期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 50, 期 14, 页码 4031-4036出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf011460u
关键词
strawberry fruit; aroma; ester biosynthesis; alcohol acyltransferase; cultivar variation
The substrate specificity of alcohol acyltransferase (AAT) enzymes from different strawberry varieties was studied. Proteins with AAT activity from fruits of Fragaria x ananassa Duch. cv. Oso Grande were purified to apparent homogeneity and used for kinetic studies with different straight-chain alcohols and acyl-CoAs. K-m values obtained for Oso Grande enzyme with six different alcohols, using acetylCoA as cosubstrate, decreased with increasing length of the alcohol chain. In similar experiments the increase in the acyl-CoA carbon chain was also found to be correlated with a higher substrate specificity. Heptanol (K-m = 0.73 mM) and hexanoyl-CoA (K-m = 0.41 mM) were the best substrates for Oso Grande AAT. Comparative catalytic studies were carried out with AAT partially purified extracts from the wild type Fragaria vesca and five commercial strawberry varieties:. Tudnew, Carisma, Camarosa, Sweet Charlie, and Eris. The specificities of these enzymes toward five selected alcohols and acyl-CoAs reflected interesting cultivar differences.
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