Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 60, Issue 26, Pages 6477-6482Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf3016738
Keywords
Olea europaea; lipoxygenase; hydroperoxide lyase; thermal inactivation; olive oil; aroma; volatiles
Funding
- Programa Nacional de Recursos y Tecnologias Alimentarias [AGL2005-03959, AGL2008-00258]
- Spanish government
- Junta de Andalucia
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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 OepILOX2 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.
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