Abstract
The asymmetric reduction of ketones by oxido-reductases is often limited by poor solubility of the substrates. We have explored the use of heptakis-(2,6-di-O-methyl)-β-cyclodextrin (DIMEB) to resolve this problem. The solubility of the poorly water soluble 2-acetylnaphthalene and the corresponding 1-(2-naphthyl)ethanol in DIMEB buffer was up to 147 fold higher than in buffer alone. The dissociation constants (KDiss) of the DIMEB complexes and the kinetics of the asymmetric reduction were determined. Batch reductions reached high yields with excellent enantioselectivity and were simulated with good agreement using the values of KDISS and the kinetic parameters. The oxido-reductases used for preparative reductions, Candida parapsilosis carbonyl reductase (CPCR) and formate dehydrogenase (FDH), showed no DIMEB-induced deactivation.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call