Abstract Pea proteins (PPs) have limited application in the food industry due to their unfavorable solubility and poor digestibility. This study aimed to improve the quality of PPs through physical modifications followed by 24 h of fermentation using Lactiplantibacillus plantarum ATCC 8014. The conformational, secondary, and tertiary structures of both fermented and unfermented PPs were analyzed using ultraviolet, fluorescence, and Fourier-transform infrared spectroscopy (FTIR) spectroscopies. The results showed substantial modifications to the protein structure during fermentation. Specifically, water solubility increased (P0.05) from 78.03% to 84.43%, while digestibility improved (P0.05) from 84.77% to 89.95%. Substantial changes were also observed in surface properties. Particle size shifted (P0.05) from 750.6 to 877.0 nm, and surface charge changed (P0.05) from -33.40 to -39.87 mV. Conversely, surface hydrophobicity decreased (P0.05) from 384 to 270 a.u. Furthermore, the total phenolic content increased (P0.05) during fermentation, reaching approximately 789.64 mg GAE/100 g. In summary, fermenting PPs with L. plantarum can effectively enhance their digestibility, protein structure, and nutritional value.
Hani et al. (Fri,) studied this question.