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Updated: Aug 15, 2026

Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
Oxidation of dietary polyphenolics by hydroperoxidase activity of lipoxygenase
Maria del Carmen Pinto1, Pedro Macias
1Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain.
Abstract:
Lipoxygenase, in the presence of hydrogen peroxide, produces the oxidative decomposition of quercetin, naringenin, and resveratrol, known antioxidant molecules. Quercetin was the molecule more efficiently oxidized, followed by resveratrol and naringenin. When this molecule was incubated in the presence of GSH, a quinoid derivative was produced. This compound was not obtained in the presence of naringenin or resveratrol, suggesting that in the presence of hydrogen peroxide and lipoxygenase, quercetin may be oxidized to a prooxidant species. When hydrogen peroxide was substituted by hydroperoxy linoleic acid, the same oxidative process was observed. This means that in food products in which lipoxygenase and linoleic acid are presents, quercetin may be oxidized to prooxidant species; in contrast, naringenin and resveratrol may constitute a valid additive for the prevention of the oxidative degradation of foods.
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