Discovering and Designing a Chimeric Hyperthermophilic Chitinase for Crystalline Chitin DegradationClick to copy article linkArticle link copied!
- Bo SunBo SunKey Laboratory of Plant Immunity, Joint International Research Laboratory of Soil Health, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing 210095, People’s Republic of ChinaMore by Bo Sun
- Xingchu ZhaoXingchu ZhaoCollege of Science, Nanjing Agricultural University, Nanjing 210095, People’s Republic of ChinaMore by Xingchu Zhao
- Birui XuBirui XuCollege of Science, Nanjing Agricultural University, Nanjing 210095, People’s Republic of ChinaMore by Birui Xu
- Erzheng SuErzheng SuCollege of Light Industry and Food Engineering, Nanjing Forestry University, Nanjing 210037, People’s Republic of ChinaMore by Erzheng Su
- Andrey KovalevskyAndrey KovalevskyNeutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, United StatesMore by Andrey Kovalevsky
- Qirong ShenQirong ShenKey Laboratory of Plant Immunity, Joint International Research Laboratory of Soil Health, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing 210095, People’s Republic of ChinaMore by Qirong Shen
- Dongyang LiuDongyang LiuKey Laboratory of Plant Immunity, Joint International Research Laboratory of Soil Health, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing 210095, People’s Republic of ChinaMore by Dongyang Liu
- Qun Wan*Qun Wan*Email: [email protected]Key Laboratory of Plant Immunity, Joint International Research Laboratory of Soil Health, College of Resources and Environmental Sciences, Nanjing Agricultural University, Nanjing 210095, People’s Republic of ChinaMore by Qun Wan
Abstract

Chitin is one of the most abundant renewable biopolymers on earth. However, it is highly crystalline and recalcitrant to degrade. Here, we report a hyperthermophilic chitinase (ActChi) to directly hydrolyze crystalline chitin at its optimal temperature of 80 °C. It contains a malectin domain, a fibronectin type-III (Fn3) domain, and a catalytic domain (CDchi). Both Fn3 and malectin have the function of chitin binding domain (ChBD) to increase the activity. Fn3 also significantly increases thermostability, but malectin decreases it. To enhance both activity and thermostability, we introduced a heterogeneous and hyperthermophilic ChBD at the N-terminus of CDchi to obtain ChBD-CDchi. The activity of this hybrid enzyme is 201 U/μmol for crystalline chitin, which has increased 400% compared with that of ActChi. In addition, ChBD-CDchi can continuously degrade crystalline chitin for more than 4 days at 70 °C to increase the overall hydrolysis rate. The strategy is a good example of green sustainable degradation for crystalline biopolymer in nature.
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