Cloning, expression, and characterization of Pseudomonas vesicularis MA103 β-1,3-xylanase in Escherichia coli ClearColi BL21(DE3)
Fisheries Science(2015)
摘要
Xylanase is one of the most important hydrolyzed enzymes with multiple functions in industry processing. Since there has been limited research related to β-1,3-xylanse, more attention needs to be paid to discovering an efficient way to produce this enzyme. In the present study, β-1,3-xylanase gene ( xyl II) from Pseudomonas vesicularis MA103 was cloned into pET-39b(+) expression vector and transformed into Escherichia coli ClearColi BL21(DE3). The catalytic domain of the β-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. β-1,3-xylanase showed an optimal activity at 35 °C and pH 7.5. According to its substrate specificity, the purified XYLII was considered to be an endo-type β-1,3-xylanase (EC 3.2.1.32). Experimental results of this work suggested an efficient way to obtain β-1,3-xylanase with great potential in industry applications. These findings can be helpful to explore and study the use of β-1,3-xylanase in the future and further associated investigation.
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关键词
Pseudomonas vesicularis MA103,Β-1,3-xylanase,Expression
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