PARTIAL-PURIFICATION AND SOME PROPERTIES OF ALCOHOL ACYLTRANSFERASE FROM STRAWBERRY FRUITS

The enzyme system concerning volatile ester formation in strawberry Fr agaria ananassa x Duchessne var. Chandler was studied. Protein with al cohol acyltransferase activity was purified about 29-fold from Chandle r strawberry fruits by ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography. The enzyme activity had a pH optim um of 8.0 and an optimum temperature of 35-degrees-C. The apparent M(r ) estimated by gel filtration was 70 000. The enzyme was tested for it s preference in using different acyl-CoAs and alcohols. Maximum activi ty was obtained using acetyl-CoA and hexyl alcohol as substrates. A cl ear correlation was observed between substrate preference and volatile esters present in strawberry var. Chandler.