Xue_2024_Bioresour.Technol_408_131177

Reference

Title : Bacterial surface display of PETase mutants and MHETase for an efficient dual-enzyme cascade catalysis - Xue_2024_Bioresour.Technol_408_131177
Author(s) : Xue K , Bai Z , Fordour E , Guo S , Zhou Y , Yang Y , Liu X , Li Y , Liu CL
Ref : Bioresour Technol , 408 :131177 , 2024
Abstract :

Biological degradation of PET plastic holds great potential for plastic recycling. However, the high costs associated with preparing free enzymes for degrading PET make it unfeasible for industrial applications. Hence, we developed various cell catalysts by surface-displaying PETase mutants and MHETase using autotransporters in E. coli and P. putida. The efficiency of surface display was enhanced through modifying the host, co-expressing molecular chaperones, and evoluting the autotransporter. In strain EC9F, PET degradation rate was boosted to 3.85 mM/d, 51-fold and 23-fold increase compared to free enzyme and initial strain ED1, respectively. The reusability of cell catalyst EC9F was demonstrated with over 38 % and 30 % of its initial activity retained after 22 cycles of BHET degradation and 3 cycles of PET degradation. The highest reported PET degradation rate of 4.95 mM/d was achieved by the dual-enzyme cascade catalytic system EC9F+EM2+R, a mixture of cell catalyst EC9F and EM2 with surfactant rhamnolipid.

PubMedSearch : Xue_2024_Bioresour.Technol_408_131177
PubMedID: 39097240

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Citations formats

Xue K, Bai Z, Fordour E, Guo S, Zhou Y, Yang Y, Liu X, Li Y, Liu CL (2024)
Bacterial surface display of PETase mutants and MHETase for an efficient dual-enzyme cascade catalysis
Bioresour Technol 408 :131177

Xue K, Bai Z, Fordour E, Guo S, Zhou Y, Yang Y, Liu X, Li Y, Liu CL (2024)
Bioresour Technol 408 :131177