Abstract
The xynA gene encoding a xylanase from the recently isolated Bacillus sp. strain BP-7 has been cloned and expressed in Escherichia coli. Recombinant xylanase A showed high activity on xylans from hardwoods and cereals, and exhibited maximum activity at pH 6 and 60°C. The enzyme remained stable after incubation at 50°C and pH 7 for 3 h, and it was strongly inhibited by Mn2+, Fe3+, Pb2+, and Hg2+. Analysis of xylanase A in zymograms showed an apparent molecular size of 24 kDa and a pI of above 9. The amino acid sequence of xylanase A, as deduced from xynA gene, shows homology to alkaline pI-low molecular weight xylanases of family 11 such as XynA from Bacillus subtilis. Analysis of codon usage in xynA from Bacillus sp. BP-7 shows that the G+C content at the first and second codon positions is notably different from the mean values found for glycosyl hydrolase genes from Bacillus subtilis.
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Gallardo, ., Diaz, . & Pastor, . Cloning and Characterization of Xylanase A from the Strain Bacillus sp. BP-7: Comparison with Alkaline pI-Low Molecular Weight Xylanases of Family 11. Curr Microbiol 48, 276–279 (2004). https://doi.org/10.1007/s00284-003-4196-0
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DOI: https://doi.org/10.1007/s00284-003-4196-0