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Impact of legume protein type and location on lipid oxidation in fish oil-in-water emulsions: Lentil, pea, and faba bean proteins

Author:
Gumus, Cansu Ekin, Decker, Eric Andrew, McClements, David Julian
Source:
Food research international 2017 v.100 pp. 175-185
ISSN:
0963-9969
Subject:
beverages, droplets, emulsifiers, emulsions, faba beans, fish, fish oils, functional foods, ingredients, iron, legume protein, lentils, light scattering, lipid peroxidation, microscopy, microstructure, omega-3 fatty acids, oxidative stability, particle size, peas, peroxides, sulfates, thiobarbituric acid-reactive substances, whey protein isolate
Abstract:
Emulsion-based delivery systems are being developed to incorporate ω-3 fatty acids into functional foods and beverages. There is interest in formulating these delivery systems from more sustainable and label-friendly ingredients. The aim of this study was therefore to examine the impact of plant-protein emulsifiers on the oxidative stability of 1wt% fish oil-in-water emulsions. Fish oil emulsions stabilized by three types of legume protein (lentil, pea, and faba bean) were produced using a high-pressure microfluidizer. The formation of primary (peroxides) and secondary (TBARS) lipid oxidation products was measured when the emulsions were stored at 37°C under accelerated (+100μM iron sulfate) or non-accelerated (no added iron) conditions for 21 or 33days, respectively. The particle size, charge and microstructure of the emulsions were monitored during storage using light scattering and microscopy to detect changes in physical stability. Emulsions stabilized by whey protein isolate, a commonly used animal-based protein, were utilized as a control. The emulsions formed using whey protein had smaller initial particle sizes, better physical stability, and slightly better stability to lipid oxidation than the ones formed using plant-based proteins. The impact of protein location (adsorbed versus non-adsorbed) on the oxidative stability of the emulsions was also investigated. The presence of non-adsorbed proteins inhibited lipid oxidation, presumably by binding transition metals and reducing their ability to interact with ω-3 fatty acids in the lipid droplets. Overall, these results have important implications for fabricating emulsion-based delivery systems for bioactive lipids, e.g., they indicate that including high levels of non-adsorbed proteins could improve oxidative stability.
Agid:
5820960