Adsorption of charged anisotropic nanoparticles at oil–water interfaces

Abstract

Oil properties significantly affect the adsorption of charged anisotropic nanoparticles at oil–water interfaces.

Effects of ultrasonic conditions on the interfacial property and emulsifying property of cellulose nanoparticles from ginkgo seed shells

“…However, in contrast to the time scale of hours for CNCs adsorption at the A/W interface [31] , the time scale of present lag-phase was only minutes. This indicated that the lower kinetic adsorption barrier for cellulose nanoparticles adsorbed at the O/W interface compared to the A/W interface, probably due to enhanced wetting of cellulose nanoparticles by oil compared to air [33] .

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“…This decreased lag-phase time indicated earlier adsorption for cellulose nanoparticles at the O/W interface, due to its small particle size and higher hydrophobicity. Moreover, those nanoparticles lowered interfacial tension, resulting in the decrease of the particle adsorption energy [33] . However, the G” was always larger than G’ and no crossover of G’ and G” within the measured time sweep.…”

Globular protein assembly and network formation at fluid interfaces: effect of oil

“…A clear correlation between the oil polarity and the adsorption behavior was found. 28,38 Furthermore, it was shown that the oil properties significantly control the interfacial network rheology and formation kinetics of BLG. 29 Herein, we systematically investigate the influence of oil polarity on layer formation and rheological strength of the 2D nanolayers of three different well-studied globular proteins (BLG, BSA, and LSZ) at fluid interfaces.…”

“…The purity of the oil phase was confirmed by measuring the constant oil-water interfacial tension with a droplet profile tensiometer (PAT-1, SINTERFACE Technologies), as described in literature. 28,29,38,45,46 An oil droplet was formed at the tip of an U-shaped capillary tip in 10 mg/L protein solution. The interfacial tension was extracted from the contour of the drop, monitored by a charge-coupled device camera, by axisymmetric drop shape analysis.…”

“…2,[20][21][22][23][24] The impact of the chemical properties of the hydrophobic subphase is widely neglected and systematic studies are missing, even though a small number of publications indicated changes in interfacial processes at different hydrophobic interfaces. 23,[25][26][27][28][29][30] Globular proteins, such as β-lactoglobulin (BLG), bovine serum albumin (BSA), and hen egg white lysozyme (LSZ), consist of an amino acid chain which arranges into a well-defined secondary and tertiary structures. In water, they have a sphere-like native configuration with most of their hydrophilic amino acid groups at the exterior and hydrophobic residues located at the interior.…”