Department of Physiology and Technology of Plant Products, Instituto de la Grasa, CSIC, Seville, Spain.
J Agric Food Chem. 2012 Jul 4;60(26):6477-82. doi: 10.1021/jf3016738. Epub 2012 Jun 25.
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.
本工作旨在通过脂氧合酶（LOX）途径对与 virgin olive oil（VOO）挥发性化合物生物合成相关的重组蛋白的热失活动力学参数进行表征。研究了三种纯化的 LOX 同工酶（Oep2LOX1、Oep1LOX2 和 Oep2LOX2）和一种氢过氧化物裂解酶（HPL）蛋白（OepHPL）。根据其热失活动力学参数，鉴定出重组 Oep1LOX2 和 Oep2LOX2 是在橄榄果实粗提物中负责合成 13-氢过氧化物的两种 LOX 同工酶，13-氢过氧化物是 VOO 挥发性化合物合成的主要底物。重组 Oep2LOX1 显示出较低的热稳定性，这表明在考虑当前工业过程的热条件下，其在油提取过程中的作用较弱。此外，重组 OepHPL 可被鉴定为粗提物中的 HPL 活性。与研究的重组蛋白相比，其热稳定性最高，表明 HPL 活性不是 VOO 挥发性化合物合成的限制因素。
