Mixed monolayers of gluten-emulsifiers at the air-water interface

in Biopolymer Science: Food And Non Food Applications (1999), (91), 213-216

The interactions and miscibility analysis of gluten-emulsifiers mixed film show that those films are not completely miscible as demonstrated by the presence of both two transition zones and also by the ... [more ▼]

The interactions and miscibility analysis of gluten-emulsifiers mixed film show that those films are not completely miscible as demonstrated by the presence of both two transition zones and also by the deviation of the mean molecular areas of mixed films from the values calculated according to the rule of additivity (GAINES, 1966). Furthermore, the free energy excess of mixing is positive in presence of emulsifiers, confirming the partial miscibility of gluten emulsifier monolayers. [less ▲]

Relationships between structure, interfacial properties, and functional qualities in foams and emulsions of surfactin, a lipopeptide from Bacillus subtilis.

Book published by Ed :E.Dickinson and J.M.R. Patino, Royal Society of Chemistry (1999)

Computer Simulation Of Surfactin Conformation At A Hydrophobic/Hydrophilic Interface

in Langmuir (1999), 15(7), 2409-13

Using a molecular modeling method, different conformations of surfactin at a hydrophobic/hydrophilic interface are established. Two conformations of the peptide ring (S1 and S2) provided by NMR ... [more ▼]

Using a molecular modeling method, different conformations of surfactin at a hydrophobic/hydrophilic interface are established. Two conformations of the peptide ring (S1 and S2) provided by NMR experiments built with three different aliphatic chains in folded or extended configurations were studied. For the structures including the S2 peptide ring conformation, the theoretical interfacial molecular area corresponds to the experimental limiting area A0 value obtained with a Langmuir film balance. The peptide ring is positioned in the plane of the interface with the two acidic chains close to each other and protruding in the aqueous phase, and the β-hydroxy fatty acid chain, folded to interact mainly with the Leu2 side chain and also with the Val4 side chain. This design has the largest calculated molecular area and would correspond to the most stable amphipathic structure representing the surfactin experimental behavior in weak compression. [less ▲]

Mixed monolayers of gluten-emulsifiers at the air-water interface.

Poster (1998, September)

Relationships between structure, interfacial properties and functional qualities in foam and emulsion of Bacillus subtilis lipopeptides.

Poster (1998, March)

Foaming properties of lipopeptides produced by Bacillus subtilis: effect of lipid and peptide structural attributes

in Journal of Agricultural and Food Chemistry (1998), 46(3), 911-916

To study the effect of lipid and peptide structural attributes of Bacillus subtilis lipopeptides on their foaming properties, the formation, stability, and appearance of foams prepared with surfactins ... [more ▼]

To study the effect of lipid and peptide structural attributes of Bacillus subtilis lipopeptides on their foaming properties, the formation, stability, and appearance of foams prepared with surfactins (C13 C15) and iturins A (C14 C17) were characterized. The density and stability of lipopeptide foams depend on both the alkyl chain hydrophobic character and peptide molecular intrinsic properties. A lipidic chain length of 14 carbon atoms provides lipopeptides with the best foaming properties in terms of foam density and liquid stability in foams. Increases in alkyl chain length above 15 carbon atoms result in a drastic decrease of iturin A foam density. With the same alkyl chain, surfactin produces denser foam whereas iturin A exhibits better foaming stability. These results demonstrate the importance of the peptide structural attributes of B. subtilis on their foaming properties. [less ▲]

Lipopeptides alter Bacillus subtilis hydrophobicity by adsorbing onto cell surfaces

Poster (1997, October 29)

Surface-active properties of surfactin-iturinA mixtures produced by Bacillus subtilis

Scientific conference (1997, March 16)

Interfacial and emulsifying properties of Bacillus suvtilis lipopeptides

Poster (1997)

Proprietes interfaciales des films de gluten de farines de qualites boulangeres differentes.

in Sciences des Aliments (1997), 17(3), 271-278

Interfacial properties of gluten proteins are important in determining flour breadmaking quality especially the gas bubbles stability in dough, which influences the loaf volume and crumb texture. The ... [more ▼]

Interfacial properties of gluten proteins are important in determining flour breadmaking quality especially the gas bubbles stability in dough, which influences the loaf volume and crumb texture. The interfacial properties of gluten extracted from four commercial flours have been studied. The behaviour of gluten monolayer spread at the air-water interface is influenced by the gliadins/glutenins ratio. Films of gluten extracted from flours with high gliadins/glutenins ratio spread more quickly, present a higher stability (Pi c) and are more resistant under high compression. [less ▲]