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Cloning and expression of a Clostridium thermocellum xylanase gene in Escherichia coli
Author(s) -
Jung Kyung Hwa,
Lee Kang Moon,
Kim Hoon,
Yoon KiHong,
Park SeungHwan,
Pack Moo Young
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800201302
Subject(s) - clostridium thermocellum , xylanase , escherichia coli , biochemistry , cellulosome , xylan , clostridium , glycoside hydrolase , gene , chemistry , cloning (programming) , hydrolysis , biology , enzyme , microbiology and biotechnology , cellulase , bacteria , genetics , programming language , computer science
Abstract A Clostridium thermocellum xylanase gene, designated xynX, was cloned in Escherichia coli and was catagorized a novel gene as a result of the comparison of restriction patterns of the C. thermocellum xylanase genes so far reported. The xynX gene encodes a xylanase having the molecular weight of 105 kilodaltons. A number of smaller truncated proteins with activities towards 4‐methylumbelliferyl‐β‐d‐cellobioside and xylan were also produced. The enzyme hydrolyzed xylan to xylo‐oligosaccharide, indicating typical activity of endo‐β‐1,4‐xylanase. This endoxylanase hydrolyzed carboxymethylcellulose without notable reduction of the viscosity as an exo‐β‐1,4‐glucanase, even though the enzyme exhibited very low levels of activity against other soluble and insoluble cellulosic substrates.