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- W4220683485 endingPage "154947" @default.
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- W4220683485 abstract "The enormous waste of polyethylene terephthalate (PET) plastic has a great negative impact on the ecological environment because of its chemical inertia. To reduce the environmental threat posed by PET plastic, researchers gradually concentrate on the biodegradation of PET plastic. In this study, DuraPETase N233C/S282C/H214S/S245R (DuraPETase-4M) was designed through protein engineering, which can be used to improve the efficiency of PET plastic biodegradation. Based on the DuraPETase, a pair of disulfide bonds (N233C/S282C) was added to improve the thermal stability. Meanwhile, the key region flexibility adjustment (H214S) was proposed to enhance the biodegradation capacity of PET plastic. Additionally, protein surface electrostatic charge optimization (S245R) was adopted to improve the binding ability between enzyme and PET plastic. Based on molecular dynamic simulations (MDs), the rationality of the design was further verified. This study provides a strategy for obtaining high-efficiency PET degradation mutants and a new possibility of environmentally friendly plastic degradation. • The overall rigidity of DuraPETase can be further enhanced by introducing disulfide bonds • Under the premise of rigidity, increasing the flexibility of key region can ameliorate degradation capacity of DuraPETase • The degradation capacity of DuraPETase can be improved by electrostatic charge optimization • Rigidity-flexibility adjustment and charge optimization can cooperatively improve the degradation capacity of DuraPETase" @default.
- W4220683485 created "2022-04-03" @default.
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- W4220683485 date "2022-08-01" @default.
- W4220683485 modified "2023-10-10" @default.
- W4220683485 title "Enhancement of the degradation capacity of IsPETase for PET plastic degradation by protein engineering" @default.
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- W4220683485 doi "https://doi.org/10.1016/j.scitotenv.2022.154947" @default.
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