Effects of modified KGM on the gelling capability of fish protein: Novel insights into hooking effect

This study investigated the effects of modified Konjac-Gluco-Mannan (KGM) on the gelling capability of fish protein through experimental and dynamic simulation methods. The addition of deacetylated KGM (DKGM) and carboxymethylated KGM (CKGM) significantly increased the gel strength of myosin gel by 0.69 times and 0.36 times, respectively, compared to KGM. Notably, myosin with DKGM exhibited the highest storage modulus (G') and facilitated the conversion of α-helix structures during heating, leading to a denser gel network. Thermodynamic analysis revealed DKGM had the highest stoichiometric binding ratio with fish protein, indicating strong intermolecular interactions. Molecular docking identified binding sites between KGM tails and myosin heads, showing DKGM formed the most hydrogen bonds and hydrophobic interactions. The simulation of the DKGM-myosin complex demonstrated the highest interaction energy and lowest molecular radius of gyration, supporting the hypothesis that DKGM's tails enhance gelling capability through a hooking effect on adjacent proteins.