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Cited by 580

The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.

Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy

Cui, Yinglu, Chen, Yanchun, Liu, Xinyue, Dong, Saijun, Tian, Yu’e, Qiao, Yuxin, Mitra, Ruchira, Han, Jing, Li, Chunli, Han, Xu, Liu, Weidong, Chen, Quan, Wei, Wangqing, Wang, Xin, Du, Wenbin, Tang, Shuangyan, Xiang, Hua, Liu, Haiyan, Liang, Yong, Houk, Kendall N., Wu, Bian·2021·ACS Catalysis
DOI 10.1021/acscatal.0c05126
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Abstract

Nature has provided a fantastic array of enzymes that are responsible for essential biochemical functions but not usually suitable for technological applications. Not content with the natural repertoire, protein engineering holds promise to extend the applications of improved enzymes with tailored properties. However, engineering of robust proteins remains a difficult task since the positive mutation library may not cooperate to reach the target function in most cases owing to the ubiquity of epistatic effects. The main demand lies in identifying an efficient path of accumulated mutations. Herein, we devised a computational strategy (greedy accumulated strategy for protein engineering, GRAPE) to improve the robustness of a PETase from Ideonella sakaiensis . A systematic clustering analysis combined with greedy accumulation of beneficial mutations in a computationally derived library enabled the redesign of a variant, DuraPETase, which exhibits an apparent melting temperature that is drastically elevated by 31 °C and a strikingly enhanced degradation toward semicrystalline poly(ethylene terephthalate) (PET) films (30%) at mild temperatures (over 300-fold). Complete biodegradation of 2 g/L microplastics to water-soluble products under mild conditions is also achieved, opening up opportunities to steer the biological degradation of uncollectable PET waste and further conversion of the resulting monomers to high-value molecules. The crystal structure revealed the individual mutation match with the design model. Concurrently, synergistic effects are captured, while epistatic interactions are alleviated during the accumulation process. We anticipate that our design strategy will provide a broadly applicable strategy for global optimization of enzyme performance.

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Metadata

Authors
Cui, Y., Chen, Y., Liu, X., Dong, S., Tian, Y., Qiao, Y., Mitra, R., Han, J., Li, C., Han, X., Liu, W., Chen, Q., Wei, W., Wang, X., Du, W., Tang, S., Xiang, H., Liu, H., Liang, Y., Houk, K. N., & Wu, B.
Venue
ACS Catalysis
Publisher
American Chemical Society (ACS)
Published
2021-01-13
Volume
11
Issue
3
Pages
1340-1350
ISSN
2155-5435 (ISSN-L)
DOI
10.1021/acscatal.0c05126
OpenAlex
W3121331573
Cited by
580
References
53
FWCI
25.36
Type
journal article
Language
en
Open access
closed

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