Foaming properties of protein/pectin electrostatic complexes and foam structure at nanoscale.
The foaming properties, foaming capacity and foam stability, of soluble complexes of pectin and a globular protein, napin, have been investigated with a "Foamscan" apparatus. Complementary, we also used SANS with a recent method consisting in an analogy between the SANS by foams and the neutron reflectivity of films to measure in situ film thickness of foams. The effect of ionic strength, of protein concentration and of charge density of the pectin has been analysed. Whereas the foam stability is improved for samples containing soluble complexes, no effect has been noticed on the foam film thickness, which is almost around 315Å whatever the samples. These results let us specify the role of each specie in the mixture: free proteins contribute to the foaming capacity, provided the initial free protein content in the bulk is sufficient to allow the foam formation, and soluble complexes slow down the drainage by their presence in the Plateau borders, which finally results in the stabilisation of foams.
Schmidt
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I
UR1268 Biopolymères Interactions Assemblages, INRA, F-44300 Nantes, France.
Novales
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B
Boué
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F
Axelos
M A V
MA
D055516:2S Albumins, Plant / Q000737:chemistry*; D009994:Osmolar Concentration; D010368:Pectins / Q000737:chemistry*; D055672:Static Electricity
D055516:2S Albumins, Plant; D010368:Pectins