The present study aims at investigating the absorption behaviour of acetylated (AFBPI) and non-acetylated (FBPI) faba bean protein isolate at a sunflower oil-water interface in dependence on different environmental conditions (protein concentration, pectin addition).
Materials and methodsSpray dried AFBPI and FBPI were produced from faba bean as described previously [l]. The acetylation degree of protein determined according [2] was 97%. The oil phase was commercial sunflower oil purified by treatment with aluminium oxide [3]. All aqueous solutions contained 0.02% sodium azide. A 1 % protein basic suspension was prepared by dispersing the isolate in bidistilled water (pH 6.5) at 25 "C with a magnetic stirrer. A 1 % pectin basic solution was produced by dispersing of low methoxy pectin (Herbstreith KG, Numberg, FRG, mole mass 29,400, average degree of esterification of 32%) also in bidestilled water (pH 6.5) at 80 "C with a mechanical stirrer. The pectin solution was centrifugated at 15,000 x g for 30 min and the resulting protein suspension was separated from the slurry at 3,800 x g for 20 min. After determination of the protein isolate and pectin contents by the dry weight method the basic solutions were diluted at the desired concentrations. All pH adjustments were made with 0.5 N NaOH and 0.1 N HCI solutions, respectively.The interfacial tension was measured with a KRUSS digital tensiometer (KRUSS, Hamburg, FRG) using the plate method and checking with the ring. The starting point was set by determining a first value 5 min after the oil layering. All measurements were made at a temperature of 25 "C.
ResultsThe interfacial tension value of the oil-bidistilled water interface at pH 7.0 is 28.4 mN/m and remains constant during the measuring time. The influence of concentration of AFBPI and FBPI on the time dependent reduction of interfacial tension between the oil and the water phase at pH 7.0 is shown in Fig. 1. The protein concentration affects the initial and the final values and also the reduction rate of the interfacial tension. The higher the protein concentration the lower is the interfacial tension and the higher the reduction rate, i. e. the steady-state level is reached more quickly. The reduction of the interfacial tension is higher in the case of AFBPI than in the case of FBPI. A pure pectin solution in water at pH 7.0 decreases the interfacial tension but only to a certain extent (Fig. 2). The mixture of pectin with AFBPI leads to a considerable increase of initial and final values of the interfacial tension. The reduction rate of the interfacial tension is decreased. Concerning the initial value the addition of pectin to FBPI produces a remarkable lower interfacial tension compared with the addition to AFBPI. The steady-state values are comparable with those values of FBPI in water (Fig. 1). Iqcreased pectin concentration increases the interfacial tension. In the case of AFBPI this effect is pronounced.