This week’s featured article is from the group of Roland Furstoss and is entitled Preparative scale Baeyer-Villiger biooxidation at high concentration using recombinant Escherichia coli and in situ substrate feeding and product removal process
Enzymes can be very useful catalysts in organic synthesis as they tend to have excellent enantio- and regioselectivity. The enzyme used for this reaction is cyclohexanone monooxygenase (CHMO) from A. calcoaceticus. In this method both the starting material and the product are adsorbed on a resin so that neither build up in the reaction medium, and they can be effectively removed once the reaction is complete.
Other related methods described in Nature Protocols are listed here:
Here, an example of an enzyme combination used is: E. coli K-12 sialic acid aldolase, NmCSS, multifunctional P. multocida sialyltransferase and P. damsela 2,6-sialyltransferase
Pyruvate aldolases in chiral carbon–carbon bond formation
The enzyme is 2-Keto-3-deoxy-6-phosphogluconate aldolase (KDPG)
High-throughput screening of activity and enantioselectivity of esterases
In this protocol the objective was to screen esterases (or other hydrolases) produced after random mutagenesis to determine their substrate specificity and enantioselectivity. The idea being to “optimize” enzymes for specific reactions.
Immobilization of enzymes on heterofunctional epoxy supports
Attaching an enzyme to a solid support is advantageous, because (1) it means that it can easily removed from the reaction medium once the reaction is complete and (2) the immobilised enzyme is pinned into a more rigid conformation making it so that its function is less sensitive to temperature, pH and the presence of organic solvent.
