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Microbial Polyethylene Terephthalate Hydrolases: Current and Future Perspectives
Summary
This review surveys microbial enzymes capable of breaking down PET plastic, focusing on the structure and function of key hydrolases like PETase and cutinases. Researchers found that while several enzymes show promising PET-degrading activity, most work slowly and under limited temperature conditions, with engineered variants showing improved performance. The study highlights both the potential and the current limitations of using biological approaches for plastic waste management.
Plastic has rapidly transformed our world, with many aspects of human life now relying on a variety of plastic materials. Biological plastic degradation, which employs microorganisms and their degradative enzymes, has emerged as one way to address the unforeseen consequences of the waste streams that have resulted from mass plastic production. The focus of this review is microbial hydrolase enzymes which have been found to act on polyethylene terephthalate (PET) plastic. The best characterized examples are discussed together with the use of genomic and protein engineering technologies to obtain PET hydrolase enzymes for different applications. In addition, the obstacles which are currently limiting the development of efficient PET bioprocessing are presented. By continuing to study the possible mechanisms and the structural elements of key enzymes involved in microbial PET hydrolysis, and by assessing the ability of PET hydrolase enzymes to work under practical conditions, this research will help inform large-scale waste management operations. Finally, the contribution of microbial PET hydrolases in creating a potential circular PET economy will be explored. This review combines the current knowledge on enzymatic PET processing with proposed strategies for optimization and use, to help clarify the next steps in addressing pollution by PET and other plastics.
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