Desmodium intortum (Mill.) Urb. Protein Isolate Aggregates as Pickering Stabilizers: Physicochemical Characteristics and Emulsifying Properties

This work aimed to investigate the feasibility of fabricating Pickering emulsions stabilized by <i>Desmodium intortum</i> protein isolate (DIPI) aggregates. The DIPI aggregates were formed using heat treatment, and the effects of ionic strength and pH on their properties were investigated. The heat-treated protein exposes its hydrophobic groups due to structural damage, resulting in rapid aggregation of the protein into aggregates with a size of 236 nm. The results showed that the aggregates induced by ionic strength had larger particle size and higher surface hydrophobicity and partial wettability. Moreover, this study explored effective strategies for bolstering Pickering emulsion stability through optimized DIPI aggregate concentration (c) and oil fraction (ø). The DIPI Pickering emulsion (DIPIPE) formed at c = 5% and ø = 0.7 was still highly stable after 30 days of storage. As confirmed by laser confocal microscopy, DIPI aggregates could be adsorbed onto the oil-water interface to form a network structure that could trap oil droplets in the network. Collectively, the Pickering emulsion stabilized by DIPI aggregates exhibited excellent stability, which not only deeply utilizes the low-value protein resources in the <i>Desmodium intortum</i> for the first time, but also demonstrates the potential of DIPI for the bio-based field.