4.7 Article

Structure and stability of sodium-caseinate-stabilized oil-in-water emulsions as influenced by heat treatment

期刊

FOOD HYDROCOLLOIDS
卷 66, 期 -, 页码 307-317

出版社

ELSEVIER SCI LTD
DOI: 10.1016/j.foodhyd.2016.11.041

关键词

Sodium caseinate; Heat-induced proteolysis; Depletion flocculation; Emulsion stability; Rheology

资金

  1. Fonterra Research and Development Centre
  2. Foundation for Research, Science and Technology

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The emulsion stability and rheological properties of heated (120 degrees C, 0-60 min) 30% w/w oil-in-water emulsions (droplet diameter similar to .73 mu m, pH 6.8) containing sodium caseinate (Na-CN), 2-6% w/w, were investigated. The creaming kinetics, determined by multiple light scattering (Turbiscan), showed that the phase separation of Na-CN-stabilized emulsions was markedly dependent on the duration of the heat treatment. The differences between unheated and heated emulsions were attributed to heat induced physicochemical changes in the aqueous Na-CN nanoparticles. The heat treatment caused protein degradation and changed the intact Na-CN concentration in the continuous phase. The emulsion structures, with varied extents of depletion flocculation, were well reflected by small and large deformation rheology. In the recombined Na-CN emulsions, the depletion attraction was weakened at low and moderate Na-CN concentrations (2% and 4% w/w) but was strengthened at high Na-CN concentration (6% w/w). The former structural change was predominantly due to reduced depletion attraction, whereas reduced depletion attraction and decreased continuous phase viscosity influenced the latter structural change. The intact Na-CN concentration in the continuous phase is determined by the heat-induced physicochemical changes of Na-CN nanoparticles, which played a significant role in the physical stability of the emulsions. The insights from this study can be used to create novel droplet sizes and protein particle sizes to manipulate the droplet/protein size ratio, and therefore the extent of droplet droplet interactions. (C) 2016 Elsevier Ltd. All rights reserved.

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