• Microbiology and Biotechnology Letters
• /
• v.30 no.2
• /
• pp.123-128
• /
• 2002

A bacterium producing the extracellular xylanase was isolated from soil and has been identified as a Bacillus sp. strain. The isolate, named Bacillus sp. AMX-4, was shown to be similar to B. subtilis strain on the basis of its chemical compositions. The xylanase of culture supernatant was most active at 50℃ and pH 6.0. The additional carbon sources including monosaccharides, disaccharides, wheat bran, and rice straw increased the enzyme productivity. Especially, the maximum xylanase productivity was reached 29.2 units/ml in LB medium supplemented with 1.5％ (w/v) xylose, which was 16-folds more than that in LB medium. As the results of investigating the effects of xylose on cell growth and xylanase productivity of Bacillus sp. AMX-4, increase of xylanase production was owing to the induction of xylanase biosynthesis. It was also found that the enzyme production was in association with the growth of Bacillus sp. AMX-4.

• Journal of Microbiology and Biotechnology
• /
• v.19 no.12
• /
• pp.1514-1519
• /
• 2009

A gene encoding the xylanase of Bacillus subtilis AMX-4 isolated from soil was cloned into Escherichia coli and the gene product was purified from the cell-free extract of the recombinant strain. The gene, designated xylA, consisted of 639 nucleotides encoding a polypeptide of 213 residues. The deduced amino acid sequence was highly homologous to those of xylanases belonging to glycosyl hydrolase family 11. The molecular mass of the purified xylanase was 23 kDa as estimated by SDS-PAGE. The enzyme had a pH optimum of 6.0-7.0 and a temperature optimum of $50-55^{\circ}C$. Xylanase activity was significantly inhibited by 5 mM $Cu^{2+}$ and 5 mM $Mn^{2+}$, and noticeably enhanced by 5 mM $Fe^{2+}$. The enzyme was active on xylans including arabinoxylan, birchwood xylan, and oat spelt xylan, but it did not exhibit activity toward carboxymethylcellulose or p-nitrophenyl-$\beta$-xylopyranoside. The predominant products resulting from xylan and xylooligosaccharide hydrolysis were xylobiose and xylotriose. The enzyme could hydrolyze xylooligosaccharides larger than xylotriose.