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Long-term storage of Pink Lady apples modifies volatile-involved enzyme activities: consequences on production of volatile esters
Villatoro Gonzàlez, Carmen; Echeverría Cortada, Gemma; Graell i Sarle, Jordi; López Fructuoso, Mª Luisa; Lara Ayala, Isabel
Pink Lady apples were harvested at commercial maturity and stored at 1 °C and 92% relative humidity under either air or controlled atmosphere conditions (2 kPa O2:2 kPa CO2 and 1 kPa O2:1 kPa CO2) for 27 weeks. Data on the emission of volatile compounds and on the activity of some related enzymes in both skin and flesh tissues were obtained during subsequent shelf life at 20 °C. Major effects of storage atmosphere and poststorage period were observed on the emission of volatile esters and their precursors. Changes in the production of volatile esters were partly due to alterations in the activity of alcohol o-acyltransferase, but the specific esters emitted by fruit after storage also resulted largely from modifications in the supply of the corresponding substrates. Samples stored under air were characterized by higher availability of acetaldehyde, whereas those stored under CA showed enhanced emission of the alcohol precursors ethanol and 1-hexanol (2 kPa O2) and 1-butanol (1 kPa O2), with accordingly higher production of ethyl, hexyl, and butyl esters. Multivariate analysis revealed that a large part of the observed differences in precursor availability arose from modifications in the activity of the enzymes considered. Higher pyruvate decarboxylase activity in air-stored fruit possibly accounted for higher acetaldehyde levels in these samples, while storage under 1 kPa O2 led to significantly decreased lipoxygenase activity and thus to lessened production of 1-hexanol and hexyl esters. Low acetaldehyde availability together with enhanced hydroperoxide lyase and alcohol dehydrogenase levels in these fruits are suggested to have led to higher emission of 1-butanol and butyl esters.
-Alcohol o-acyltransferase
-Alcohol dehydrogenase
-Controlled atmosphere
-Hydroperoxide lyase
(c) American Chemical Society, 2008
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