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Substrate Inhibition of the Highly Efficient PET Hydrolase

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Abstract

Polyethylene terephthalate (PET) is one of the most abundant polyester materials used in daily life and it is also one of the culprits of environmental pollution. ICCG (F243I/D238C/S283C/Y127G) is a quadruple mutant of leaf-branch compost cutinase (LCC) displaying outstanding performance in hydrolyzing PET and holding a great potential in further applications. Substrate concentration is one of the important factors affecting the catalytic degradation efficiency. The conventional fast equilibrium theory holds that the degradation rate reaches the maximum and tends to be stable with the increase of substrate concentration, however, in practice, too much substrate will inhibit the catalytic reaction. In this study, the substrate inhibitory effect of PET plastic particles with different particle sizes on ICCG was evaluated. Combined with kinetic constant analysis, the optimal PET particle size was determined to be 300 μm. Meanwhile, several mutants (Y95K, M166S and H218S) of ICCG were obtained by site-directed mutagenesis. The effect of substrate concentration on mutant was studied under the condition of optimal reaction particle size. This study provides a strategy for obtaining high-efficiency PET degradation mutants and a new possibility of environmentally friendly plastic degradation.

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Funding

The study was financially supported by the National Natural Science Foundation of China (Grant no. 22273032 to J.Y.) and the Shandong Provincial Natural Science Foundation of China (Grants ZR2022MC046 to J.Y. and Grants ZR2022MB138 to X.W.).

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  1. Qiang Li and Nannan Jing contributed equally to this work.

Authors and Affiliations

  1. School of Biological Science and Technology, University of Jinan, 250022, Jinan, China

    Qiang Li, Nannan Jing, Xueqi Leng, Wenhong Liu, Qingqing Li, Kang Yang, Xia Wang & Jianzhuang Yao

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  1. Qiang Li
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  2. Nannan Jing
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  3. Xueqi Leng
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Correspondence to Xia Wang or Jianzhuang Yao.

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Li, Q., Jing, N., Leng, X. et al. Substrate Inhibition of the Highly Efficient PET Hydrolase. Appl Biochem Microbiol 60, 280–286 (2024). https://doi.org/10.1134/S0003683824020091

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