Partial purification and some properties of alcohol acyltransferase from strawberry fruits
1993
Perez, A.G. | Sanz, C. | Olias, J.M.
The enzyme system concerning volatile ester formation in strawberry Fragaria ananassa X Duchessne var. Chandler was studied. Protein with alcohol acyltransferase activity was purified about 29-fold from Chandler strawberry fruits by ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography. The enzyme activity had a pH optimum of 8.0 and an optimum temperature of 35 degrees C. The apparent Mr estimated by gel filtration was 70 00. The enzyme was tested for its preference in using different acyl-CoAs and alcohols. Maximum activity was obtained using acetyl-CoA and hexyl alcohol as substrates. A clear correlation was observed between substrate preference and volatile eaters present in strawberry var. Chandler.
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