Lipase kinetic enantiomeric resolution of 1-heteroarylethanols

Tetrahedron: Asymmetry 2016, 27 (7-8), 341‑345

DOI: 10.1016/j.tetasy.2016.02.012

Kucher O. V.; Kolodyazhnaya A. O.; Smolii O. B.; Nazarenko N. K.; Kubyshkin V.; Mykhailiuk P. K.; Tolmachev A. A.

The use of lipases offers a simple and straightforward method toward various chiral secondary alcohols. Here we examined the lipase resolution of 1-heteroarylethanols. Racemic substrates were subjected to a two step resolution strategy. The difference between the substituent sizes around the chiral fragment allowed the successful isolation of the (S)-alcohols with assistance of the Burkholderia cepacia lipase (ee ⩾ 96%). The (R)-isomers were obtained after hydrolysis of the enantioenriched O-acetylated alcohols either with Candida antarctica lipase B or with potassium carbonate. The performance of the latter step was found to be substrate dependent.

Lipase kinetic enantiomeric resolution of 1-heteroarylethanols