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Soy protein due to its amphiphilic property has been widely accepted as an emulsifier in the food industry. Many emulsion products such as ice cream or other frozen food need freezing storage to either extend products shelf life and/or maintain the best sensory/texture attributes. In this case, the freezethaw stability is essential for this type of application. When the oilinwater emulsions were frozen, the absorption of oilwater interface was decreased, resulting in coalescence, flocculation, sedimentation, creaming, oiling off and Ostwald ripening. Therefore, the investigation of limited hydrolysis combined with Maillardinduced glycation on improving the freezethaw stability of soy protein isolate (SPI) was carried out. Soy protein isolate hydrolysate (SPH) was first prepared by trypsin with different hydrolysis degrees. Afterwards, SPI and SPH were conjugated with dextran to form a covalent complex macromolecule, which were named as SPI-D and SPH-D, respectively. Covalent bond was formed between SPI/SPH and dextran molecules via the glycation reaction when it was confirmed by grafting degree, browning index and fluorescence spectra analysis. Subsequently, the freezethaw stability of SPI-D and SPH-D was evaluated. After three freezethaw cycles, the characters of SPH-D emulsions exhibited smaller values than those of SPI-D emulsions in terms of particle size, coalescence degree and oiling off. In addition, SPH3-D emulsions were more stable after freezethaw treatment compared with other emulsions. After three freezethaw cycles, the particle size, coalescence degree and oiling off of SPH3-D were decreased by 48.28%, 81.61% and 63.81% compared with SPI-D, respectively. Confocal laser scanning microscopy (CLSM) was used to investigate its microstructure. It was found that the fresh emulsions were distributed uniformly without obvious differences. After three freezethaw cycles, there was a large number of irregularly shaped individual oil droplets appeared in SPI-D emulsions. In sharp contrast, oil droplets and aggregates were all relatively small in SPH-D emulsions, which was in accordance with the results of particle size, coalescence degree and oiling off. Thus, including information on limited proteolysis composition and SPH-D structure in order to further interpret this relation was necessary.