Abstract
ω-Transaminases have been immobilized on macrocellular silica monoliths and used as heterogeneous biocatalysts in a continuous flow mode enantioselective transamination reaction. The support was prepared by a sol-gel method based on emulsion templating. The enzyme was immobilized on the structured silica monoliths both by adsorption, and by covalent grafting using amino-functionalized silica monoliths and glutaraldehyde as a coupling agent. A simple reactor set-up based on the use of a heat-shrinkable Teflon tube is presented and successfully used for the continuous flow kinetic resolution of a chiral amine, 4-bromo-α-methylbenzylamine. The porous structure of the supports ensures effective mass transfer and the reactor works in the plug flow regime without preferential flow paths. When immobilized in the monolith and used in the flow reactor, transaminases retain their activity and their enantioselectivity. The solid biocatalyst is also shown to be stable both on stream and during storage. These essential features pave the way to the successful development of an environmentally friendly process for chiral amines production.
Highlights
While the use of enzymes as catalysts in the chemical sector is extremely appealing—especially in the perspective of sustainability—their application in industrially relevant processes is not straightforward
Thisneeded elegantnutriments strategy, alive by feeding them with all the along therequires process.keeping the living organisms alive Here, by feeding them with all the needed nutriments along the we propose the immobilization of a transaminase onprocess
This study shows that such heterogeneous biocatalyst exhibits all the required features for an enzymatic flow process
Summary
While the use of enzymes as catalysts in the chemical sector is extremely appealing—especially in the perspective of sustainability—their application in industrially relevant processes is not straightforward. The use of free enzymes in homogeneous batch processes suffers from severe limitations related to the impossibility to reuse and recover the biocatalysts [1]. One particular challenge is to make them recyclable while maintaining their activity [2]. This is typically achieved by immobilizing the enzymes on an appropriate support—inorganic, biological, polymer or hybrid materials [3,4]. Transaminases are enzymes that catalyze the enantioselective transfer of an amine group from an amine donor to an amino acceptor
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