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Updated: Jun 12, 2025

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

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[Advances in the structure and function of MHETase].

Meiyuan Yang1, Fangfang Fan1,2, Lingjuan He1

  • 1Key Laboratory of Chemical and Biological Processing Technology for Farm Products of Zhejiang Province, Zhejiang Provincial Collaborative Innovation Center of Agricultural Biological Resources Biochemical Manufacturing, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou 310023, Zhejiang, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology
|September 25, 2024
PubMed
Summary

Mono(2-hydroxyethyl) terephthalate hydrolase (MHETase) is key to fully degrading polyethylene terephthalate (PET) plastic waste. This review details MHETase structure, function, and engineering for improved PET hydrolysis when combined with PETase.

Keywords:
biodegradationmono(2-hydroxyethyl) terephthalate hydrolase (MHETase)plastic degradationpolyethylene terephthalate (PET)two-enzyme system

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