Engineering dual-functional and thermophilic BMHETase for efficient degradation of polyethylene terephthalate

文献类型： 外文期刊

第一作者： Miao, Ruiju

作者： Miao, Ruiju;Xu, Guoshun;Tu, Tao;Luo, Huiying;Yao, Bin;Tian, Jian;Ding, Yekun;Ding, Zundan;Wu, Ningfeng;Guan, Feifei;Tian, Jian;Woodard, Jaie

作者机构：

关键词： PET degradation; Enzyme mining; Thermostability; Molecular modification; Bifunctional enzyme

期刊名称：BIORESOURCE TECHNOLOGY （ 影响因子：9.0； 五年影响因子：9.5 ）

ISSN： 0960-8524

年卷期： 2024 年 414 卷

页码：

收录情况： SCI

摘要： Polyethylene terephthalate (PET) biodegradation is hindered by the intermediates bis (2-hydroxyethyl) terephthalate (BHET) and mono (2-hydroxyethyl) terephthalate (MHET). BMHETase, a thermophilic hydrolase identified from the UniParc database, exhibits degradation activity towards both BHET and MHET. BMHETase showed higher activity on BHET than LCCICCG and FASTPETase at temperatures ranging from 50 to 70 degrees C. To enhance its activity in degrading MHET, BMHETase was engineered to mimic Ideonella sakaiensis MHETase. The resulting 6-point mutant's activities on MHET and BHET were 8 and 2 times those of the WT, with both optimal temperatures increased by 5 degrees C. This enhancement may be attributed to the BMHETase6M's intensified binding ability with MHET and enlarged binding pocket. When combined with LCCICCG, BMHETase6M achieved complete degradation of MHET in PET films to terephthalic acid, indicating broad application potential. These findings suggest that BMHETase6M holds promise as a candidate for enhancing PET biodegradation efficiency and plastic waste management.

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