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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39252

Title: Cloning, expression, and characterization of Pseudomonas vesicularis MA103 β-1,3-xylanase in Escherichia coli ClearColi BL21(DE3)
Authors: Chorng-Liang Pan
Wen-Sing Liang
Tsuei-Yun Fang
Hong-Ting Lin
Tristan C. Liu
Wen-Jung Lu
Wen-Shyong Tzou
Shye-Jye Tang
Fu-Pang Lin
Shiu-Mei Liu
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: Pseudomonas vesicularis MA103
Β-1,3-xylanase
Expression
Date: 2015-11
Issue Date: 2016-11-30T07:40:54Z
Publisher: Fisheries Science
Abstract: Abstract: 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 (xylII) from Pseudomonas vesicularis MA103 was cloned into pET-39b(+) expression vector and transformed into Escherichiacoli 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.
Relation: 81(6)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39252
Appears in Collections:[食品科學系] 期刊論文

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