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BACKGROUND Goose meat was rough and embedded with dense connective tissue, impairing protein solubility. Therefore, in order to improve the functional properties of goose myofibrillar protein (GMP), ultrasound was used to assist phosphorylation of GMP. RESULTS The fact, GMP attached covalently with the phosphate group of sodium tripolyphosphate (GMP-STP), was disclosed directly by the Fourier transform infrared spectroscopy (FT-IR). Furthermore, ultrasound significantly improved the hydrophobicity and solubility of GMP-STP, which could be attributed to the conversion of α-helix to β-sheet, β-turns, and random coils by sonication. The spatial stabilization of the protein phosphorylation process was boosted by ultrasound, making the droplets more dispersed, and thus, an improvement in the functional properties of GMP-STP was observed. Water-holding capacity, oil-binding capacity, emulsifying and foaming properties were the best at ultrasound power of 400 W. CONCLUSION Ultrasound-assisted phosphorylation has great potential to modulate the structure-function relationship of proteins. This article is protected by copyright. All rights reserved.