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Lipoxygenase and hydroperoxide lyase activities in ripening strawberry fruits.
J Agric Food Chem. 1999 Jan; 47(1):249-53.JA

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.

Authors+Show Affiliations

Departamento de Fisiología y Tecnología de Productos Vegetales, Instituto de la Grasa, CSIC, Padre García Tejero 4, 41012 Sevilla, Spain. agracia@cica.esNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10563880

Citation

Pérez, A G., et al. "Lipoxygenase and Hydroperoxide Lyase Activities in Ripening Strawberry Fruits." Journal of Agricultural and Food Chemistry, vol. 47, no. 1, 1999, pp. 249-53.
Pérez AG, Sanz C, Olías R, et al. Lipoxygenase and hydroperoxide lyase activities in ripening strawberry fruits. J Agric Food Chem. 1999;47(1):249-53.
Pérez, A. G., Sanz, C., Olías, R., & Olías, J. M. (1999). Lipoxygenase and hydroperoxide lyase activities in ripening strawberry fruits. Journal of Agricultural and Food Chemistry, 47(1), 249-53.
Pérez AG, et al. Lipoxygenase and Hydroperoxide Lyase Activities in Ripening Strawberry Fruits. J Agric Food Chem. 1999;47(1):249-53. PubMed PMID: 10563880.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Lipoxygenase and hydroperoxide lyase activities in ripening strawberry fruits. AU - Pérez,A G, AU - Sanz,C, AU - Olías,R, AU - Olías,J M, PY - 1999/11/24/pubmed PY - 2000/8/19/medline PY - 1999/11/24/entrez SP - 249 EP - 53 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 47 IS - 1 N2 - 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. SN - 0021-8561 UR - https://www.unboundmedicine.com/medline/citation/10563880/Lipoxygenase_and_hydroperoxide_lyase_activities_in_ripening_strawberry_fruits_ DB - PRIME DP - Unbound Medicine ER -