Rational redesign of thermophilic PET hydrolase LCCICCG to enhance hydrolysis of high crystallinity polyethylene terephthalates

文献类型： 外文期刊

第一作者： Ding, Zundan

作者： Ding, Zundan;Miao, Ruiju;Wu, Ningfeng;Zhang, Wei;Guan, Feifei;Tian, Jian;Miao, Ruiju;Xu, Guoshun;Yao, Bin;Huang, Huoqing;Tian, Jian

作者机构： Chinese Acad Agr Sci, Biotechnol Res Inst, Beijing 100081, Peoples R China;Hebei Univ Econ & Business, Coll Biosci & Engn, Shijiazhuang 050061, Hebei, Peoples R China;Chinese Acad Agr Sci, Inst Anim Sci, Beijing 100193, Peoples R China

关键词： PET; High crystallinity; Thermophilic mutant; LCCICCG

期刊名称：JOURNAL OF HAZARDOUS MATERIALS （ 2022影响因子：13.6； 五年影响因子：12.7 ）

ISSN： 0304-3894

年卷期： 2023 年 453 卷

页码：

收录情况： SCI

摘要： Polyethylene terephthalate (PET)-degrading enzymes represent a promising solution to the plastic pollution. However, PET-degrading enzymes, even thermophilic PETase, can effectively degrade low-crystallinity (similar to 8%) PETs, but exhibit weak depolymerization of more common, high-crystallinity (30-50%) PETs. Here, based on the thermophilic PETase, LCCICCG, we proposed two strategies for rational redesign of LCCICCG using the machine learning tool, Preoptem, combined with evolutionary analysis. Six single-point mutants (S32L, D18T, S98R, T157P, E173Q, N213P) were obtained that exhibit higher catalytic efficiency towards PET powder than wildtype LCCICCG at 75 degrees C. Additionally, the optimal temperature for degrading 39.07% crystalline PET increased from 65 degrees C in the wild-type LCCICCG to between 75 and 80 degrees C in the LCCICCG_I6M mutant that carries all six single-point mutations. Especially, the LCCICCG_I6M mutant has a significantly higher degradation effect on some commonly used bottle-grade plastic powders at 75-80 degrees C than that of wild type. The enzymatic digestion of ground 31.30% crystalline PET water bottles by LCCICCG_I6M yielded 31.91 +/- 0.99 mM soluble products in 24 h, which was 3.64 times that of LCCICCG (8.77 +/- 1.52 mM). Overall, this study provides a feasible route for engineering thermostable enzymes that can degrade high-crystallinity PET plastic.

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