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- W2088915604 abstract "Changes in the tensio-active properties of the main storage protein from faba beans (legumin) after succinylation were studied at a low salt concentration. Surface tension, surface dilatational properties of monolayers and emulsifying activity were measured at a ionic strength of I = 0.02. The results were compared with those at a high ionic strength of I = 0.3. Parameters of the Gibbs' adsorption isotherm indicate that the most surface-active derivatives are legumins with a moderate degree of succinylation (34% and 65%). The equilibrium surface pressure, πe, inreased from 18.47 (native legumin) to 20.72 mN/m (65% succinylation). The critical association concentration, CAC, i. e., the subphase concentration at which the plateau of πe was reached, decreased from 15.9·10–6 to 7.12·10–6 g/ml after 34% succinylation. The film forming properties differed from the adsorption behaviour. Only monolayers of the 65% succinylated legumin exhibited viscoelastic behaviour. By contrast, the emulsifying activity, EAI, reached the highest values for the 65% and 95% succinylated legumins. Low salt concentrations favour the adsorption of the native legumin and reduce the surface activity of succinylated legumin. Monolayer formation and especially the ability to form elastic networks seems to be diminished by the repulsive interaction of like-charged molecules. The emulsifying properties of the higher succinylated legumins are not influenced by the ionic strength whereas those of the native and low succinylated legumin are distinctly lower at I = 0.02. This result points to different adsorption and stabilizing processes during emulsion formation." @default.
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- W2088915604 date "1999-01-01" @default.
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- W2088915604 title "Interfacial behaviour of succinylated faba bean legumin at low ionic strength" @default.
- W2088915604 doi "https://doi.org/10.1002/(sici)1521-3803(19990101)43:1<9::aid-food9>3.0.co;2-v" @default.
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