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Applied and Environmental Microbiology, April 2000, p. 1734-1736, Vol. 66, No. 4
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
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Genetic and Biochemical Characterization of a
Highly Thermostable
-L-Arabinofuranosidase from
Thermobacillus xylanilyticus
-L-arabinofuranosidase from
Thermobacillus xylanilyticus D3, AbfD3, was isolated.
Characterization of the purified recombinant
-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.
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