Flow-induced alignment of protein nanofibril dispersions

J Colloid Interface Sci. 2023 May 15:638:487-497. doi: 10.1016/j.jcis.2023.01.105. Epub 2023 Jan 27.

Abstract

Hypothesis: Protein nanofibrils (PNF) resulting from the self-assembly of proteins or peptides can present structural ordering triggered by numerous factors, including the shear flow. We hypothesize that i) depending on the contour length of the PNF and the magnitude of the shear rate applied to the PNF dispersion, they exhibit specific orientation, and ii) it is possible to predict the alignment of PNF by establishing a flow-alignment relationship. Understanding such a relationship is pivotal to improving the fundamental knowledge and application of fibril systems.

Experiments: We use β-lactoglobulin PNF aqueous dispersions with different average contour lengths but equal persistence lengths. We employ simple shear-dominated microfluidic devices with state-of-the-art imaging techniques: flow-induced birefringence (FIB) and micro-particle image velocimetry (μ-PIV), to probe the effect of shear flow on PNF alignment.

Findings: We provide an empirical relationship connecting the birefringence Δn (quantifying the extent of PNF alignment), and the Péclet number Pe (correlating the shear rate of the flow relative to the rotational diffusion of PNF) to understand the flow-alignment behavior of PNF under shear-dominated flows. Furthermore, we assess the alignment and flow profile of PNF at both high and low flow rates. The length of PNF emerges as a controlling parameter capable of modulating PNF alignment at specific shear rates. Our results shed new insights into the hydrodynamic behavior of PNF, which is highly relevant to various industrial processes involving the fibril systems.

Keywords: -lactoglobulin; Colloidal rods; Flexibility; Microfluidics; Shear flow; Whey protein.

MeSH terms

  • Proteins*
  • Rheology

Substances

  • Proteins