Enhancing gel behavior of yellow croaker surimi by fruit extracts: Physicochemical properties and molecular mechanism

The aim of this study was to investigate the effects of grape seed extract (GSE), acerola cherry extract (ACE), and blueberry extract (BBE) on the physicochemical properties and structure of the yellow croaker surimi gel. In addition, molecular docking and molecular dynamics (MD) simulation were utilized to study the binding mechanism of yellow croaker's fibrillin and fruit extracts. Surimi gel with 1.5% GSE, ACE, and BBE had the highest water holding capacity, hardness, chewability, cohesion, breaking force, breaking distance, gel strength, and densest 3D network structure, according to the experiment's findings. Nevertheless, the cross-linking of proteins in surimi was blocked with the further increase of fruit extract (1.5%–2.0%), and the existing network of surimi was weakened or even destroyed. Three fruit extracts had little effect on the secondary structure of the surimi gel. Besides, hydrophobic and disulfide bonds are the main chemical bonds of croaker surimi. Molecular docking showed that B-type procyanidine (BP) interacted with ASN-183, SER-571, ASP-525, ARG-350, LYS-188, GLU-349, CYS-353, and other active amino acids in croaker protein. Moreover, it can form strong hydrogen bond interaction with ASN-183, SER-571, ASP-525, and ARG-350 at the active sites of protein. The BP- Larimichthys crocea protein system's MD simulation was carried out, and calculations for the simulation's root mean square deviation, root mean square fluctuation, radius of gyration, solvent accessible surface area, and hydrogen bonds were made. It was found that these indices can demonstrate that the BP binding contributes to the stability of the yellow croaker structure.