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Applied and Environmental Microbiology, April 2000, p. 1734-1736, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Genetic and Biochemical Characterization of a Highly Thermostable alpha -L-Arabinofuranosidase from Thermobacillus xylanilyticus

Takoua Debeche,1 Nicola Cummings,2 Ian Connerton,2 Philippe Debeire,1 and Michael J. O'Donohue1,*

INRA, Unité de Physicochimie et Biotechnologie des Polymères, 51687 Reims Cedex 02, France,1 and Division of Food Science, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough LE12 5RD, United Kingdom2

Received 17 November 1999/Accepted 1 February 2000

The gene encoding an alpha -L-arabinofuranosidase from Thermobacillus xylanilyticus D3, AbfD3, was isolated. Characterization of the purified recombinant alpha -L-arabinofuranosidase produced in Escherichia coli revealed that it is highly stable with respect to both temperature (up to 90°C) and pH (stable in the pH range 4 to 12). On the basis of amino acid sequence similarities, this 56,071-Da enzyme could be assigned to family 51 of the glycosyl hydrolase classification system. However, substrate specificity analysis revealed that AbfD3, unlike the majority of F51 members, displays high activity in the presence of polysaccharides.


* Corresponding author. Mailing address: INRA, Unité de Physicochimie et Biotechnologie des Polymères, B.P. 1039, Moulin de la Housse, 51687 Reims Cedex 02, France. Phone: 33 326 913 224. Fax: 33 326 913 887. E-mail: michael.odonohue{at}univ-reims.fr.


Applied and Environmental Microbiology, April 2000, p. 1734-1736, Vol. 66, No. 4
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.



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