Changes in interfacial behaviour, emulsifying and foaming properties of faba bean legumin after modification with dimethylsuberimidate.
The effect of a rising rigidity and surface hydrophobicity of the 11S storage protein from faba beans--legumin--induced by chemical modification with dimethylsuberimidate (DMS) on some surface functional properties was studied. Short-time adsorption kinetics using a droplet-volume tensiometer, pressure transformation and desorption behaviour of monolayer using a film balance, and emulsifying and foaming properties were determined to characterize surface activity and interfacial film forming behaviour. Tensio-active properties at the air-water interface, i.e. decay in surface tension and pressure transformation in monolayer, were improved by modification. However, a decrease in emulsifying activity, foam capacity and foam expansion after modification of the legumin points to an overall deterioration of energy-induced film forming behaviour. The results support the view that surface activity is generally governed more by molecular flexibility than by surface hydrophobicity.
Krause
J P
JP
Institut für Angewandte Proteinchemie, c/o BBA, Stahnsdorfer Damm 81, D-14532 Kleinmachnow, Germany. food.proteins@prochem.shuttle.de
Dudek
S
S
Schwenke
K D
KD
D004120:Dimethyl Suberimidate / Q000737:chemistry*; D004655:Emulsions; D007525:Isoelectric Focusing; D010940:Plant Proteins / Q000737:chemistry* / Q000187:drug effects; D013500:Surface Tension; D013816:Thermodynamics; D000097793:Legumins
D004120:Dimethyl Suberimidate; D004655:Emulsions; D010940:Plant Proteins; D000097793:Legumins