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 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Journal of Colloid and Interface Science
Vol/bind	479
Sider (fra-til)	199-206
Antal sider	8
ISSN	0021-9797
DOI	https://doi.org/10.1016/j.jcis.2016.06.062
Status	Udgivet - 1 okt. 2016
Udgivet eksternt	Ja

Emneord

Hydrophobin
IFT
Pendant drop tensiometry
Rheology
Self-assembly

Adgang til dokumentet

10.1016/j.jcis.2016.06.062

Citationsformater

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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.",

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

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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 -