Germination as a Pre-isolation Modification Method for Common Buckwheat Protein Isolate.

This study investigated germination as a pre-isolation modification method to enhance the techno-functional and nutritional properties of common buckwheat (Fagopyrum esculentum Moench) protein. Germination was conducted at two different temperatures (20 and 30 °C) for 24, 48, and 72 h, and isolated proteins were analyzed for their chemical, structural, and functional properties. Results showed that the highest protein yield was achieved at 30 °C for 24 h, though durations exceeding 48 h reduced purity. SDS-PAGE and FTIR analyses confirmed that endogenous protease activity degraded high-molecular-weight proteins and increasing random coil proportions, indicating partial unfolding. SEM imaging revealed that germination transformed the dense protein surface into a porous morphology. Increasing germination time and temperature led to decreased lightness (L*) and hue angle, along with moderate increases in redness (a*), indicating notable changes in the visual appearance of the protein isolates. DSC results showed a decrease in thermal stability (Td) due to structural changes. In addition, germination significantly improved solubility, emulsifying activity, foaming capacity, and water/oil absorption, particularly at the 24 h of germination. Most notably, germination at 30 °C for 24 h increased in vitro protein digestibility from 75.67 to 82.19%. The results show that the germination is a promising approach to enhance the functionality and digestibility of buckwheat protein for potential application in food industry.