Discovering and Designing a Chimeric Hyperthermophilic Chitinase for Crystalline Chitin Degradation

Bo Sun; Xingchu Zhao; Birui Xu; Erzheng Su; Andrey Kovalevsky; Qirong Shen; Dongyang Liu; Qun Wan

doi:10.1021/acssuschemeng.2c07050

Discovering and Designing a Chimeric Hyperthermophilic Chitinase for Crystalline Chitin Degradation

Bo Sun, Xingchu Zhao, Birui Xu, Erzheng Su, Andrey Kovalevsky, Qirong Shen, Dongyang Liu, Qun Wan

Single Crystal Diffraction

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8 Scopus citations

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 (CD_chi). 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 CD_chi to obtain ChBD-CD_chi. 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-CD_chi 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.

Original language	English
Pages (from-to)	4690-4698
Number of pages	9
Journal	ACS Sustainable Chemistry and Engineering
Volume	11
Issue number	12
DOIs	https://doi.org/10.1021/acssuschemeng.2c07050
State	Published - Mar 27 2023

Funding

Research at ORNL’s Spallation Neutron Source was sponsored by the Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy. This work was supported by the National Natural Science Foundation of China (no. 32071264 and no. 32271317) and the Fundamental Research Funds for the Central Universities (no. KYXK202009).

Funders	Funder number
Scientific User Facilities Division
U.S. Department of Energy
Basic Energy Sciences
National Natural Science Foundation of China	32071264, 32271317
Fundamental Research Funds for the Central Universities	KYXK202009

Keywords

chitin binding domain (ChBD)
chitinase
fibronectin type-III (Fn3)
hyperthermophilic
malectin

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10.1021/acssuschemeng.2c07050

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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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AU - Liu, Dongyang

AU - Wan, Qun

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N2 - 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.

AB - 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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Discovering and Designing a Chimeric Hyperthermophilic Chitinase for Crystalline Chitin Degradation

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