who will be working on W-enzymes in the research group of Frank Hollmann and Caroline E. Paul. My background is mainly in chemistry, but enzymes have always amazed me with their ability to perform chemically challenging reactions under mild conditions.

💡 Currently, industry doesn't use enzymes to convert carboxylic acids to aldehydes and alcohols because the naturally occurring enzymes require expensive co-substrates such as ATP and NADPH. However, the existence of W-enzymes, which can carry out this conversion efficiently using H2 as an energy source, opens up possibilities for various applications, such as the reduction of CO2 to formic acid or the conversion of benzene derivatives. By using these enzymes with hydrogen power, it's possible to create a process that converts waste materials into useful compounds such as alcohols and aldehydes for cosmetics and flavours.

🔬 Within the W-BioCat project, I will investigate the biocatalytic potential of these W-enzymes. The substrate scope will be systematically characterised to identify the optimal reaction conditions for each substrate and for further scale-up. In addition, new substrates and new reactions catalysed by W-enzymes will be identified to increase their versatility in biotechnological applications.

Caroline E.Paul's group

The team led by Caroline E. Paul in the Biocatalysis section at Delft University of Technology explores the synthetic potential of enzymes, specifically reductases, dehydrogenases and transferases via cofactor engineering, and also takes a retrosynthetic approach to produce valuable target molecules.

In particular, we have characterised and applied several key flavin-dependent monooxygenases and reductases in biocatalytic reactions to obtain high-value products with new C-O, C-N, C-C and C-halogen bonds: hydroxylases for selective aromatic hydroxylation, styrene monooxygenases for asymmetric epoxidation (with further nucleophilic reactions) and sulfoxidation, halogenases for selective halogenation, #ene reductases for asymmetric reduction of alkenes (including coupled to amine dehydrogenases to obtain chiral amines). These applications demonstrated the use of redox enzymes in industrially relevant chemical syntheses for fragrance and pharmaceutical industries. A recent example is on the synthesis of the (R)-citronellal, a precursor for (–)-menthol.

https://lnkd.in/d689VTGb

In W-Biocat, we are interested in aromatic reductions and together we will develop a platform technology to dearomatize aromatic compounds. The current state-of-the-art involves stoichiometric amounts of pyrophoric sodium in liquid ammonia for Birch reduction of arenes. With W-dependent Birch reductases, we will enable biocatalytic Birch reductions at scale to make our chemical industry safer.

Tunable Production of (R)- or (S)-Citronellal from Geraniol via a Bienzymatic Cascade Using a Copper Radical Alcohol Oxidase and Old Yellow Enzyme | ACS Catalysis

https://pubs.acs.org/doi/10.1021/acscatal.1c05334

Deborah Boes, PhD student at TU Delft

My name is Deborah Boes and I am a PhD student in the group of Peter-Leon Hagedoorn. I have a background in Biocatalysis and immunology by obtaining a double master degree Life Science and Technology at the TU Delft and Leiden University. After that I have worked for a year in industry, where I focused on differentiating human iPSCs into other cells types, before I started my PhD at TU Delft.

Within the W-BioCat project, my research focuses on expressing tungsten-containing enzymes in an industrial workhorse micro-organism, such as E. coli, to be able to produce these enzymes on a large scale. This requires overcoming several bottlenecks in the biosynthesis of the W-cofactor.