Interfacial characterization of beta-lactoglobulin networks: displacement by bile salts.
The competitive displacement of a model protein (beta-lactoglobulin) by bile salts from air-water and oil-water interfaces is investigated in vitro under model duodenal digestion conditions. The aim is to understand this process so that interfaces can be designed to control lipid digestion thus improving the nutritional impact of foods. Duodenal digestion has been simulated using a simplified biological system and the protein displacement process monitored by interfacial measurements and atomic force microscopy (AFM). First, the properties of beta-lactoglobulin adsorbed layers at the air-water and the olive oil-water interfaces were analyzed by interfacial tension techniques under physiological conditions (pH 7, 0.15 M NaCl, 10 mM CaCl2, 37 degrees C). The protein film had a lower dilatational modulus (hence formed a weaker network) at the olive oil-water interface compared to the air-water interface. Addition of bile salt (BS) severely decreased the dilatational modulus of the adsorbed beta-lactoglobulin film at both the air-water and olive oil-water interfaces. The data suggest that the bile salts penetrate into, weaken, and break up the interfacial beta-lactoglobulin networks. AFM images of the displacement of spread beta-lactoglobulin at the air-water and the olive oil-water interfaces suggest that displacement occurs via an orogenic mechanism and that the bile salts can almost completely displace the intact protein network under duodenal conditions. Although the bile salts are ionic, the ionic strength is sufficiently high to screen the charge allowing surfactant domain nucleation and growth to occur resulting in displacement. The morphology of the protein networks during displacement is different from those found when conventional surfactants were used, suggesting that the molecular structure of the surfactant is important for the displacement process. The studies also suggest that the nature of the oil phase is important in controlling protein unfolding and interaction at the interface. This in turn affects the strength of the protein network and the ability to resist displacement by surfactants.
Institute of Food Research, Norwich Research Park, NR4 7UA, Norwich, UK.
Julia
J
Maldonado-Valderrama
Nicola C
NC
Woodward
A Patrick
AP
Gunning
Mike J
MJ
Ridout
Fiona A
FA
Husband
Alan R
AR
Mackie
Victor J
VJ
Morris
Peter J
PJ
Wilde
D000818:Animals; D001647:Bile Acids and Salts / Q000737:chemistry*; D002417:Cattle; D007782:Lactoglobulins / Q000737:chemistry* / Q000648:ultrastructure; D018625:Microscopy, Atomic Force; D011312:Pressure; D012212:Rheology
D001647:Bile Acids and Salts; D007782:Lactoglobulins