Preparative Production of Optically Active Esters and Alcohols Using Esterase-Catalyzed Stereospecific Transesterification in Organic Media

Article abstract of DOI:10.1021/ja00321a033

A novel enzymatic approach to the production of optically active alcohols and esters from racemates is developed.It involves the use of esterase catalyzed transesterifications carried out in biphasic aqueous-organic mixtures.Water-insoluble substrates constitute the organic phase, while the enzyme is located in the aqueous phase.Since the fraction of the latter phase can be made very low, such an arrangement solves the problem of both the competition of an alcohol (the nucleophile) with water in the enzymatic reaction and poor solubility of most organic esters and alcohols in water.By use of porous supports (Sepharose or Chromosorb) filled with aqueous solutions of hog liver carboxyl esterase as a stereoselective catalyst and methyl propionate as a matrix ester, the following optically active alcohols and their propionic esters were produced on a preparative scale: 3-methoxy-1-butanol, 3-methyl-1-pentanol, 3,7-dimethyl-1-octanol, and β-citronellol.To overcome a rather narrow substrate specificity of hog liver carboxyl esterase, a nonspecific lipase from yeast (Candida cylindracea) also was employed as a stereoselective transesterification catalyst.Using an aqueous solution of this enzyme confined to the pores of Chromosorb and tributyrin as a matrix ester, we have prepared gram amounts of the following optically active alcohols and their butyric esters: 2-butanol, sec-phenethyl alcohol, 2-octanol, 1-chloro-2-propanol and 2,3-dichloro-1-propanol (subsequently nonenzymatically converted to optically active propylene oxide and epichlorohydrin, respectively), 6-methyl-5-hepten-2-ol, and 1,2-butanediol.