Cloning, expression, and characterization of Pseudomonas vesicularis MA103 β-1,3-xylanase in Escherichia coli ClearColi BL21(DE3)

Xylanase is one of the most important hydrolyzed enzymes with multiple functions in industry processing. Since there has been limited research related to beta-1,3-xylanse, more attention needs to be paid to discovering an efficient way to produce this enzyme. In the present study, beta-1,3-xylanase gene (xylII) from Pseudomonas vesicularis MA103 was cloned into pET-39b(+) expression vector and transformed into Escherichia coli ClearColi BL21(DE3). The catalytic domain of the beta-1,3-xylanase (XYLII) belongs to family 26 of glycoside hydrolases, and is followed by two family 31 carbohydrate-binding modules at the C terminus. beta-1,3-xylanase showed an optimal activity at 35 A degrees C and pH 7.5. According to its substrate specificity, the purified XYLII was considered to be an endo-type beta-1,3-xylanase (EC 3.2.1.32). Experimental results of this work suggested an efficient way to obtain beta-1,3-xylanase with great potential in industry applications. These findings can be helpful to explore and study the use of beta-1,3-xylanase in the future and further associated investigation.