Linked Life Data

15137868

Source:http://linkedlifedata.com/resource/pubmed/id/15137868

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2004-5-12
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-8561
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3155-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Characterization of alcohol acyltransferase from olive fruit.
pubmed:affiliation
Instituto de la Grasa, CSIC, Av. Padre García Tejero, 4, 41012, Sevilla, Spain. jjsalas@cica.es
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't