Here, we present the immobilization of TA on cylindrical silica monoliths that are particularly appropriate for the design of continuous flow reactors. The monoliths are prepared by a bottom-up sol-gel method based on emulsion templating. They minimize pressure drop, ensure a plug flow regime, and are easy to manipulate. Their surface is functionalized to bring epoxy or amino groups on the surface, allowing to anchor the enzyme. A simple flow reactor featuring covalently immobilized TA (ATA-117 from Codexis) is presented as a proof-of-concept. The transamination of pyruvate with racemic 4-bromo-α-methylbenzylamine (BMBA) to produce bromoacetophenone (BAP) was used as a model reaction (kinetic resolution). We show how the immobilization of the enzyme – and therefore the catalyst performance – can be optimized by tuning parameters of the monolith surface functionalization.
van den Biggelaar, L., Gauchet, A., Khan, M. S., Soumillion, P., & Debecker, D. (2019). Flow mode enantioselective transamination using transaminase enzymes immobilized in a macroporous silica monolith. International Symposium on Green Chemistry, La Rochelle, France. https://hdl.handle.net/2078.5/124848