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To understand the interactions between enzyme-modified potato proteins and potato starch, herein transglutaminase or peroxidase was used to create covalent crosslinked structure of potato protein. The mixtures of native or enzyme-treated protein and potato starch in different proportions were prepared and the structural and physicochemical characteristics were studied. The results revealed that the new covalent and/or noncovalent linkages formed after enzyme modification of potato protein. Compared with the mixtures of native protein and starch, the mixtures of enzyme-treated protein and starch had larger shear resistance (breakdown value decreased by about 2–100 times) and higher gel strength (G′ and G″), but smaller thermal stability (312.3–307.3, 309.1 °C) and lower peak viscosity (decreased by 1.5–4 times). In conclusion, transglutaminase or peroxidase accelerated the formation of cross-networked structure in potato protein, which increased the interaction with starch, hence greatly improving the gel properties of the mixture of protein and starch.
Gui et al. (Mon,) studied this question.