Discovering and Designing a Chimeric Hyperthermophilic Chitinase for Crystalline Chitin Degradation
Journal Article
·
· ACS Sustainable Chemistry & Engineering
- Nanjing Agricultural University (China)
- Nanjing Forestry University (China)
- Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
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
Similar Records
The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly
Crystallization and preliminary X-ray diffraction analysis of a chitin-binding domain of hyperthermophilic chitinase from Pyrococcus furiosus
Enzymatically hydrolyzed fluorescence-based chemical probe enables in situ mapping of chitinase activity in the rhizosphere
Journal Article
·
Thu Feb 21 19:00:00 EST 2019
· Scientific Reports
·
OSTI ID:1544878
Crystallization and preliminary X-ray diffraction analysis of a chitin-binding domain of hyperthermophilic chitinase from Pyrococcus furiosus
Journal Article
·
Sun May 01 00:00:00 EDT 2005
· Acta Crystallographica. Section F
·
OSTI ID:22356008
Enzymatically hydrolyzed fluorescence-based chemical probe enables in situ mapping of chitinase activity in the rhizosphere
Journal Article
·
Sun Jul 09 20:00:00 EDT 2023
· Soil Biology and Biochemistry
·
OSTI ID:2000746