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The endoxylanase (642 bp; 213 amino acids) andb-xylosidase (1,602 bp; 533 amino acids) genes from Bacillussp. were amplified by PCR and separately inserted into thedownstream of the yeast ADH1 promoters, resulting in thepAEDX-1 (7.63 kb) and pAEX (8.47 kb) plasmids, respectively.When the yeast transformants, S. cerevisiae SEY2102harboring pAEDX-1 or pAEX, were grown on YPD medium,the total activities of the enzymes were approximately9.8 unit/ml for endoxylanase and 2.9 unit/ml for b-xylosidase.When the three kinds of xylan from oat spelts, birch wood,and corncob were hydrolyzed by treating with recombinantendoxylanase and b-xylosidase, it was found that xylose,xylobiose, and xylotriose were produced. To efficiently hydrolyzexylan, various reaction conditions such as amount of enzymes,substrate type, substrate concentration, temperature, and reactiontime were examined. The optimized conditions for thehydrolysis of xylan were as follows: amount of endoxylanase,10 units; amount of b-xylosidase, 10 units; temperature, 50oC;substrate type, oat spelts xylan; substrate concentration, 6%;reaction time, 1 h. Under the optimal condition, xylose wasmainly produced from oat spelts xylan by cooperative actionof endoxylanase and b-xylosidase.

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