Cloning and Characterization of Xylanase A from the Strain <Emphasis Type="Italic">Bacillus</Emphasis> sp. BP-7: Comparison with Alkaline pI-Low Molecular Weight Xylanases of Family 11 |
| |
Authors: | Óscar Gallardo Pilar Diaz FI Javier Pastor |
| |
Institution: | (1) Departament de Microbiologia, Facultat de Biologia, Universitat de Barcelona, Avinguda Diagonal 645, 08028 Barcelona, Spain |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|