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Francesca Paradisi

Associate Professor in Biocatalysis and Enzyme Engineering, Faculty of Science

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Biography

Dr. Paradisi completed an MSc in Organic Chemistry from the University of Bologna in 1998 under the supervision of Prof. Cainelli. In 2002 she completed her PhD at the same institution with a thesis on the synthesis of non-natural amino acids via diketopiperazine scaffolds. She joined the group of Prof. Engel at University College Dublin as Post-Doctoral Fellow where she remained until 2005 and developed several projects mainly focused on amino acid dehydrogenases and their applications in the synthesis of non-natural amino acids. She joined Enzolve Technologies in 2005, a spin-off company of UCD where she worked on the use of mutant dehydrogeanse enzymes for neonatal screening of metabolic disorders. in 2006 she was appointed Lecturer in Chemical Biology at the Centre for Synthesis and Chemical Biology in UCD (fix term), and in 2009 she got a tenured lectureship at the UCD School of Chemistry. She was promoted in 2014 to Senior Lecturer and in 2016 she took up the position of Associate Professor in Biocatalysis and Enzyme Engineering in the School of Chemistry at the University of Nottingham.

Research Summary

We have a keen interest in the development of alternative biocatalysts for synthetic and industrial applications. Predominantly our research focuses on the characterization and evolution of enzymes… read more

Selected Publications

Current Research

We have a keen interest in the development of alternative biocatalysts for synthetic and industrial applications. Predominantly our research focuses on the characterization and evolution of enzymes originating from extremophilic organisms, both archaea and bacteria, which thrive in high-salt environments or below freezing temperatures. Currently we are working with a variety of enzymes encompassing oxido-reductases, transaminases, and hydrolases. The environmental adaptation of the organisms translates into unique enzymatic properties such as high tolerance to organic solvents and broad substrate scope.

To maximize enzymatic stability we have developed tailored immobilization strategies which allow us to use (and re-use) the enzymes in batch as well as in flow-systems.

Our research is highly interdisciplinary with a number of collaborators in the US as well as Europe, and together we are looking at the assembly of semi-synthetic enzymes with enhanced biocatalytic properties.

We have a smaller synthetic stream in our lab which is dedicated to the incorporation of rigid, non-natural amino acids into peptidomimeticts which have demonstrated superior anti-cancer activity.

See our group website www.paradisiresearch.com for more information on opportunities, our research and news

School of Chemistry

University Park Nottingham, NG7 2RD

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