In situ measurement of the displacement of protein films from the air/water interface by surfactant.
The displacement of spread protein films from the air/water interface by surfactant was followed using Brewster angle microscopy (BAM) and interfacial rheology. The displacement of beta-lactoglobulin and beta-casein by a nonionic surfactant was monitored as a function of both surface pressure and time. In both cases, protein displacement occurred over the same surface pressure range that had been observed previously by atomic force microscopy (AFM). In the case of the beta-lactoglobulin, surfactant domains grew large enough in the protein film to be visible in the BAM images. The shapes of the domains were very similar to those seen previously by AFM in the late stages of displacement. The results from both proteins confirm the results published previously while highlighting some implications for the application of the "orogenic" model of displacement for large protein films. The surface rheological data showed that the beta-lactoglobulin/surfactant mixed film retained much of its elasticity until the latter stages of displacement. This indicates that at least in the early stages of displacement, the mixed film was dominated by the behavior of the protein in the film.
Mackie
A R
AR
Institute of Food Research, Norwich Research Park, Colney, NR4 7UA, United Kingdom. alan.mackie@bbsrc.ac.uk
Gunning
A P
AP
Ridout
M J
MJ
Wilde
P J
PJ
Rodriguez Patino
J
J
D000388:Air; D002364:Caseins / Q000737:chemistry; D004548:Elasticity; D005504:Food Analysis; D007782:Lactoglobulins / Q000737:chemistry; D046911:Macromolecular Substances; D011312:Pressure; D011506:Proteins / Q000737:chemistry*; D012212:Rheology; D013499:Surface Properties; D013501:Surface-Active Agents; D014867:Water
D002364:Caseins; D007782:Lactoglobulins; D046911:Macromolecular Substances; D011506:Proteins; D013501:Surface-Active Agents; D014867:Water