Modification mechanism of potato protein by twin-screw extrusion from the perspective of temperature variation.

Potato protein has attracted much attention due to its unique nutritional and structural properties. In this study, the twin-screw extrusion technology was employed to modify potato protein, while the modification mechanism was investigated from the perspective of temperature variation. Results indicated that extruded potato protein (EPP) led to the extremely significantly decreased surface hydrophobicity (1350 to 307-396) and foaming capacity (41.08 % to 11.32-22.95 %). Solubility, emulsifying capacity, hydrophobic amino acids and the maintained forces of protein conformation varied greatly with the changes of extrusion temperature. Sufficient evidences could be found in SEM, DSC, SDS-PAGE and secondary/tertiary structures of EPP, possessing the higher crosslinking degree and highly distinct structures. The potential modification mechanism was revealed in a vivid schematic diagram. Results demonstrated that twin-screw extrusion provided more possibilities for modifying the highly heterogeneous structure of potato protein, highlighting a promising strategy for its high-value application in food production.