Exploit and elucidate chaperone assisted PET hydrolase for upcycling plastics

被引:0
作者
Ting, Wan-Wen [1 ]
Yu, Jie-Yao [1 ]
Hsiang, Chuan-Chieh [1 ]
Tan, Shih-, I [2 ]
Chang, Chang-Chun [3 ]
Huang, Hsiang-Ling [4 ]
Yu, Chi-Hua [3 ,4 ]
Hu, Ruei-En [1 ]
Ma, Hsing-Ning [1 ]
Ng, I. -Son [1 ]
机构
[1] Natl Cheng Kung Univ, Dept Chem Engn, Tainan 70101, Taiwan
[2] Univ Illinois, Dept Chem & Biomol Engn, Champaign, IL USA
[3] Natl Cheng Kung Univ, Acad Innovat Semicond & Sustainable Mfg, Tainan 70101, Taiwan
[4] Natl Cheng Kung Univ, Dept Engn Sci, Tainan 70101, Taiwan
关键词
Ideonella sakaiensis; PETase; GroELS; Lipase secretion chaperone; Sequence similarity network (SSN); Molecular dynamic simulation; ESCHERICHIA-COLI; PROTEIN; MACHINE; SERVER;
D O I
10.1016/j.cej.2024.157777
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
Polyethylene terephthalate (PET) is the most abundant plastic waste in the environment. Currently, a new biocatalyst PETase, was discovered in 2016 from Ideonella sakaiensis bacteria, owned the high ability to digest PET through a mild and sustainable process. However, the high-level production of PETase in the model Escherichia coli remains a challenge and limits its application. Therefore, we employed the native molecular chaperones from Ideonella sakaiensis to improve the quality and quantity of an outstanding PETase variant, FASTPETase (FA) at the first time. We selected GroELS from E. coli (EcG) and I. sakaiensis (IsG) using three genetic designs while the co-expressing FA with IsG chaperone increased soluble FA and elevated its activity by 25%. On the other hand, through the genome mining of I. sakaiensis, we identified a lipase secretion chaperone (IsLsC) at the upstream of native PETase. When co-expressing IsLsC and FA, the degradation efficiency toward PET film was up to 51.7 % within one day at 50 degrees C. More LsC-like chaperones could be explored from the sequence similarity network (SSN) with corresponding function to IsLsC. Finally, molecular docking and dynamic simulation exploited a hydrogen bond formation between FA and IsLsC to stabilizing the overall structure. The discovery of a novel chaperone offers a promising strategy for attractive PETase engaging in PET waste valorization.
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页数:12
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