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. 1999 Jan;47(1):249-53.
doi: 10.1021/jf9807519.

Lipoxygenase and Hydroperoxide Lyase Activities in Ripening Strawberry Fruits

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Lipoxygenase and Hydroperoxide Lyase Activities in Ripening Strawberry Fruits

A G Pérez et al. J Agric Food Chem. .

Abstract

The enzymes lipoxygenase and hydroperoxide lyase have been identified in strawberry (Fragariax ananassa Duch.) var. Camarosa. Their subcellular localization, substrate preference, and product specificity were determined in mature strawberry fruits. The activity of both enzymes was located mainly in the microsomal fraction. Linolenic acid was the preferred substrate for strawberry lipoxygenase, forming 13- and 9-hydroperoxides of this acid in the proportion 70:30. The strawberry hydroperoxide lyase cleaves 13-hydroperoxide of linoleic (13% relative activity) and linolenic (100% relative activity) acids to form hexanal and (3Z)-hexenal, respectively. Both enzyme activities and endogenous content of volatile aldehydes formed by sequential action of lipoxygenase-hydroperoxide lyase were evaluated during strawberry development and ripening. A sequential enzymatic pathway for the formation of green odor compounds in strawberry is proposed.

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