| Summary: | 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 <i>r</i> = 5:1 and pH<sub>max</sub> (pH 3.41) by forming insoluble complexes; and only soluble complexes were formed at <i>r</i> = 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.
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