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

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1993年 / 41卷 / 09期

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.

引用

页码：1462 / 1466

页数：5

共 26 条

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