In　order　to　study　the　effect　of　cold　chain　storage　on　the　structural　and　functional　properties　of　myofibrillar　protein　and　the　chemical　interactions　of　surimi　gel,　the　changes　in　the　functional　groups　and　secondary　and　tertiary　structure　of　myofibrillar　protein　and　the　chemical　interactions　of　surimi　gel　were　investigated　as　a　function　of　cold　chain　storage　time,　and　the　relationship　between　chemical　interactions　and　myofibrillar　protein　was　evaluated　by　principal　component　analysis　(PCA)and　correlation　analysis.　Results　showed　that　the　salt-soluble　protein　content,　Ca2+-ATPase　activity　and　total　sulfhydryl　content　in　surimi　gel　decreased,　while　the　carbonyl　content　increased　during　storage.　In　addition,　the　secondary　structures　of　myofibrillar　protein　transformed　from　an　ordered　to　a　disordered　state,　and　the　fluorescence　intensity　decreased,　indicating　changes　in　the　polar　environment　of　the　protein.　These　findings　demonstrate　that　the　active　groups　in　myofibrillar　protein　are　closely　related　to　the　formation　of　gel　chemical　forces.　Therefore,　preventing　protein　oxidation　and　freeze　denaturation　at　the　initial　stage　of　storage　is　an　effective　way　to　maintain　the　chemical　interactions　of　surimi　gel　and　the　gel　characteristics.　This　study　can　provide　basic　theoretical　support　for　the　quality　maintenance　of　surimi　during　cold　chain　storage.　©　2022,　China　Food　Publishing　Company.　All　right　reserved.