Gel　property　is　one　of　the　most　important　abilities　to　surimi　products.　In　this　research,　the　β-glucan　from　yeast　and　oat　were　applied　in　enhancing　the　gel　properties　of　unwashed　surimi　gel.　The　texture　profile　analysis　(TPA),　storage　modulus　(G＇),　loss　modulus　(G＇)　of　unwashed　surimi　gel,　and　β-glucan　linking　with　myofibrillar　protein　were　investigated,　at　the　addition　of　0　%–1.5　%　β-glucan.　The　β-glucan　from　yeast　and　oat　could　induce　more　unfolding　and　promoted　cross-linking　of　myofibrillar　protein,　improving　the　hardness　and　gel　strength　of　unwashed　surimi　gel.　At　the　1.0　%　addition　of　yeast　β-glucan　(YG)　or　oat　β-glucan　(OG),　the　gel　strength　of　unwashed　surimi　gel　increased　by　434.30　g·mm　and　314.39　g·mm,　respectively,　compared　with　the　control.　In　addition,　YG　with　a　branched-chain　structure　was　more　likely　to　crosslink　with　myofibrillar　protein　(MHC)　through　hydrogen　bond,　and　YG-MHC　CDOCKER　energy　lower　than　OG-MHC,　proved　by　molecular　docking　analysis.　The　grafting　degree　and　intermolecular　interactions　in　the　YG　treated　surimi　gel　are　stronger　than　those　in　the　OG　one,　enhancing　the　physical　properties　and　WHC　of　unwashed　surimi　gel.　However,　as　the　added　amount　β-glucan　increased　1.5　%,　the　pores　in　the　network　became　excessively　expansive,　the　continuous　structure　of　the　myofibrillar　protein　was　gradually　destroyed,　leading　to　the　decreasing　gel　properties　and　rheological　properties.　In　conclusion,　1.0　%　YG　treatment　can　effectively　improve　the　gel　properties　of　unwashed　surimi　gel,　providing　a　practical　method　for　the　processing　of　myofibrillar　protein　based　gel　products.　©　2025　Elsevier　Ltd