The Xyn2083 from Clostridium clariflavum was a bifunctional xylanase, which consisted of two xylanase catalytic domains (glycoside hydrolase family 11 and 10, GH11 and GH10) and one non-catalytic dockerinΙ domain. In this study, the bifunctional Xyn2083 and two truncated xylanases with GH11, GH10 domain organization were expressed as soluble proteins. The enzymatic properties of these recombinant xylanases were studied. The results showed that the optimal temperature and pH value of Xyn2083 were 60 ℃ and 6.0, respectively. The Xyn2083 was stable below 60 ℃ or at pH 4.5～10.5. The hydrolytic products analysis showed that the GH11 domain and GH10 domain in Xyn2083 had the functional cooperative action in hydrolysis of xylan into xylose and xylobiose.