Impact of Phenolic Acid Derivatives on the Oxidative Stability of β-Lactoglobulin-Stabilized Emulsions.
Alina BockHelena KieserlingUlrike SteinhäuserSascha RohnPublished in: Antioxidants (Basel, Switzerland) (2023)
Proteins, such as β-lactoglobulin (β-Lg), are often used to stabilize oil-water-emulsions. By using an additional implementation of phenolic compounds (PC) that might interact with the proteins, the oxidative stability can be further improved. Whether PC have a certain pro-oxidant effect on oxidation processes, while interacting non-covalently (pH-6) or covalently (pH.9) with the interfacial protein-film, is not known. This study aimed to characterize the impact of phenolic acid derivatives (PCDs) on the antioxidant efficacy of the interfacial β-Lg-film, depending on their structural properties and pH-value. Electron paramagnetic resonance (EPR) analyses were performed to assess the radical scavenging in the aqueous and oil phases of the emulsion, and the complexation of transition metals: these are well known to act as pro-oxidants. Finally, in a model linseed oil emulsion, lipid oxidation products were analyzed over storage time in order to characterize the antioxidant efficacy of the interfacial protein-film. The results showed that, at pH.6, PCDs can scavenge hydrophilic radicals and partially scavenge hydrophobic radicals, as well as reduce transition metals. As expected, transition metals are complexed to only a slight degree, leading to an increased lipid oxidation through non-complexed reduced transition metals. At pH.9, there is a strong complexation between PCDs and the transition metals and, therefore, a decreased ability to reduce the transition metals; these do not promote lipid oxidation in the emulsion anymore.
Keyphrases
- human health
- electron transfer
- health risk
- health risk assessment
- ionic liquid
- fatty acid
- anti inflammatory
- hydrogen peroxide
- risk assessment
- oxidative stress
- heavy metals
- healthcare
- room temperature
- primary care
- reduced graphene oxide
- protein protein
- climate change
- quality improvement
- binding protein
- perovskite solar cells
- high resolution
- energy transfer
- structure activity relationship