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The physicochemical, structural properties, antioxidant, and angiotensin I-converting enzyme (ACE) inhibitory activities of fish skin protein hydrolysate (SPH) that were freeze-dried (SPH-FD) and spray-dried (SPH-SD) were investigated. SPH-SD showed abundant volatile compounds, higher DPPH radical scavenging activity and ferrous iron chelating activity than SPH-FD, while the ABTS radical scavenging activity and ACE inhibitory activity were not influenced by the drying method. Amino acid compositions showed a higher proportion of proline and hydroxyproline residues in SPH-FD. The major molecular weights were both distributed below 1000 Da. SPH-SD had spherical structures, while SPH-FD had glass shard-like structures. The results indicated that the drying method could affect the physicochemical properties of hydrolysates, and SPH-SD showed potential prospects in developing functional fortified foods.