Effect of ultrasonic pre-treatment on Ara h 1 in peanut sprouts

•US pre-treatment had profound effects on Ara h 1 protein in peanut sprouts.•Protease activity increased significantly during germination after US.•Cavitation and the heat effect from US destroyed intramolecular hydrogen bonds and resulted in the blue shift phenomenon.•The gene expression level of Ara h 1 was significantly lower in the US group than in the control BK group. Ara h 1 is the most abundant sensitizing protein in peanuts; it has high thermal stability and is difficult to degrade. The peanut sprout is a high-quality, natural food that has various beneficial effects and lower allergenicity than peanut seeds. In this study, ultrasonication (US) of peanut sprouts was used to alter their Ara h 1 content. We determined that the optimal parameters for the US process were 35 °C temperature, 30 min duration, 240 W power, and 100 kHz frequency. After 5 days of germination, the protease activity of the control (blank) group increased to 262.39 ± 0.10 U, whereas that of the US group increased to 290.1 ± 0.25 U. We also investigated the effects of US on Ara h 1 protein composition, structure, and related gene expression during germination. ELISA results showed that after 5 days of germination, Ara h 1 content in the blank group decreased from 20.63 ± 0.31 ppm to 3.35 ± 0.42 ppm, whereas in the US group, they decreased to below the detection limit. SDS-PAGE bands between 50 and 70 kDa from peanut sprout extracts gradually became lighter in both groups. The band almost disappeared at day 5 of germination in the US group, indicating that US reduced the Ara h 1 content of peanut sprouts, consistent with the ELISA results. The expression of the Ara h 1 gene in peanut seeds was 173.92 ± 26.37. In the BK control group, it decreased to 0.49 ± 0.17 on the fourth day and increased slightly to 0.75 ± 0.09 on the fifth day. In the US group, it decreased to 1.37 ± 0.28 on the first day, dropped sharply to 0.00 on the third day, and increased slightly to 0.04 ± 0.01 on the fourth and fifth days. Protein structure results showed that the α-helix structure of Ara h 1 decreased after US, whereas the content of β-fold structures increased. The surface hydrophobicity decreased, and the secondary and tertiary structures of Ara h 1 were loose.