Synthetic genes encoding the 190 amino acid Trichoderma reesei xylanase II (TrX) and the closely related Trichoderma viride xylanases have been synthesized in a two-step procedure. Initially, a partial gene encoding amino acids 92-190 was constructed in fusion with the N-terminal half of the Bacillus circulans xylanase (BcX). The remaining BcX gene sequence was replaced during the assembly of the coding sequence for amino acids 1-91. Expression of the synthetic genes in Escherichia coli yielded recombinant xylanases with specific activity generally identical with the natural TrX. However, the recombinant TrX showed thermostability and temperature optimum lower than those of the natural TrX, thus indicating that the posttranslational modifications of the latter in its fungal host are essential to its greater stability. A mutation N19K further decreased the thermostability of the recombinant TrX.
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