4.4 Review

IsPETase Is a Novel Biocatalyst for Poly(ethylene terephthalate) (PET) Hydrolysis

Journal

CHEMBIOCHEM
Volume 22, Issue 10, Pages 1706-1716

Publisher

WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202000767

Keywords

IsPETase; PET-hydrolyzing enzymes; poly(ethylene terephthalate) (PET); protein engineering

Funding

  1. National Key Research and Development Program of China [2016YFA0502700, 2018YFA0903300]
  2. National Natural Science Foundation of China [81670008, 81501787, 32071426]
  3. Natural Science Foundation of Tianjin City [19JCYBJC24200]

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PET is widely used but also a major source of plastic pollution. Enzymatic processes have been explored for PET waste disposal, with IsPETase showing potential for industrial applications. Continuing research on cutinase-like enzymes could lead to suitable biocatalysts for industrial use.
Poly(ethylene terephthalate) (PET) is one of the most widely used synthetic polyesters, but also a major cause of plastic pollution. Because the chemical degradation of PET would be uneconomical and rather burdensome, considerable efforts have been devoted to exploring enzymatic processes for the disposal of PET waste. Many PET-hydrolyzing enzymes have been reported in recent decades, some of which demonstrate excellent potential for industrial applications. This review sets out to summarize the state of investigation into IsPETase, a cutinase-like enzyme from Ideonella sakaiensis possessing ability to degrade crystalline PET, and to gain further insight into the structure-function relationship of IsPETase. Benefiting from the continuing identification of novel cutinase-like proteins and growing availability of the engineered IsPETase, we may anticipate future developments in this type of enzyme would generate suitable biocatalyst for industrial use.

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