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Microfluidic Mixers for Studying Protein Folding

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Rescaling Flow Curves of Protein-Stabilized Emulsions.

Santiago F Velandia^1,2, Philippe Marchal¹, Véronique Sadtler¹

¹Université de Lorraine, CNRS, LRGP, F-54000 Nancy, France.

Nanomaterials (Basel, Switzerland)

|May 13, 2025

Summary

This summary is machine-generated.

This study reveals that oil-in-water Pickering emulsions stabilized by bovine serum albumin (BSA) exhibit flow behavior similar to surfactant-stabilized emulsions. Scaling parameters effectively describe rotational rheology but show limitations in oscillatory modes for these complex fluids.

Keywords:

Cox–Merz rule jamming transition rheological modelling scaling of flow curves viscoelastic behavior

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Area of Science:

Colloid and Surface Science
Rheology of Complex Fluids
Emulsion Science

Background:

Pickering emulsions offer unique stabilization mechanisms using solid particles.
Bovine serum albumin (BSA) is explored as a protein-based stabilizer for oil-in-water emulsions.
Understanding the rheological properties of emulsions is crucial for their application and processing.

Purpose of the Study:

To investigate the flow behavior of oil-in-water Pickering emulsions stabilized by BSA.
To compare the rheological characteristics with surfactant-stabilized emulsions using established scaling parameters.
To evaluate the applicability of existing rheological models in both rotational and oscillatory flow regimes.

Main Methods:

Utilized a phase transition analogy for rheological analysis.
Applied scaling parameters commonly used for surfactant-stabilized emulsions.
Conducted rotational and oscillatory rheometry experiments on BSA-stabilized emulsions.
Analyzed the flow behavior above the jamming fraction.

Main Results:

Successfully described the flow behavior of BSA-stabilized Pickering emulsions using scaling parameters, indicating similarities with surfactant systems.
Observed similar trends between scaled rotational and oscillatory rheology data above the jamming fraction.
Identified limitations in accurately rescaling the behavior of G* under oscillatory conditions.

Conclusions:

The study highlights the universality of certain scaling parameters across different emulsion stabilization mechanisms.
Findings provide valuable insights into the rheological behavior of protein-stabilized Pickering emulsions.
The research suggests potential for unified rheological modeling of complex fluid systems.