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Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis.
J Agric Food Chem. 2007 Jul 25; 55(15):6309-13.JA

Abstract

Thermal stabilities of main enzymes involved in the biosynthesis of virgin olive oil (VOO) aroma through the lipoxygenase (LOX) pathway were studied in crude enzymatic preparations. Kinetic parameters of thermal inactivation for LOX were determined graphically and were shown to be compatible with the presence of two LOX isoenzymes (LOXlab and LOXres) having different thermal stabilities and displaying relative activities of 88 and 12% each. Data on hydroperoxide lyase (HPL) suggest the existence of just one HPL isoform. Thermal stabilities of LOX and HPL enzymatic activities in crude preparations seem to explain the observed decrease of volatile contents in VOO aroma as a consequence of heat treatments of olive fruit. Moreover, differences in thermal stability of LOXlab and LOXres would justify the distinct pattern of reduction of C6 and C5 compound contents observed in the aroma of these oils.

Authors+Show Affiliations

Department of Physiology and Technology of Plant Products, Instituto de la Grasa, C.S.I.C., Padre García Tejero 4, 41012-Seville, Spain.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

17595102

Citation

Luaces, Pilar, et al. "Thermal Stability of Lipoxygenase and Hydroperoxide Lyase From Olive Fruit and Repercussion On Olive Oil Aroma Biosynthesis." Journal of Agricultural and Food Chemistry, vol. 55, no. 15, 2007, pp. 6309-13.
Luaces P, Sanz C, Pérez AG. Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis. J Agric Food Chem. 2007;55(15):6309-13.
Luaces, P., Sanz, C., & Pérez, A. G. (2007). Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis. Journal of Agricultural and Food Chemistry, 55(15), 6309-13.
Luaces P, Sanz C, Pérez AG. Thermal Stability of Lipoxygenase and Hydroperoxide Lyase From Olive Fruit and Repercussion On Olive Oil Aroma Biosynthesis. J Agric Food Chem. 2007 Jul 25;55(15):6309-13. PubMed PMID: 17595102.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thermal stability of lipoxygenase and hydroperoxide lyase from olive fruit and repercussion on olive oil aroma biosynthesis. AU - Luaces,Pilar, AU - Sanz,Carlos, AU - Pérez,Ana G, Y1 - 2007/06/27/ PY - 2007/6/28/pubmed PY - 2007/10/10/medline PY - 2007/6/28/entrez SP - 6309 EP - 13 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 55 IS - 15 N2 - Thermal stabilities of main enzymes involved in the biosynthesis of virgin olive oil (VOO) aroma through the lipoxygenase (LOX) pathway were studied in crude enzymatic preparations. Kinetic parameters of thermal inactivation for LOX were determined graphically and were shown to be compatible with the presence of two LOX isoenzymes (LOXlab and LOXres) having different thermal stabilities and displaying relative activities of 88 and 12% each. Data on hydroperoxide lyase (HPL) suggest the existence of just one HPL isoform. Thermal stabilities of LOX and HPL enzymatic activities in crude preparations seem to explain the observed decrease of volatile contents in VOO aroma as a consequence of heat treatments of olive fruit. Moreover, differences in thermal stability of LOXlab and LOXres would justify the distinct pattern of reduction of C6 and C5 compound contents observed in the aroma of these oils. SN - 0021-8561 UR - https://www.unboundmedicine.com/medline/citation/17595102/Thermal_stability_of_lipoxygenase_and_hydroperoxide_lyase_from_olive_fruit_and_repercussion_on_olive_oil_aroma_biosynthesis_ DB - PRIME DP - Unbound Medicine ER -