Lipase-catalyzed kinetic resolution of 1-(1,3-benzothiazol-2-ylsulfanyl)propan-2-ol with antifungal activity: a comparative study of transesterification versus hydrolysis

A study of chemoenzymatic synthesis of both enantiomers of 1-(1,3-benzothiazol-2-ylsulfanyl)propan-2-ol was carried out. Several commercially available lipase preparations were tested as biocatalysts in the kinetic resolution process of target compound by enantioselective transesterification and/or hydrolysis. CAL-B (Novozym 435) was found to be the optimal catalyst. The lipase-mediated hydrolysis approach appeared to be superior to the transesterification reaction. Absolute configuration of the obtained alcohol was postulated, applying modified Mosher's methodology. The inhibitory activity of the synthesized benzothiazole derivatives against pathogenic fungi was checked.