Effects of dynamic adsorption on bubble formation and coalescence in partitioned-EDGE devices

Boxin Deng, Karin Schroën, Jolet de Ruiter*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Hypothesis: Dynamic adsorption effects can play a crucial role in bubble formation and stabilization. We hypothesize that microfluidic tools provide direct insights to these effects, and that the final bubble size depends on the intersection of time scales for bubble formation versus adsorption of proteins. Experiments: We use a microfluidic device to study Laplace pressure-driven formation of bubbles that are stabilized by whey proteins. Bubble behavior is studied as a function of the pressure difference imposed across the pores (Pd), and thus the bubble formation time (τ, ranging from μs to s), using highspeed recordings, quasi-static pressure arguments and a semi-empirical coalescence model. Findings: We observe two distinct bubble formation regimes, delimited by the pressure difference required to initiate bubble formation in pure water, Pd= 1400 mbar. When Pd<1400 mbar, protein adsorption is a requisite to lower the surface tension and initialize bubble formation. Individual bubbles (fixed d0~ 25 μm) are formed slowly with τ≫1 ms. When Pd exceeds 1400 mbar, bubbles (fixed d0~ 16 μm) experience no adsorption lag and thus are formed at steeply increasing frequency, with τ < 1 ms. Interaction between these bubbles causes finite coalescence to a diameter dcoal that increases for lower τ. A minimum time of 0.4 ms is needed to immediately stabilize individual bubbles. Our study provides a promising microfluidic tool to study bubble formation and coalescence dynamics simultaneously.

Original languageEnglish
Pages (from-to)316-324
Number of pages9
JournalJournal of Colloid and Interface Science
Volume602
DOIs
Publication statusPublished - 15 Nov 2021

Keywords

  • Bubble formation dynamics
  • Coalescence
  • Empirical coalescence model
  • Microfluidics
  • Overlapping time scales
  • Pressure-driven flow
  • Protein stabilization

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