The mechanical properties of milk protein films spread at the air-water interface

1973 ◽  
Vol 45 (3) ◽  
pp. 478-486 ◽  
Author(s):  
J.V Boyd ◽  
J.R Mitchell ◽  
L Irons ◽  
P.R Musselwhite ◽  
P Sherman
Keyword(s):  
Mechanical Properties ◽  
Milk Protein ◽  
Water Interface ◽  
Protein Films ◽  
Air Water Interface

Correlation between Mechanical Behavior of Protein Films at the Air/Water Interface and Intrinsic Stability of Protein Molecules

Langmuir ◽  
2005 ◽  
Vol 21 (9) ◽  
pp. 4083-4089 ◽  
Author(s):  
Anneke H. Martin ◽  
Martien A. Cohen Stuart ◽  
Martin A. Bos ◽  
Ton van Vliet
Keyword(s):  
Mechanical Behavior ◽  
Water Interface ◽  
Protein Films ◽  
Intrinsic Stability ◽  
Air Water Interface ◽  
Protein Molecules

scholarly journals The interfacial structure and Young's modulus of peptide films having switchable mechanical properties

2007 ◽  
Vol 5 (18) ◽  
pp. 47-54 ◽  
Author(s):  
A.P.J Middelberg ◽  
L He ◽  
A.F Dexter ◽  
H.-H Shen ◽  
S.A Holt ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Young’S Modulus ◽  
Self Assembly ◽  
Molecular Design ◽  
Foam Stability ◽  
Young's Modulus ◽  
Interfacial Structure ◽  
Water Interface ◽  
Air Water Interface ◽  
Peptide Dissociation

We report the structure and Young's modulus of switchable films formed by peptide self-assembly at the air–water interface. Peptide surfactant AM1 forms an interfacial film that can be switched, reversibly, from a high- to low-elasticity state, with rapid loss of emulsion and foam stability. Using neutron reflectometry, we find that the AM1 film comprises a thin (approx. 15 Å) layer of ordered peptide in both states, confirming that it is possible to drastically alter the mechanical properties of an interfacial ensemble without significantly altering its concentration or macromolecular organization. We also report the first experimentally determined Young's modulus of a peptide film self-assembled at the air–water interface ( E =80 MPa for AM1, switching to E <20 MPa). These findings suggest a fundamental link between E and the macroscopic stability of peptide-containing foam. Finally, we report studies of a designed peptide surfactant, Lac21E, which we find forms a stronger switchable film than AM1 ( E =335 MPa switching to E <4 MPa). In contrast to AM1, Lac21E switching is caused by peptide dissociation from the interface (i.e. by self-disassembly). This research confirms that small changes in molecular design can lead to similar macroscopic behaviour via surprisingly different mechanisms.

Linear and nonlinear microrheology of lysozyme layers forming at the air–water interface

Soft Matter ◽  
2014 ◽  
Vol 10 (36) ◽  
pp. 7051-7060 ◽  
Author(s):  
Daniel B. Allan ◽  
Daniel M. Firester ◽  
Victor P. Allard ◽  
Daniel H. Reich ◽  
Kathleen J. Stebe ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Water Interface ◽  
Nonlinear Mechanical ◽  
Air Water Interface ◽  
Linear And Nonlinear

Microrheology tracks the evolution in the linear and nonlinear mechanical properties of layers of the protein lysozyme adsorbing at the air–water interface as the layers undergo a viscoelastic transition.

Langmuir films and mechanical properties of polyethyleneglycol fatty acid esters at the air-water interface

2016 ◽  
Vol 498 ◽  
pp. 50-57 ◽  
Author(s):  
Stephanie Ortiz-Collazos ◽  
Yan M.H. Gonçalves ◽  
Bruno A.C. Horta ◽  
Paulo H.S. Picciani ◽  
Sonia R.W. Louro ◽  
...  
Keyword(s):  
Mechanical Properties ◽  
Fatty Acid ◽  
Langmuir Films ◽  
Fatty Acid Esters ◽  
Water Interface ◽  
Air Water Interface ◽  
Acid Esters

In Situ Measurement of the Displacement of Protein Films from the Air/Water Interface by Surfactant

2001 ◽  
Vol 2 (3) ◽  
pp. 1001-1006 ◽  
Author(s):  
Alan R. Mackie ◽  
A. Patrick Gunning ◽  
Mike J. Ridout ◽  
Peter J. Wilde ◽  
J. Rodriguez Patino
Keyword(s):  
In Situ Measurement ◽  
Water Interface ◽  
Protein Films ◽  
Air Water Interface
Sign in / Sign up

Export Citation Format

Share Document