Asparagine Residue at Position 71 is Responsible for Alkali-Tolerance of the Xylanase from Bacillus Pumilus A-30

  • Liu, Xiang-Mei (State key Laboratory of Microbial Technology, Shandong University) ;
  • Qi, Meng (State key Laboratory of Microbial Technology, Shandong University) ;
  • Lin, Jian-Aiang (State key Laboratory of Microbial Technology, Shandong University) ;
  • Wu, Zhi-Hong (State key Laboratory of Microbial Technology, Shandong University) ;
  • Qu, Yin-Bo (State key Laboratory of Microbial Technology, Shandong University)
  • Published : 2001.06.01

Abstract

The xynA gene encoding an alikali-tolerant endo-1,4-${\beta}$-xylanase (XYN) was cloned from the alkalophilic Bacillus pumilus A-30. The nucleotide sequence of a 974-bp DNA fragment containing the xynA was determined. An ORF of 684 nucleotides that encoded a protein of 228 amino aicds was detected. Asparagine-71 of XYN from B. Pumilus A-30 showed to be highly conservative in alkaline xylanases of family G/11, upon comparing the amino acid sequences of 17 family G/11 xylanases. Site-directed mutation of N71D of the xynA gene resulted in a decrease of 12.4% in the specific acitivity and a significant decline in the enzyme activity in the alkaline pH range.

Keywords

References

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