Effect of dual-frequency ultrasound on the formation of lysinoalanine and structural characterization of rice dreg protein isolates.

The effect of dual-frequency ultrasound treatment with different working modes on the lysinoalanine (LAL) formation and structural characterization of rice dreg protein isolates (RDPI) was studied during alkaline exaction processing. Ultrasonic notably decreased the LAL amount of RDPI and enhanced the protein dissolution rate. The LAL content of RDPI, especially sequential dual frequency 20/40 kHz, decreased by 12.02% (P < 0.05), compared to non-sonicated samples. Herein, the protein dissolution rate was higher. The changes in sulfhydryl groups was positively correlated with the LAL formation. The amino acids (AA) such as threonine (Thr), lysine (Lys), and arginine (Arg) were reduced, resulting in a decrease in LAL content following sonication. Besides, ultrasonication altered protein secondary structure by reducing random coil and β-sheet contents, while α-helix and β-turn contents increased. Alterations in the surface hydrophobicity, particle size, particle size distribution, and microstructure indicated more irregular fragment with microparticles of RDPI by sonochemical treatment. Thus, ultrasound treatment may be a new and efficacious process for controlling the LAL generation in prepared-protein food(s) during alkali extraction.