Candida antartica lipase A is an enzyme which has received increased attention since the crystal structure was reported in 20081. It is a highly thermostable lipase that shows activity towards bulky substrates such as tertiary alcohols. In contrast to the well-known Candida antartica Lipase B, Lipase displays interfacial activation which is suggested to be due to a flexible region rich in hydrophobic residues, assigned as an active site flap. Our group has previously reported several successful projects on directed evolution of this enzyme for hydrolysis of 2-aryl propionic esters yielding enantiomerically enriched acids.The reverse reaction of hydrolysis, transesterification, is more suited for organic synthesis, since it can be performed in organic solvents and does not require water. This work covers engineering of CalA for improved transesterification/transacylation activity.

Protein engineering of <i>Candida antartica</i> Lipase A for altered performance in organic synthesis

245th National Meeting (2013)

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Protein engineering of Candida antartica Lipase A for altered performance in organic synthesis