Abstract
The discovery of the lactoperoxidase system as a biocatalyst in milk was a landmark finding. The activation of this system using hydrogen peroxide (H2O2) raised hopes for oxidation of various organic substrates. The involvement of lactoperoxidase system in the catalyzed-oxidation of carotenoids in the whey proteins, and the effect of various solvents on carotenoids' oxidation reaction rate has been studied. However, there is no evidence for this reaction without the addition of oxidizing agents, such as peroxides. Here, we reveal that carotenoids are oxidized through the addition of just ethanol in the presence of lactoperoxidase. The oxidation of carotenoids through this exquisite strategy is ∼360 times faster than harnessing the lactoperoxidase system in whey proteins via the addition of hydrogen peroxide. Bearing in mind that ethanol is not an oxidizing agent, this observation suggests a potential paradigm shift in our understanding of lactoperoxidase and catalyzed oxidation in biochemical systems.
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