Abstract
The widerapplications of these DKR procedures in organic synthesis,however, can be hampered by the narrow specificity, moder-ate enantioselectivity, and low activity of the enzymeemployed. Therefore, it is of great importance to develop ahighly active enzyme having high enantioselectivity toward awide range of substrates for DKR. We herein report thationic-surfactant-coated Burkholderia cepacia lipase(ISCBCL) has great potential as such an excellent enzyme.Commercially available Burkholderia cepacia lipase(BCL; brand names: Lipase PS and Lipase PS-C) displayssignificantly lower activity than Candida antarctica lipase B(CALB; brand name: Novozym 435) (Table 1, entries 1–3);the latter has been most frequently employed in the metallo-enzymatic DKR. Fortunately, we have developed a practicalapproach for enhancing its activity dramatically. In a typicalprocedure, buffer-free soluble BCL (24% protein),
Published Version
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