Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome
Journal Article
·
· Applied Microbiology and Biotechnology
- Nanjing Agricultural Univ. (China)
- Zhejiang Univ. of Technology, Hangzhou (China). Key Laboratory of Bioorganic Synthesis of Zhejiang Province
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Qingdao Vland Biotech Group Inc., Qingdao (China)
- 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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