Dr Anca Pordea is part of the Bioprocess, Environmental and Chemical Technologies Research Group.
Anca graduated from the National Institute of Applied Research (INSA) in Rouen (France) in 2004, with a Master Degree in Chemical Engineering focused on the synthesis of fine chemicals. She completed her PhD in Neuchâtel (Switzerland), working on the development of enantioselective catalytic reactions by using artificial metalloenzymes, with Prof. Thomas R. Ward. As a postdoc, she worked on the chemical modification of subtilisin in Oxford (UK) and on the development of organocatalysts in Neuchâtel ( Switzerland). She joined the University of Nottingham in 2012 as a lecturer.
The group's scientific interest lays in the design of enzymes for organic chemical transformations, with applications in fine chemical synthesis and in the functionalisation of complex organic molecules. Our research covers the following areas:
- Incorporation of metal-based chemical catalysts into protein scaffolds
- Design of enzymes for non-natural chemical transformations
- Integration of chemical catalysis with enzymatic / whole-cell catalysis
We have expertise in the synthesis and catalytic applications of ligands and metal complexes compatible with proteins, bioconjugation of small molecules to proteins, expression and purification of recombinant enzymes and characterisation of modified metalloproteins.
I teach two modules in the chemical engineering curriculum:
- Separation Processes 1, second year module, autumn semester. We study the design of gas-liquid separation equipment (distillation columns, absorbers); and solid-liquid-gas (dryers). We also look at equipment used in bioseparation trains;
- Advanced Biochemical Engineering, fourth year module, spring semester. We study the design of reactors for enzymatic transformations (kinetics of soluble and immobilised enzymes) and the design of fermenters. Bioseparation equipment for protein purification is also studied.
The development of new and efficient catalysts for the synthesis of complex molecules is an ongoing need in the chemical industry. Both enzymatic and chemical catalysts offer advantages and raise… read more
The development of new and efficient catalysts for the synthesis of complex molecules is an ongoing need in the chemical industry. Both enzymatic and chemical catalysts offer advantages and raise challenges. Enzymes can be engineered to perform useful transformations, but modifications are never too far from the natural world. On the other hand, chemical catalysts offer novel reactivities, but their selectivities are difficult to control. Chemical modification of proteins to introduce chemo-catalytic functionalities within a biomolecule is an exciting tool to expand enzymes' functionality space.
We are interested in combining chemical and enzymatic catalysis, by designing hybrid chemo-enzymatic catalysts to perform reactions that are not common, or are entirely absent in nature. We are also exploring the integration of chemical catalysis with enzymatic / whole-cell catalysis, in catalytic cascades. Current projects include
- chemical modification of zinc-dependent alcohol dehydrogenases with metal catalysts based on second and third row transition metals. We are investigating the change in specificity of the modified ADHs, from ketone to imine reduction;
- introduction of non-natural metalloporphyrins into P450, to catalyse C-H insertions