The gene xynB from Aspergillus sulphureus encoding the endo-beta-1,4-xylanase was de novo synthesized by splicing overlap extension polymerase chain reaction according to Pichia pastoris protein's codon bias. The synthetic DNA and wild-type DNA were placed under the control of a glyceraldehyde-3-phosphate dehydrogenase gene promoter (GAP) in the constitutive expression vector plasmid pGAPz alpha A and electrotransformed into the P. pastoris X-33 strain, respectively. The transformants screened by Zeocin were able to constitutively secrete the xylanase in YPD liquid medium. The maximum yield of the recombinant xylanase produced by the synthetic DNA was 105 U ml(-1), which was about 5-fold higher than that by wild-type DNA under the flask culture at 28 A degrees C for 3 days. The enzyme showed optimal activity at 50 A degrees C and pH 5.0. The residual activity remained above 90% after the recombinant xylanase was pretreated in Na2HPO4-citric acid buffer (pH 2.4) for 2 h. The xylanase activity was significantly improved by Zn2+. These biochemical characteristics suggest that the recombinant xylanase has a prospective application in feed industry as an additive.