Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis

被引:172
|
作者
Liu, Bing [1 ,2 ]
He, Lihui [2 ,3 ]
Wang, Liping [1 ,2 ]
Li, Tao [2 ,3 ]
Li, Changcheng [2 ,3 ]
Liu, Huayi [1 ,2 ]
Luo, Yunzi [1 ,2 ]
Bao, Rui [2 ,3 ]
机构
[1] Sichuan Univ, West China Hosp, Dept Gastroenterol, Chengdu 610041, Sichuan, Peoples R China
[2] Collaborat Innovat Ctr Biotherapy, Chengdu 610041, Sichuan, Peoples R China
[3] Sichuan Univ, West China Hosp, Ctr Infect Dis, Chengdu 610041, Sichuan, Peoples R China
基金
中国国家自然科学基金;
关键词
mutagenesis; polymers; protein engineering; sustainable chemistry; waste disposal; CUTINASE; CARBOXYLESTERASE; HYDROLYSIS; ESTERASES; PLASTICS; ENZYMES; LIPASE;
D O I
10.1002/cbic.201800097
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis.
引用
收藏
页码:1471 / 1475
页数:5
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