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


Gumus C. E., Decker E. A., McClements D. J.

Food Research International, cilt.100, ss.175-185, 2017 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 100
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1016/j.foodres.2017.08.029
  • Dergi Adı: Food Research International
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.175-185
  • Anahtar Kelimeler: Omega-3 oils, Legume protein, Pulse protein, Emulsion, Natural emulsifier, Lipid oxidation, CONTINUOUS-PHASE PROTEIN, ANTIOXIDANT ACTIVITY, BETA-LACTOGLOBULIN, POTENTIAL APPLICATIONS, EMULSIFYING PROPERTIES, STABILIZED EMULSIONS, DROPLET SIZE, FLAXSEED OIL, FOOD SYSTEMS, OMEGA-3
  • Ankara Üniversitesi Adresli: Hayır

Özet

© 2017Emulsion-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 1 wt% 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 (+ 100 μM iron sulfate) or non-accelerated (no added iron) conditions for 21 or 33 days, 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.