4.7 Article

Influence of protein type on oxidation and digestibility of fish oil-in-water emulsions: Gliadin, caseinate, and whey protein

Journal

FOOD CHEMISTRY
Volume 175, Issue -, Pages 249-257

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.11.112

Keywords

Wheat gliadin; Sodium caseinate; Whey protein isolate; Emulsion; Oxidative stability; Lipid digestibility

Funding

  1. National High Technology Research and Development Program of China (863 Program) [2013AA102201]
  2. Cooperative State Research, Extension, Education Service
  3. United State Department of Agriculture
  4. Massachusetts Agricultural Experiment Station
  5. United States Department of Agriculture
  6. CREES
  7. NRI
  8. AFRI [2011-03539, 2013-03795]
  9. Chinese Research Council

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The influence of three surface-active proteins on the oxidative stability and lipase digestibility of emulsified omega-3 oils was examined: deamidated wheat gliadin (gliadin); sodium caseinate (CN); whey protein isolate (WPI). Gliadin and WPI were more effective at inhibiting lipid oxidation (hydroperoxides and TBARS) of fish oil-in-water emulsions than CN. Protein oxidation during storage was determined by measuring the loss of tryptophan fluorescence. The CN-emulsions exhibited the highest loss of tryptophan fluorescence during aging, as well as the highest amount of lipid oxidation. Potential reasons for the differences in oxidative stability of the emulsions with different proteins include differences in interfacial film thickness, protein chelating ability, and antioxidant amino acids profiles. During in vitro digestion, gliadin-stabilized emulsions had the lowest digestion rate of the three proteins. These results have important implications for using proteins to fabricate emulsion-based delivery systems for omega-3 oils. (c) 2014 Elsevier Ltd. All rights reserved.

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