角质酶
聚对苯二甲酸乙二醇酯
酶
降级(电信)
材料科学
聚酯纤维
聚合物
化学
生物化学
复合材料
计算机科学
电信
作者
Maria Eduarda Sevilla,M.D. Garcia,Yunierkis Pérez‐Castillo,Vinicio Armijos‐Jaramillo,Santiago Casado,Karla Vizuete,Alexis Debut,Liliana Cerda-Mejía
出处
期刊:Polymers
[MDPI AG]
日期:2023-04-03
卷期号:15 (7): 1779-1779
被引量:8
标识
DOI:10.3390/polym15071779
摘要
Extensive plastic production has become a serious environmental and health problem due to the lack of efficient treatment of plastic waste. Polyethylene terephthalate (PET) is one of the most used polymers and is accumulating in landfills or elsewhere in nature at alarming rates. In recent years, enzymatic degradation of PET by Ideonella sakaiensis PETase (IsPETase), a cutinase-like enzyme, has emerged as a promising strategy to completely depolymerize this polymer into its building blocks. Here, inspired by the architecture of cutinases and lipases homologous to IsPETase and using 3D structure information of the enzyme, we rationally designed three mutations in IsPETase active site for enhancing its PET-degrading activity. In particular, the S238Y mutant, located nearby the catalytic triad, showed a degradation activity increased by 3.3-fold in comparison to the wild-type enzyme. Importantly, this structural modification favoured the function of the enzyme in breaking down highly crystallized (~31%) PET, which is found in commercial soft drink bottles. In addition, microscopical analysis of enzyme-treated PET samples showed that IsPETase acts better when the smooth surface of highly crystalline PET is altered by mechanical stress. These results represent important progress in the accomplishment of a sustainable and complete degradation of PET pollution.
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