T. Debeche et al., Genetic and biochemical characterization of a highly thermostable alpha-L-arabinofuranosidase from Thermobacillus xylanilyticus, APPL ENVIR, 66(4), 2000, pp. 1734-1736
The gene encoding an alpha-L-arabinofuranosidase from Thermobacillus xylani
lyticus D3, AbfD3, was isolated. Characterization of the purified recombina
nt alpha-L-arabinofuranosidase produced in Escherichia coli revealed that i
t is highly stable with respect to both temperature (up to 90 degrees C) an
d 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 g
lycosyl hydrolase classification system. However, substrate specificity ana
lysis revealed that AbfD3, unlike the majority of F51 members, displays hig
h activity in the presence of polysaccharides.