By introducing nine mutations simultaneously, the active site of the enzyme Candida antartica Lipase A (CalA) was enlarged. The resculptured biocatalyst is environmentally friendly, fast, highly enantioselective and tailor-made for our needs.    The applied combinatorial mutagenesis approach allows for fine tuning of the active site for a specific organic transformation. In this way, the enzyme substrate binding pocket is designed to convert only one enantiomer of a racemic substrate into product. 

Radical resculpturing of an enzyme active site: Tailoring the substrate pocket

243rd National Meeting (2012)

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