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Discovering and Designing a Chimeric Hyperthermophilic Chitinase for Crystalline Chitin Degradation

Journal Article · · ACS Sustainable Chemistry & Engineering
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, here 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.
Research Organization:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Organization:
Central Universities; National Natural Science Foundation of China; USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
AC05-00OR22725
OSTI ID:
1968674
Journal Information:
ACS Sustainable Chemistry & Engineering, Journal Name: ACS Sustainable Chemistry & Engineering Journal Issue: 12 Vol. 11; ISSN 2168-0485
Publisher:
American Chemical Society (ACS)Copyright Statement
Country of Publication:
United States
Language:
English

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