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Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin

The process of recycling poly(ethylene terephthalate) (PET) remains a major challenge due to the enzymatic degradation of high-crystallinity PET (hcPET). Recently, a bacterial PET-degrading enzyme, PETase, was found to have the ability to degrade the hcPET, but with low enzymatic activity. Here we p...

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Autores principales: Chen, Zhuozhi, Duan, Rongdi, Xiao, Yunjie, Wei, Yi, Zhang, Hanxiao, Sun, Xinzhao, Wang, Shen, Cheng, Yingying, Wang, Xue, Tong, Shanwei, Yao, Yunxiao, Zhu, Cheng, Yang, Haitao, Wang, Yanyan, Wang, Zefang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9681837/
https://www.ncbi.nlm.nih.gov/pubmed/36414665
http://dx.doi.org/10.1038/s41467-022-34908-z
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author Chen, Zhuozhi
Duan, Rongdi
Xiao, Yunjie
Wei, Yi
Zhang, Hanxiao
Sun, Xinzhao
Wang, Shen
Cheng, Yingying
Wang, Xue
Tong, Shanwei
Yao, Yunxiao
Zhu, Cheng
Yang, Haitao
Wang, Yanyan
Wang, Zefang
author_facet Chen, Zhuozhi
Duan, Rongdi
Xiao, Yunjie
Wei, Yi
Zhang, Hanxiao
Sun, Xinzhao
Wang, Shen
Cheng, Yingying
Wang, Xue
Tong, Shanwei
Yao, Yunxiao
Zhu, Cheng
Yang, Haitao
Wang, Yanyan
Wang, Zefang
author_sort Chen, Zhuozhi
collection PubMed
description The process of recycling poly(ethylene terephthalate) (PET) remains a major challenge due to the enzymatic degradation of high-crystallinity PET (hcPET). Recently, a bacterial PET-degrading enzyme, PETase, was found to have the ability to degrade the hcPET, but with low enzymatic activity. Here we present an engineered whole-cell biocatalyst to simulate both the adsorption and degradation steps in the enzymatic degradation process of PETase to achieve the efficient degradation of hcPET. Our data shows that the adhesive unit hydrophobin and degradation unit PETase are functionally displayed on the surface of yeast cells. The turnover rate of the whole-cell biocatalyst toward hcPET (crystallinity of 45%) dramatically increases approximately 328.8-fold compared with that of purified PETase at 30 °C. In addition, molecular dynamics simulations explain how the enhanced adhesion can promote the enzymatic degradation of PET. This study demonstrates engineering the whole-cell catalyst is an efficient strategy for biodegradation of PET.
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spelling pubmed-96818372022-11-24 Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin Chen, Zhuozhi Duan, Rongdi Xiao, Yunjie Wei, Yi Zhang, Hanxiao Sun, Xinzhao Wang, Shen Cheng, Yingying Wang, Xue Tong, Shanwei Yao, Yunxiao Zhu, Cheng Yang, Haitao Wang, Yanyan Wang, Zefang Nat Commun Article The process of recycling poly(ethylene terephthalate) (PET) remains a major challenge due to the enzymatic degradation of high-crystallinity PET (hcPET). Recently, a bacterial PET-degrading enzyme, PETase, was found to have the ability to degrade the hcPET, but with low enzymatic activity. Here we present an engineered whole-cell biocatalyst to simulate both the adsorption and degradation steps in the enzymatic degradation process of PETase to achieve the efficient degradation of hcPET. Our data shows that the adhesive unit hydrophobin and degradation unit PETase are functionally displayed on the surface of yeast cells. The turnover rate of the whole-cell biocatalyst toward hcPET (crystallinity of 45%) dramatically increases approximately 328.8-fold compared with that of purified PETase at 30 °C. In addition, molecular dynamics simulations explain how the enhanced adhesion can promote the enzymatic degradation of PET. This study demonstrates engineering the whole-cell catalyst is an efficient strategy for biodegradation of PET. Nature Publishing Group UK 2022-11-21 /pmc/articles/PMC9681837/ /pubmed/36414665 http://dx.doi.org/10.1038/s41467-022-34908-z Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Chen, Zhuozhi
Duan, Rongdi
Xiao, Yunjie
Wei, Yi
Zhang, Hanxiao
Sun, Xinzhao
Wang, Shen
Cheng, Yingying
Wang, Xue
Tong, Shanwei
Yao, Yunxiao
Zhu, Cheng
Yang, Haitao
Wang, Yanyan
Wang, Zefang
Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
title Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
title_full Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
title_fullStr Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
title_full_unstemmed Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
title_short Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin
title_sort biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial petase and hydrophobin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9681837/
https://www.ncbi.nlm.nih.gov/pubmed/36414665
http://dx.doi.org/10.1038/s41467-022-34908-z
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