In the GH11 family of xylanases, the cord region, a dynamic peptide linker connecting the "thumb" and "palm" regions, exhibits remarkable flexibility. To reveal the structure-function relationship in this region, saturation mutagenesis was performed on the cord segment of XynASP, a xylanase derived from Aspergillus saccharolyticus JOP 1030⁃1 GH11. Among the generated mutants, two variants, D116S and E119V, showed superior enzymatic properties and were subsequently combined to generate XynASP-SV. XynASP-SV exhibited a 3.05-fold increase in specific enzyme activity compared to the wild type, a 6 °C rise in T