Now, a team of researchers from the University of Illinois at Urbana-Champaign and the Universite Paul Sabatier in Toulouse, France, has developed a microreactor that efficiently regenerates cofactors through enzyme-catalyzed reactions.
"Enzymes are nature's catalysts, but in some cases, enzymes can not prompt a speedy chemical reaction," said Paul Kenis, a professor of chemical and biomolecular engineering at Illinois and a researcher at the Beckman Institute for Advanced Science and Technology. "In those cases, one or more cofactors are required."
By continuously regenerating the required cofactors, the microreactor enables the desired biocatalytic processes. Kenis and his colleagues describe their work in a paper that has been accepted for publication in the Journal of the American Chemical Society, and posted on its Web site.
The microreactor uses a Y-shaped microfluidic channel in which two liquid streams (a reactant stream and a buffer stream) merge and flow laminarly between two electrodes without mixing. By adjusting the flow rates of the two streams, the researchers can focus the reactant stream close to the cathode, and a normally unfavorable reaction equilibrium is driven into the desired direction of cofactor regeneration.
"In large batch reactors, a spontaneous reverse reaction prevents the regeneration of essential cofactors," Kenis said. "The absence of a bulk phase in our microreactor prevents the unwanted reverse reaction from occurring, while permitting continuous operation."
Using their microreactor, the researchers performed a model biocatalytic process by converting an achiral substrate (pyruvate) into a chiral product (L-lactate), using lacta
Source:University of Illinois at Urbana-Champaign