Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces

Marina J. Richter; Alexander Schulz; Thomas Subkowski; Alexander Böker

doi:10.1016/j.jcis.2016.06.062

Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces

Marina J. Richter, Alexander Schulz, Thomas Subkowski, Alexander Böker

8 Citations (Scopus)

Abstract

Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H∗Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior.

Original language	English
Journal	Journal of Colloid and Interface Science
Volume	479
Pages (from-to)	199-206
Number of pages	8
ISSN	0021-9797
DOIs	https://doi.org/10.1016/j.jcis.2016.06.062
Publication status	Published - 1 Oct 2016
Externally published	Yes

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10.1016/j.jcis.2016.06.062

Cite this

@article{4ce43469512842dd80598d05156cf2ab,

title = "Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces",

abstract = "Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H∗Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior.",

keywords = "Hydrophobin, IFT, Pendant drop tensiometry, Rheology, Self-assembly",

author = "Richter, {Marina J.} and Alexander Schulz and Thomas Subkowski and Alexander B{\"o}ker",

year = "2016",

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language = "English",

volume = "479",

pages = "199--206",

journal = "Journal of Colloid and Interface Science",

issn = "0021-9797",

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TY - JOUR

T1 - Adsorption and rheological behavior of an amphiphilic protein at oil/water interfaces

AU - Richter, Marina J.

AU - Schulz, Alexander

AU - Subkowski, Thomas

AU - Böker, Alexander

PY - 2016/10/1

Y1 - 2016/10/1

N2 - Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H∗Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior.

AB - Hydrophobins are highly surface active proteins which self-assemble at hydrophilic-hydrophobic interfaces into amphipathic membranes. We investigate hydrophobin self-assembly at oil/water interfaces to deepen the understanding of protein behavior in order to improve our biomimetic synthesis. Therefore, we carried out pendant drop measurements of hydrophobin stabilized oil/water systems determining the time-dependent IFT and the dilatational rheology with additional adaptation to the Serrien protein model. We show that the class I hydrophobin H∗Protein B adsorbs at an oil/water interface where it forms a densely-packed interfacial protein layer, which dissipates energy during droplet oscillation. Furthermore, the interfacial protein layer exhibits shear thinning behavior.

KW - Hydrophobin

KW - IFT

KW - Pendant drop tensiometry

KW - Rheology

KW - Self-assembly

U2 - 10.1016/j.jcis.2016.06.062

DO - 10.1016/j.jcis.2016.06.062

M3 - Journal article

C2 - 27388134

SN - 0021-9797

VL - 479

SP - 199

EP - 206

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

ER -