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Title: CaXyn30B from the solventogenic bacterium Clostridium acetobutylicum is a glucuronic acid-dependent endoxylanase

Source: BMC Research Notes. 13(1): 2. 6 p.

Author(s)Crooks, Casey ; Long, Liangkun ; St John, Franz J.

Publication Year: 2020  View PDF »

Category: Journal Articles

Abstract: We previously described the structure and activity of a glycoside hydrolase family 30 subfamily 8 (GH30-8) endoxylanase, CaXyn30A, from Clostridium acetobutylicum which exhibited novel glucuronic acid (GA)-independent activity. Immediately downstream from CaXyn30A is encoded another GH30-8 enzyme, CaXyn30B. While CaXyn30A deviated substantially in the highly conserved β7-α7 and β8-α8 loop regions of the catalytic cleft which are responsible for GA-dependence, CaXyn30B maintains these conserved subfamily 8 amino acid residues thus predicting canonical GA-dependent activity. In this report, we show that CaXyn30B functions as a canonical GA-dependent GH30-8 endoxylanase in contrast to its GA-independent neighbor, CaXyn30A.

Results: A clone expressing the catalytic domain of CaXyn30B (CaXyn30B-CD) exhibited GA-dependent endoxylanase activity. Digestion of glucuronoxylan generated a ladder of aldouronate limit products as anticipated for canonical GA-dependent GH30-8 enzymes. Unlike the previously described CaXyn30A-CD, CaXyn30B-CD showed no activity on arabinoxylan or the generation of appreciable neutral oligosaccharides from glucuronoxylan substrates. These results are consistent with amino acid sequence comparisons of the catalytic cleft and phylogenetic analysis.

Keywords: Glycoside hydrolase; xylanase; GH30; glucuronoxylan; bioconversion; biorefnery

Publication Review Process: Formally Refereed

File size: 1,024 kb(s)

Date posted: 09/18/2020

This publication is also viewable on Treesearch:  view
RITS Product ID: 99154
Current FPL Scientists associated with this product (listed alphabetically)
Crooks, M.E. Casey
Research Microbiologist
St. Johns, Franz
Research Microbiologist
 

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