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

被引:78
作者
PEREZ, AG [1 ]
SANZ, C [1 ]
OLIAS, JM [1 ]
机构
[1] CSIC,INST GRASA & DERIVADOS,UEI FISIOL & TECNOL POST RECOLECC,APDO 1078,E-41012 SEVILLE,SPAIN
关键词
D O I
10.1021/jf00033a021
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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 M(r) estimated by gel filtration was 70 000. 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 esters present in strawberry var. Chandler.
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页码:1462 / 1466
页数:5
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