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United States Department of Agriculture

Agricultural Research Service

Title: Beta-D-Xylosidase from Selenomonas Ruminantium of Glycoside Hydrolase Family 43

Authors
item Jordan, Douglas
item Li, Xin Liang
item Dunlap, Christopher
item Whitehead, Terence
item Cotta, Michael

Submitted to: Gordon Research Conference Proceedings
Publication Type: Abstract Only
Publication Acceptance Date: July 22, 2006
Publication Date: July 22, 2006
Citation: Jordan, D.B., Li, X., Dunlap, C.A., Whitehead, T.R., Cotta, M.A. 2006. Beta-D-xylosidase from Selenomonas ruminantium of glycoside hydrolase family 43 [abstract]. Gordon Research Conference. p. 3.

Technical Abstract: Certain strains of the ruminal anaerobic bacterium, Selenomonas ruminantium, have been shown to enhance utilization of xylooligosaccharides under fermentation conditions. Preparations of S. ruminantium beta-D-xylosidase were shown to act on 4-nitrophenyl-beta-D-xylopyranoside and 4-nitrophenyl-alpha-L-arabinofuranoside with a 10-fold preference of the former substrate over the latter. Moreover, natural oligosaccharides, produced from reacting oatspelt xylan and wheat arabinoxylan with a xylanase, were accepted as substrates by the enzyme. Recently, X-ray structures of beta-D-xylosidase belonging to glycoside hydrolase family 43 have been reported for the enzyme from different species. The amino acid sequence of the xylosidase from Clostridium acetobutylicum has 72% identity with that of the S. ruminantium enzyme, and its X-ray structure was used to model the active site of the S. ruminantium enzyme. Beta-xylosidase from S. ruminantium, heterologously expressed in Escherichia coli, was purified to homogeneity for structure and function studies. Steady-state kinetic studies determined that the xylosidase is highly active on natural and artificial substrates. Substrate specificities, reaction stereochemistry, and effects of pH, temperature, and site-directed mutations were determined for the enzyme.

Last Modified: 11/20/2014