Effect of low degree succinylation on properties of enzyme-induced casein hydrogel.

This study examines the impact of succinic anhydride (SA) modification (0-9 %) on the gel properties of casein. Upon succinylation, the surface hydrophobicity (H) of casein initially increased before decreasing, achieving its peak at a degree of succinylation of 5.22 ± 0.16 %. The α-helix content rose to 14.13 ± 2.60 %, and the -OH peak shifted towards lower wavenumbers, suggesting enhanced hydrogen bonding within intra/intermolecular structures. The storage modulus in the rheological test escalated from 2160.11 Pa to 5047.60 Pa, and SEM analysis revealed that the optimally succinylated casein gel formed a denser and more stable gel network structure. Moreover, succinylated casein hydrogels demonstrated superior texture properties, swelling ability, and thermal stability. Molecular dynamics simulation (MD) results suggest that SA preferentially binds to LYS27 and LYS28 of β-casein via hydrogen bonds and amide bonds, respectively. The interaction between modified proteins is primarily governed by hydrogen bonds, aligning with FT-IR findings. PCA analysis identified a positive correlation between the ordered structure and gel performance. This research offers theoretical insights and reference data for modulating casein hydrogel properties through succinylation.