Antarctic krill proteins (AKPs) were successfully succinylated by using succinic anhydride, and the physicochemical and functional properties of the succinylated proteins as well as their ability to protect active curcumin were investigated. The results showed that the succinylation reaction decreased the particle size and hydrophobicity but increased the surface charge of AKPs, which greatly improved the solubility and emulsification of the proteins. On this basis, the succinylated AKPs presented an excellent ability to encapsulate curcumin to prepare emulsions and endowed the emulsions with good physical performance to resist the stress of photothermal treatment, salt and different temperatures. Notably, the succinylated proteins protected encapsulated curcumin from degradation more effectively than the reported protein-phenolic conjugates of carboxymethyl dextrin (CMD)-curcumin and zein-curcumin. These findings indicate that the succinylated AKPs are a promising food resource and present great potential for application in the food industry. • Antarctic krill proteins were covalently modified via succinylation reaction. • The solubility and emulsifying ability of the succinylated proteins were improved. • The succinylated proteins-stabilized emulsions presented an excellent stability. • The succinylated proteins endowed the emulsions with good resistance to stress. • The succinylated proteins effectively protected the curcumin from being degraded. [ABSTRACT FROM AUTHOR]