Xylanase 30 A from Clostridium thermocellum functions as a glucuronoxylan xylanohydrolase

Franz St. John; Casey Crooks; Diane Dietrich; Jason Hurlbert

doi:10.1016/j.molcatb..2017.03.008

Treesearch

Xylanase 30 A from Clostridium thermocellum functions as a glucuronoxylan xylanohydrolase

Formally Refereed

Authors:

Franz St. John, Casey Crooks, Diane Dietrich, Jason Hurlbert

Year:

2017

Type:

Scientific Journal

Station:

Forest Products Laboratory

DOI:

https://doi.org/10.1016/j.molcatb..2017.03.008

Source:

Journal of Molecular Catalysis B: Enzymatic. 1-7.

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Abstract

Endoxylanases classified into glycoside hydrolase family 30 subfamily 8 (GH30-8) have been shown to hydrolyze glucuronoxylan with dependence upon the glucuronic acid (GlcA) appendage. In a recent report, the GH30-8 xylanase from Clostridium thermocellum (CtXyn30A) was shown to hydrolyze arabinoxylan which contains no GlcA. Protein structure comparison with the originally characterized GH30-8 enzymes from Bacillus subtilis and Erwinia chrysanthemi provided no insight to hypothesize why the function of CtXyn30A is unique. In this report, we show that CtXyn30A is a GlcA dependent endoxylanase with no significant activity on arabinoxylans, an anticipated result given the amino acid conservation within the substrate binding cleft.

Keywords

Glucuronoxylan xylanohydrolase, xylanase, arabinoxylan, glucuronoxylan, Clostridium thermocellum

Citation

St John, Franz J.; Crooks, Casey; Dietrich, Diane; Hurlbert, Jason. 2017. Xylanase 30 A from Clostridium thermocellum functions as a glucuronoxylan xylanohydrolase. Journal of Molecular Catalysis B: Enzymatic. 1-7 pp.