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 a hydrolysis degree of 2% and 5%. Afterwards, SPI and SPH were conjugated with dextran to form a covalent complex macromolecule, which were named SPI-D, SPH2-D and SPH5-D, respectively. Covalent bond was formed between SPI/SPH and dextran molecules via the glycation reaction has been confirmed by fourier transform infrared (FTIR) spectroscopy 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 oiling off, particle size, flocculation degree (FD) and coalescence degree (CD). In addition, SPH2-D emulsions were more stable after freeze-thaw treatment compared with SPH5-D emulsions. Optical microscopy analysis also supported the results above.

进行了有限水解结合美拉德诱导的糖基化改善大豆分离蛋白（SPI）冻融稳定性的研究。首先用胰蛋白酶制备大豆分离蛋白水解物（SPH），水解度为2％和5％。然后，将SPI和SPH与葡聚糖偶联形成共价复合大分子，分别命名为SPI-D，SPH2-D和SPH5-D。SPI / SPH和葡聚糖分子之间通过糖基化反应形成共价键已通过傅立叶变换红外光谱（FTIR）光谱分析得到证实。随后，评估了SPI-D和SPH-D的冻融稳定性。经过三个冻融循环后，SPH-D乳液的油性，粒径，絮凝度（FD）和聚结度（CD）。另外，与SPH5-D乳液相比，冻融处理后的SPH2-D乳液更稳定。光学显微镜分析也支持上述结果。