Abstract
Acyl coenzyme A: alcohol acyltransferase was purified to homogeneity from a strain of Neurospora sp. ATCC 46892 which produces ethyl hexanoate abundantly in the culture broth.1) The apparent molecular weight was approximately 30, 000. This enzyme acted on various acyl coenzyme A's containing more than a four-carbon linear chain, but not on acetyl coenzyme A, n-propionyl coenzyme A, or the branched-chain acyl coenzyme A's that were examined. It also acted on various linear- and branched-chain alcohols tested. The optimum pH was 8.0, and the optimum temperature, 25°C at pH 8.0. The enzyme was stable from pH 3.0 to 9.0 and up to 43°C, maintaining its original activity. The enzyme activity was strongly inhibited by diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride, but not by unsaturated fatty acids.
