Structural and functional changes induced by different ultrasound-frequency-assisted xylose-glycation inhibits lysinoalanine formation in Tenebrio molitor protein.

We explored the effects of sonication-assisted xylose (Xyl) grafting on the structure and functionality of Tenebrio molitor protein (MP). Different ultrasound frequencies (20, 25, 28, 20/25, 20/28, 25/28, 20/25/28 kHz) were used, and the inhibition mechanism of ultrasound-assisted Xyl grafting on the formation of lysinoalanine (LAL) was explored. The results suggested that the turbidity and browning products of MP significantly increase, with MP-Xyl-20 kHz exhibiting the highest grafting degree (43.78 %). Compared with MP, the total sulfhydryl content of MP-Xyl and MP-Xyl-20 kHz was significantly improved by 21.90 % and 98.80 % (P < 0.05). Circular Dichroism, Fourier Transform Infrared Spectroscopy, SEM, and AFM analysis showed changes in MP conformation following various frequencies ultrasound-assisted glycosylation. Notably, emulsifying capacity, stability, and foaming ability of MP-Xyl-20 kHz were significantly enhanced by 97.08 %, 48.03 %, and 55.01 %, respectively, compared with MP. The glycol-conjugated MP treated with ultrasound-assisted glycosylation (MP-Xyl-25/28 kHz) had the lowest LAL content (7.19 μg/mg), representing a 56.56 % and 46.70 % decrease compared to the control MP and MP-Xyl, respectively. The content of LAL exhibited a positive correlation with surface hydrophobicity, whereas it demonstrated a negative correlation with sulfhydryl and carbonyl groups. These findings indicated that sonication-assisted xylose improved the functional characteristics of MP, and the inhibition effect on LAL formation. The outcome of the study could be very beneficial in the modification of MP for food industrial applications.