The researchers are looking for new xylanase sources as well as molecular modification of existing xylanase. In this study, the recombinant pET28a (+) vector containing glycosyl hydrolase families 10 domain gene of xylanase Clocl-2441 from the Clostridium clariflavum was constructed and transformed to E. coli BL21 (DE3). The rXyn2441GH10 was expressed as soluble protein and purified by Ni2+-NTA affinity chromatography. The enzymatic properties analysis showed that the optimal temperature and pH value of recombinant xylanase rXyn2441GH10 were 70 ℃ and 7.0 respectively, which indicated that rXyn2441GH10 was a neutral thermophilic xylanase. rXyn2441GH10 was stable below 65 ℃ and at pH 4.0-9.0. 5 mmol/L Mg2+ increased the enzyme activity by 79.2%. The kinetic parameters of rXyn2441GH10 for beech xylan were as follows: Vmax was 1 691.5 μmol/(mg·min), Km was 2.5 mg/mL, kcat was 1 236.4/s, kcat/Km was 494.6 mL/(mg·s). Site-directed saturation mutations indicated that histidine at position 209 had an important role on enzyme activity.