Lipase-catalysed tandem Knoevenagel condensation and esterification with alcohol cosolvents

Six lipases were screened for their ability to catalyse the Knoevenagel condensation between benzaldehyde and methyl cyanoacetate. Lipase from porcine pancreas tolerated a variety of functional groups on the aromatic ring, produced the highest yields, and also catalysed transesterification of the product in the presence of an alcoholic cosolvent. We show that, in organic solvents, lipase from porcine pancreas has higher activity for this promiscuous reaction than for naturally occurring esterification catalysis.