Methyl and ethyl cinnamate are aroma volatiles frequently occurring in fruits. Evidence was obtained that the enzymatic transfer of cinnamic acid to endogenous alcohols present in fruits (methanol, ethanol. 1-propanol) depended on energy-rich 1-O-glycosyl esters of cinnamic acid which served as acyl donor molecules. A putative l-O-trans-cinnamoyl-β-D-gluco-pyranose: alcohol cinnamoyltransferase from cape gooseberry (Physalis peruviana L.) was active towards l-O-trans-cinnamoyl-β-D-glucopyranose and l-O-trans-cinnamoyl-β-D-gentio-biose. The enzyme was purified 290-fold by a protocol including ammonium sulphate precipitation, solubilization by Triton X-100, gel permeation and affinity chromatography on conca-navalin A. The acidic glycoprotein (pI = 4.8) most probably is membrane bound. The distribution of alcohol cinnamoyltransferase activity in gel chromatography fractions suggests a native Mrof 75,000. For l-O-trans-cinnamoyl-β-D-glucopyranose, an apparent Kmof 69 was determined. At pH > 6.0, non-enzymatic transesterification superposes the enzymatic transformation.