Enhanced degradation of post-consumer polyethylene terephthalate (PET) wastes by fusion cutinase: Effects of anchor and linker peptides

Enzymatic degradation of poly(ethylene terephthalate) (PET) into its corresponding monomers provides an attractive route for green plastic recycling and environmental remediation applications. However, the binding of PET hydrolases toward the PET surface is a rate-limiting step in PET degradation. Hence, we selected three anchor peptides and four linker peptides to fuse the previously engineered leaf-branch compost cutinase for facilitating enzyme binding and improving degradation of real post-consumer PET wastes of Coca Cola and C′eastbon PET bottles, with using the amorphous PET as a control. The systematical characterization of the seven cutinases revealed that the anchor peptide with moderate hydrophobicity plus chaperone activity and the flexible linker peptide with small hydrophobicity but long length were more suitable for each domain to serve its own role, affording the facilitated PET binding affinities and enhanced PET degradation performance. Thus, the optimal fusion cutinase possessed up to 3.3 times higher catalytic efficiency ( k cat / K m ) and 76 % increased long-term degradation performance than the parental cutinase, respectively. Further, complete degradation of C′eastbon PET wastes and 77 % degradation of Coca Cola PET wastes were achieved by the optimal cutinase of 33.3 nmol·g −1 PET in 96 h, proving its superiority against the real post-consumer PET wastes.