Abstract
Lipase catalyzed transesterification between tri-n-butyrin (1) and substituted benzyl alcohols (2) gave the corresponding benzyl n-butyrates (3), which were subsequently purified by silicic acid chromatography using n-hexane containing 30vol% benzene. Six out of thirteen lipases which catalyzed the hydrolysis of triglycerides with short chain fatty acid residues, showed good activities for transesterification. The reactivity of (2) in (1) varied according to enzyme source. Solvent effect was examined and lipase activity was different for each solvent. From the present results, those reactions are applicable to the syntheses of the benzyl esters of fatty acids.
