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  • Title: Cloning and expression of a Clostridium thermocellum xylanase gene in Escherichia coli.
    Author: Jung KH, Lee KM, Kim H, Yoon KH, Park SH, Pack MY.
    Journal: Biochem Mol Biol Int; 1998 Feb; 44(2):283-92. PubMed ID: 9530511.
    Abstract:
    A Clostridium thermocellum xylanase gene, designated xynX, was cloned in Escherichia coli and was categorized 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-beta-D-cellobioside and xylan were also produced. The enzyme hydrolyzed xylan to xylo-oligosaccharide, indicating typical activity of endo-beta-1,4-xylanase. This endoxylanase hydrolyzed carboxymethylcellulose without notable reduction of the viscosity as an exo-beta-1,4-glucanase, even though the enzyme exhibited very low levels of activity against other soluble and insoluble cellulosic substrates.
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