Thermal-induced conformational changes in the product release area drive the enzymatic activity of xylanases 10B: Crystal structure, conformational stability and functional characterization of the xylanase 10B from Thermotoga petrophila RKU-1

► The hyperthermostable xylanase 10B from Thermotoga petrophila RKU-1 produces exclusively xylobiose at the optimum temperature. ► Circular dichroism spectroscopy suggests a coupling effect of temperature-induced structural changes with its enzymatic behavior. ► Crystallographic and molecular dynamics studies indicate that conformational changes in the product release area modulate the enzyme action mode.