HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Adelsberger, H. Articles by Schwarz, W. H. Search for Related Content PubMed PubMed Citation Articles by Adelsberger, H. Articles by Schwarz, W. H. Agricola Articles by Adelsberger, H. Articles by Schwarz, W. H.

Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes

Helmuth Adelsberger^1,

Christian Hertel^1,

Erich Glawischnig^1,

¹ Research Group Microbial Biotechnology, Technische Universität München, Am Hochanger 4, D-85350 Freising-Weihenstephan, Germany
² Institute of Molecular Genetics, Russian Academy of Science, Kurchatov Square, 123182 Moscow, Russia

Correspondence
Wolfgang H. Schwarz
schwarz{at}mikro.biologie.tu-muenchen.de

Four extracellular enzymes of the thermophilic bacterium Clostridium stercorarium are involved in the depolymerization of de-esterified arabinoxylan: Xyn11A, Xyn10C, Bxl3B, and Arf51B. They were identified in a collection of eight clones producing enzymes hydrolysing xylan (xynA, xynB, xynC), -xyloside (bxlA, bxlB, bglZ) and -arabinofuranoside (arfA, arfB). The modular enzymes Xyn11A and Xyn10C represent the major xylanases in the culture supernatant of C. stercorarium. Both hydrolyse arabinoxylan in an endo-type mode, but differ in the pattern of the oligosaccharides produced. Of the glycosidases, Bxl3B degrades xylobiose and xylooligosaccharides to xylose, and Arf51B is able to release arabinose residues from de-esterified arabinoxylan and from the oligosaccharides generated. The other glycosidases either did not attack or only marginally attacked these oligosaccharides. Significantly more xylanase and xylosidase activity was produced during growth on xylose and xylan. This is believed to be the first time that, in a single thermophilic micro-organism, the complete set of enzymes (as well as the respective genes) to completely hydrolyse de-esterified arabinoxylan to its monomeric sugar constituents, xylose and arabinose, has been identified and the enzymes produced in vivo. The active enzyme system was reconstituted in vitro from recombinant enzymes.

The GenBank/EMBL/DDBJ accession numbers for the sequences reported in this paper are: AJ508406 (Arf39A), Z94045 (Bgl3Z), AJ508404 (Bxl39A), AJ508405 (Bxl3B), AJ508407 (Xyn10B), AJ508408 (Xyn10C), and AJ508403 (Xyn11A).

Present address: II. Medical Hospital and Health Center, TU München, Klinikum rechts der Isar, Ismaninger St. 22, D-81675 München, Germany.

Present address: Institute of Food Technology, University of Hohenheim, Garbenstr. 28, D-70593 Stuttgart, Germany.

Present address: Institut für Genetik, TU München, Am Hochanger 8, D-85350 Freising, Germany.

This article has been cited by other articles:

				S. D. Bentley, C. Corton, S. E. Brown, A. Barron, L. Clark, J. Doggett, B. Harris, D. Ormond, M. A. Quail, G. May, et al. Genome of the Actinomycete Plant Pathogen Clavibacter michiganensis subsp. sepedonicus Suggests Recent Niche Adaptation J. Bacteriol., March 15, 2008; 190(6): 2150 - 2160. [Abstract] [Full Text] [PDF]

				S. Shulami, G. Zaide, G. Zolotnitsky, Y. Langut, G. Feld, A. L. Sonenshein, and Y. Shoham A Two-Component System Regulates the Expression of an ABC Transporter for Xylo-Oligosaccharides in Geobacillus stearothermophilus Appl. Envir. Microbiol., February 1, 2007; 73(3): 874 - 884. [Abstract] [Full Text] [PDF]

				T. Kotake, K. Tsuchiya, T. Aohara, T. Konishi, S. Kaneko, K. Igarashi, M. Samejima, and Y. Tsumuraya An {alpha}-L-arabinofuranosidase/{beta}-D-xylosidase from immature seeds of radish (Raphanus sativus L.) J. Exp. Bot., July 1, 2006; 57(10): 2353 - 2362. [Abstract] [Full Text] [PDF]

				L. E. Taylor II, B. Henrissat, P. M. Coutinho, N. A. Ekborg, S. W. Hutcheson, and R. M. Weiner Complete Cellulase System in the Marine Bacterium Saccharophagus degradans Strain 2-40T J. Bacteriol., June 1, 2006; 188(11): 3849 - 3861. [Abstract] [Full Text] [PDF]

				M. Matulova, R. Nouaille, P. Capek, M. Pean, E. Forano, and A.-M. Delort Degradation of Wheat Straw by Fibrobacter succinogenes S85: a Liquid- and Solid-State Nuclear Magnetic Resonance Study Appl. Envir. Microbiol., March 1, 2005; 71(3): 1247 - 1253. [Abstract] [Full Text] [PDF]