title: Characterization of alcohol acyltransferase from olive fruit.
abstract: Alcohol acyltransferase catalyzes the esterification of volatile alcohols with acyl-CoA derivatives to produce volatile esters typically present in the aroma of some fruits. This enzyme was detected in extracts from the pericarp tissues of ripe olive fruits using hexanol and acetyl-CoA as the substrates. Alcohol acyltransferase showed a very low activity level in these fruits, with an optimum pH value at 7.5 and high K(m) values for hexanol and acetyl-CoA. The substrate specificity of this enzyme for various alcohols was also studied. The involvement of the studied enzyme in the biogenesis of the volatile esters present in the aroma of virgin olive oil was discussed.
authors.affiliation: Instituto de la Grasa, CSIC, Av. Padre García Tejero, 4, 41012, Sevilla, Spain. jjsalas@cica.es
authors.forename: Joaquín J
authors.initials: JJ
authors.lastname: Salas
mesh_terms: D000217:Acyltransferases / Q000032:analysis* / Q000378:metabolism; D005638:Fruit / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D031658:Olea / Q000201:enzymology*; D010940:Plant Proteins; D013379:Substrate Specificity
chemical_list: D010940:Plant Proteins; D000217:Acyltransferases; C411082:alcohol acyltransferase, Fragaria ananassa