초록
An alkali tolerant xylanase gene from Bacillus subtilis Lucky9 was cloned and extracellular expressed in E. coli BL21. Xylanase amino acid sequence showed 99% identity with xylanase sequence from Bacillus subtilis 168, and was belonged to glycoside hydrolase family 11. The recombinant E. coli (pET-pelB-xynLC9) containing pelB signal peptide produced extracellular xylanase of 436.5U/mL for 8h, which was used arabinose as extra carbon source and inducer for enhancing extracellular production. The extracellular xylanase was determined by SDS-PAGE with a relative molecular mass of 21kDa. The recombinant xylanase was optimally activity at pH 6.5 and 60<SUP>o</SUP>C. The xylanase exhibited 80% residual activity over a broad pH range of 6.0-9.0 for 24h. Thermostability studies showed that xylanase retained 60% residual activity after 2h at 60<SUP>o</SUP>C. The main end-products of hydrolysis of beech-wood xylan and corncob by the extracellular xylanase were xylobiose and xylotriose. This extracellular xylanase without purification is a suitable candidate for application in the industrial production of xylooligosaccharides from agro-industrial waste for use as prebiotics.