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© 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.

Abstract

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.

Details

Title
Degradation of PET Bottles by an Engineered Ideonella sakaiensis PETase
Author
Sevilla, Maria Eduarda 1 ; Garcia, Mario D 1   VIAFID ORCID Logo  ; Perez-Castillo, Yunierkis 2   VIAFID ORCID Logo  ; Armijos-Jaramillo, Vinicio 3   VIAFID ORCID Logo  ; Casado, Santiago 1   VIAFID ORCID Logo  ; Vizuete, Karla 4 ; Debut, Alexis 5   VIAFID ORCID Logo  ; Cerda-Mejía, Liliana 1   VIAFID ORCID Logo 

 Facultad de Ciencia e Ingeniería en Alimentos y Biotecnología, Universidad Técnica de Ambato, Ambato 180216, Ecuador 
 Área de Ciencias Aplicadas, Facultad de Ingeniería y Ciencias Aplicadas, Universidad de Las Américas, Quito 170125, Ecuador; Grupo de Bio-Quimioinformática, Universidad de Las Américas, Quito 170125, Ecuador 
 Grupo de Bio-Quimioinformática, Universidad de Las Américas, Quito 170125, Ecuador; Ingeniería en Biotecnología, Facultad de Ingeniería y Ciencias Aplicadas, Universidad de Las Américas, Quito 170125, Ecuador 
 Centro de Nanociencia y Nanotecnología, Universidad de Las Fuerzas Armadas ESPE, Sangolquí 171103, Ecuador 
 Centro de Nanociencia y Nanotecnología, Universidad de Las Fuerzas Armadas ESPE, Sangolquí 171103, Ecuador; Departamento de Ciencias de la Vida y Agricultura, Universidad de Las Fuerzas Armadas ESPE, Sangolquí 171103, Ecuador 
First page
1779
Publication year
2023
Publication date
2023
Publisher
MDPI AG
e-ISSN
20734360
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2799741932
Copyright
© 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.