Camelina protein is a new source of plant protein. This work aimed to investigate the structural changes and improve functional properties of ultrasound treated camelina protein isolate (CPI). Structural analysis revealed that ultrasonic treatment did not change the molecular weight distribution of CPI, but increased the content of β-sheet. Moreover, the tertiary structure of CPI was altered under ultrasonic treatment with the tryptophan partially exposed to a polar environment characterized by intrinsic fluorescence spectra. Additionally, under ultrasonic treatment of 15 min, the particle size was reduced by 43%, the surface area between protein and water was increased, and the solubility of CPI was enhanced by 42%. Ultrasonic treatment exposed the positively charged groups inside the protein, increasing the zeta potential (from − 14.9 mV to -9.7 mV). Furthermore, the H0 was increased due to the destruction of hydrophobic interactions in the protein molecule by ultrasonic treatment, allowing the internal hydrophobic groups to be exposed. As a result, this reduced the hindrance at the air-water interface, increasing the adsorption rate, and improving the emulsifying and foaming properties. The foaming ability of CPI reached 202% at 35 min of ultrasound, which was 1.32 times that of untreated CPI. The foaming stability was best at 25 min. The emulsifying activity index increased from 10.87 m2/g to 14.09 m2/g, and the emulsifying stability index reached the highest value at 5 min. Under ultrasonic treatment, the fragmented protein surface was observed by SEM images. The finding contributes to the effective utilization of camelina protein resources.