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Thermal inactivation kinetics of recombinant proteins of the lipoxygenase pathway related to the synthesis of virgin olive oil volatile compounds.
J Agric Food Chem. 2012 Jul 04; 60(26):6477-82.JA

Abstract

The aim of this work was to characterize the thermal inactivation parameters of recombinant proteins related to the biosynthesis of virgin olive oil (VOO) volatile compounds through the lipoxygenase (LOX) pathway. Three purified LOX isoforms (Oep2LOX1, Oep1LOX2, and Oep2LOX2) and a hydroperoxide lyase (HPL) protein (OepHPL) were studied. According to their thermal inactivation parameters, recombinant Oep1LOX2 and Oep2LOX2 could be identified as the two LOX isoforms active in olive fruit crude preparations responsible for the synthesis of 13-hydroperoxides, the main substrates for the synthesis of VOO volatile compounds. Recombinant Oep2LOX1 displayed a low thermal stability, which suggests a weak actuation during the oil extraction process considering the current thermal conditions of this industrial process. In addition, recombinant OepHPL could be identified as the HPL activity in crude preparations. The thermal stability was the highest among the recombinant proteins studied, which suggests that HPL activity is not a limiting factor for the synthesis of VOO volatile compounds.

Authors+Show Affiliations

Department of Physiology and Technology of Plant Products, Instituto de la Grasa, CSIC, Seville, Spain.No 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

22703291

Citation

Padilla, María N., et al. "Thermal Inactivation Kinetics of Recombinant Proteins of the Lipoxygenase Pathway Related to the Synthesis of Virgin Olive Oil Volatile Compounds." Journal of Agricultural and Food Chemistry, vol. 60, no. 26, 2012, pp. 6477-82.
Padilla MN, Martínez-Rivas JM, Pérez AG, et al. Thermal inactivation kinetics of recombinant proteins of the lipoxygenase pathway related to the synthesis of virgin olive oil volatile compounds. J Agric Food Chem. 2012;60(26):6477-82.
Padilla, M. N., Martínez-Rivas, J. M., Pérez, A. G., & Sanz, C. (2012). Thermal inactivation kinetics of recombinant proteins of the lipoxygenase pathway related to the synthesis of virgin olive oil volatile compounds. Journal of Agricultural and Food Chemistry, 60(26), 6477-82. https://doi.org/10.1021/jf3016738
Padilla MN, et al. Thermal Inactivation Kinetics of Recombinant Proteins of the Lipoxygenase Pathway Related to the Synthesis of Virgin Olive Oil Volatile Compounds. J Agric Food Chem. 2012 Jul 4;60(26):6477-82. PubMed PMID: 22703291.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thermal inactivation kinetics of recombinant proteins of the lipoxygenase pathway related to the synthesis of virgin olive oil volatile compounds. AU - Padilla,María N, AU - Martínez-Rivas,José M, AU - Pérez,Ana G, AU - Sanz,Carlos, Y1 - 2012/06/25/ PY - 2012/6/19/entrez PY - 2012/6/19/pubmed PY - 2012/10/27/medline SP - 6477 EP - 82 JF - Journal of agricultural and food chemistry JO - J Agric Food Chem VL - 60 IS - 26 N2 - The aim of this work was to characterize the thermal inactivation parameters of recombinant proteins related to the biosynthesis of virgin olive oil (VOO) volatile compounds through the lipoxygenase (LOX) pathway. Three purified LOX isoforms (Oep2LOX1, Oep1LOX2, and Oep2LOX2) and a hydroperoxide lyase (HPL) protein (OepHPL) were studied. According to their thermal inactivation parameters, recombinant Oep1LOX2 and Oep2LOX2 could be identified as the two LOX isoforms active in olive fruit crude preparations responsible for the synthesis of 13-hydroperoxides, the main substrates for the synthesis of VOO volatile compounds. Recombinant Oep2LOX1 displayed a low thermal stability, which suggests a weak actuation during the oil extraction process considering the current thermal conditions of this industrial process. In addition, recombinant OepHPL could be identified as the HPL activity in crude preparations. The thermal stability was the highest among the recombinant proteins studied, which suggests that HPL activity is not a limiting factor for the synthesis of VOO volatile compounds. SN - 1520-5118 UR - https://www.unboundmedicine.com/medline/citation/22703291/Thermal_inactivation_kinetics_of_recombinant_proteins_of_the_lipoxygenase_pathway_related_to_the_synthesis_of_virgin_olive_oil_volatile_compounds_ DB - PRIME DP - Unbound Medicine ER -