Dithiothreitol-induced reassembly of soybean lipophilic protein as a carrier for resveratrol: Preparation, structural characterization, and functional properties

[Display omitted] •Dithiothreitol (DTT) induces soy lipophilic protein (LP) recombination.•Changes in LP structure and property depend on DTT dosage.•Recombinant LP shows better performance as carrier for resveratrol (Res).•Hydroxypropyl methylcellulose stabilizes protein nanoparticles and Res. We employed dithiothreitol (DTT) to reassemble soy lipophilic protein (LP) and increased its solubility for encapsulating resveratrol (Res); we subsequently added hydroxypropyl methylcellulose (HPMC) to further stabilize Res. Physicochemical characterization, sodium dodecyl sulfate–polyacrylamide gel electrophoresis, and spectral analysis revealed that DTT triggered the breakage and reassembly of the disulfide bond. Consequently, the solubility of LP increased from 38.64 % to 71.49 %, and the number of free sulfhydryl groups increased to 7.84 mol·g−1. Furthermore, the encapsulation efficiency and structure of reassembled LP nanoparticles loaded with Res were found to be closely related to the DTT concentration used for induction. When HPMC was added, the LP-Res complex demonstrated spontaneous self-assembly, and the pH and temperature stability of the Res in the nanoparticles improved. An in vitro digestion simulation revealed that the reassembled LP was an efficient carrier for Res delivery. Particularly, HPMC improved the bioavailability and sustained release of Res.