Extensive use of polyethylene terephthalate (PET) has brought about global environmental problems. A recently reported PET hydrolase (PETase) discovered from

Ideonella sakaiensis

showed high potential for degrading PET at moderate temperatures

but its activity and stability need further improvement for practical applications. Herein

we proposed to use α-synuclein (αS) as a fusion chaperone and created six PETase-αS fusion enzymes with linkers of different types and lengths. All the fusion enzymes exhibited improved enzymatic performance

presenting 1.5 to 2.6-fold higher activity towards bis-2(hydroxyethyl) terephthalate than PETase

as well as significantly increased stabilities. Fluorescence spectroscopy indicated that the chaperone fusion tightened the overall conformation and resulted in the opening of the substrate binding pocket

which led to the improved thermal stability and catalytic activity of the fusion enzymes. Remarkably

one of the fusion proteins

PETase-[(GS)(EK)

]

10

-αS

showed 3.2 to 5.1 times higher PET degradation capability than PETase. The significantly boosted PET degradation performance was not only attributed to the enhanced enzymatic activity and stability

but also possibly d

ue to the binding affinity of the fused αS domain for PET. These findings demonstrated that αS was an effective fusion chaperone for significantly enhancing the enzymatic performance of PETase.