| Title: | Thermal inactivation kinetics of recombinant proteins of the lipoxygenase pathway related to the synthesis of virgin olive oil volatile compounds |
| Author(s): | Padilla MN; Martinez-Rivas JM; Perez AG; Sanz C; |
| Address: | "Department of Physiology and Technology of Plant Products, Instituto de la Grasa, CSIC, Seville, Spain" |
| ISSN/ISBN: | 1520-5118 (Electronic) 0021-8561 (Linking) |
| 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" |
| Keywords: | Aldehyde-Lyases/metabolism Cytochrome P-450 Enzyme System/metabolism Enzyme Stability Food Handling/methods *Hot Temperature Kinetics Lipoxygenase/*metabolism Olive Oil Plant Oils/*chemistry Recombinant Proteins/*metabolism Volatile Organic Compounds/*met; |
| Notes: | "MedlinePadilla, Maria N Martinez-Rivas, Jose M Perez, Ana G Sanz, Carlos eng Research Support, Non-U.S. Gov't 2012/06/19 J Agric Food Chem. 2012 Jul 4; 60(26):6477-82. doi: 10.1021/jf3016738. Epub 2012 Jun 25" |
