4.6 Article

Enhancing the Formation and Stability of Oil-In-Water Emulsions Prepared by Microchannels Using Mixed Protein Emulsifiers

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FRONTIERS IN NUTRITION
卷 9, 期 -, 页码 -

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FRONTIERS MEDIA SA
DOI: 10.3389/fnut.2022.822053

关键词

formation; stability; microchannel; monodisperse emulsion; mixed protein

资金

  1. Faculty of Life and Environmental Sciences, University of Tsukuba
  2. Japan Society for the Promotion of Science (JSPS) KAKENHI [21H008138]

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Although natural emulsifiers have drawbacks when used alone, their emulsifying ability and stability can be improved when used in combination. This study prepared monodisperse emulsions stabilized by combining two natural protein emulsifiers and examined the influence of various factors on the emulsion's microstructure and stability. The results showed that the emulsions stabilized by mixed protein emulsifiers exhibited better stability and were more resistant to high salt concentrations compared to synthetic emulsifiers.
Although natural emulsifiers often have many drawbacks when used alone, their emulsifying ability and stability can usually be improved unexpectedly when used in combination. In this study, monodisperse emulsions stabilized by combining two natural protein emulsifiers, i.e., whey protein isolate (WPI) and sodium caseinate (SC), in different proportions were prepared using microchannel (MC) emulsification. The influences of temperature, pH, ionic strength, and storage time on the microstructure and stability of the emulsions were examined. Analysis of the microstructure and droplet size distribution revealed that the WPI-, SC-, and mixed protein-stabilized emulsions exhibited uniform droplet distribution. The droplet size and xi-potential of the MC emulsions stabilized by mixed protein emulsifiers were higher than those of the emulsions stabilized by WPI or SC separately. The emulsions stabilized by the two types of proteins and mixed emulsifiers had better stability under high salt concentrations than the synthetic emulsifier Tween 20. WPI-SC-stabilized emulsions were more resistant to high temperatures (70-90 degrees C) and exhibited excellent stabilization than those stabilized by WPI and SC, which was attributed to the more sufficient coverage provided by the two types of protein emulsifier layers and better protein adsorption at the oil-water interface. These results indicate that WPI-SC is a potential stabilizer for MC emulsion requirements. This study provides a basis for the formulation of monodisperse and stable natural emulsion systems.

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