Recovery and Utilization of Pea Albumins as Acidic Emulsion Stabilizer by Complexation with Dextran Sulfate

Abstract

In this work, pea albumins (PAs) were efficiently recovered by complexation with dextran sulfate (DS), and the emulsifying ability and stability of PA/DS complexes were studied. The largest amounts of PAs (81.25%) were recovered at r = 5:1 and pHmax (pH 3.41) by forming insoluble complexes; and only soluble complexes were formed at r = 2:1 and over the whole pH range (2.0–7.0). The emulsions stabilized by PA/DS soluble complexes remained stable under acidic conditions due to the highly negatively charge (from −45.10 ± 0.40 to −57.23 ± 0.66 mV) and small particle size (0.168 ± 0.010–0.448 ± 0.004 μm), while emulsions stabilized by PAs alone generated a strong creaming and serum separation at pH 5 and 6. In terms of emulsifying stability, all PA emulsions and unheated PA/DS emulsions became unstable with different creaming index after 14 days storage. SDS-PAGE results showed that the interface adsorption proteins of unheated emulsions mainly consisted of PA1a, which was unfavorable to the stability of the interface. On the contrary, heat treatment (95 °C, 30 min) and complexation (PA/DS = 2:1) enhanced the adsorption of PA2 and lectin at the interface, inhibiting the aggregation of PA2 and lectin. This resulted in long-term stability of the PA/DS emulsions under acidic conditions.