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Title: Xylanase 30 A from Clostridium thermocellum functions as a glucuronoxylan xylanohydrolase

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

Author(s)St John, Franz J.; Crooks, Casey; Dietrich, Diane; Hurlbert, Jason

Publication Year: 2017  View PDF »

Category: Journal Articles
Associated Research Project(s):   FPL-4712-3B

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

Publication Review Process: Formally Refereed

File size: 3,072 kb(s)

Date posted: 10/06/2017

This publication is also viewable on Treesearch:  view
RITS Product ID: 88485
Current FPL Scientists associated with this product (listed alphabetically)
Crooks, M.E. Casey
Research Microbiologist
St. Johns, Franz
Research Microbiologist
 

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