Novel Feruloyl Esterase for the Degradation of Polyethylene Terephthalate (PET) Screened from the Gut Microbiome of Plastic-Degrading Mealworms (Tenebrio Molitor Larvae)

被引:7
作者
Mamtimin, Tursunay [1 ,2 ]
Ouyang, Xingyu [3 ]
Wu, Wei-Min [4 ]
Zhou, Tuoyu [1 ]
Hou, Xiaoxiao [1 ]
Khan, Aman [1 ,5 ]
Liu, Pu [1 ]
Zhao, Yi-Lei [3 ]
Tang, Hongzhi [3 ]
Criddle, Craig S. [4 ]
Han, Huawen [2 ]
Li, Xiangkai [1 ]
机构
[1] Lanzhou Univ, Minist Educ, Key Lab Cell Act & Stress Adaptat, Sch Life Sci, Lanzhou 730000, Peoples R China
[2] Lanzhou Univ, Coll Pastoral Agr Sci & Technol, Ctr Grassland Microbiome, State Key Lab Herbage Improvement & Grassland Agro, Lanzhou 730000, Peoples R China
[3] Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, State Key Lab Microbial Metab, Joint Int Res Lab Metab & Dev Sci, Shanghai 200000, Peoples R China
[4] Stanford Univ, William & Cloy Codiga Resource Recovery Ctr, Dept Civil & Environm Engn, Stanford, CA 94305 USA
[5] Northeast Forestry Univ, Key Lab Saline Alkali Vegetat Ecol Restorat, Coll Life Sci, Minist Educ, Harbin 150040, Peoples R China
基金
中国国家自然科学基金;
关键词
polyethylene terephthalate(PET); biodegradation; feruloyl esterase; MD simulation; Tenebriomolitor larvae; BIOMASS;
D O I
10.1021/acs.est.4c01495
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
Mealworms (Tenebrio molitor) larvae can degrade both plastics and lignocellulose through synergistic biological activities of their gut microbiota because they share similarities in chemical and physical properties. Here, a total of 428 genes encoding lignocellulose-degrading enzymes were screened from the gut microbiome of T. molitor larvae to identify poly(ethylene terephthalate) (PET)-degrading activities. Five genes were successfully expressed in E. coli, among which a feruloyl esterase-like enzyme named TmFae-PETase demonstrated the highest PET degradation activity, converting PET into MHET (0.7 mg(MHETeq) <middle dot>h(-1)<middle dot>mg(enzyme)(-1)) and TPA (0.2 mg(TPAeq) <middle dot>h(-1)<middle dot>mg(enzyme)(-1)) at 50 degrees C. TmFae-PETase showed a preference for the hydrolysis of ferulic acid methyl ester (MFA) in the presence of both PET and MFA. Site-directed mutagenesis and molecular dynamics simulations of TmFae-PETase revealed similar catalytic mechanisms for both PET and MFA. TmFae-PETase effectively depolymerized commercial PET, making it a promising candidate for application. Additionally, the known PET hydrolases IsPETase, FsC, and LCC also hydrolyzed MFA, indicating a potential origin of PET hydrolytic activity from its lignocellulosic-degrading abilities. This study provides an innovative strategy for screening PET-degrading enzymes identified from lignocellulose degradation-related enzymes within the gut microbiome of plastic-degrading mealworms. This discovery expands the existing pool of plastic-degrading enzymes available for resource recovery and bioremediation applications.
引用
收藏
页码:17717 / 17731
页数:15
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