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Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome

Journal Article · · Applied Microbiology and Biotechnology
 [1];  [2];  [3];  [4];  [1];  [5]
  1. Nanjing Agricultural Univ. (China)
  2. Zhejiang Univ. of Technology, Hangzhou (China). Key Laboratory of Bioorganic Synthesis of Zhejiang Province
  3. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  4. Qingdao Vland Biotech Group Inc., Qingdao (China)
  5. Nanjing Agricultural Univ. (China); Nanjing Agricultural Univ. (China). Key Lab. of Plant Immunity
Xylanase is efficient for xylan degradation and widely applied in industries. We found a GH11 family xylanase (Xyn11A) with high thermostability and catalytic activity from compost metatranscriptome. This xylanase has the optimal reaction temperature at 80 °C with the activity of 2907.3 U/mg. The X-ray crystallographic structure shows a typical “right hand” architecture, which is the characteristics of the GH11 family enzymes. Comparing it with the mesophilic XYN II, a well-studied GH11 xylanase from Trichoderma reesei, Xyn11A is more compact with more H-bonds. Our mutagenic results show that the electrostatic interactions in the thumb and palm region of Xyn11A could result in its high thermostability and activity. Introducing a disulfide bond at the N-terminus further increased its optimal reaction temperature to 90 °C with augmented activity.
Research Organization:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
Fundamental Research Funds for the Central Universities; National Natural Science Foundation of China (NSFC); USDOE
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
1830103
Journal Information:
Applied Microbiology and Biotechnology, Journal Name: Applied Microbiology and Biotechnology Journal Issue: 20 Vol. 105; ISSN 0175-7598
Publisher:
SpringerCopyright Statement
Country of Publication:
United States
Language:
English

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