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Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation
Remarkably, a hydrolase from Ideonella sakaiensis 201-F6, termed PETase, exhibits great potential in polyethylene terephthalate (PET) waste management due to it can efficiently degrade PET under moderate conditions. However, its low yield and poor accessibility to bulky substrates hamper its further...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9559558/ https://www.ncbi.nlm.nih.gov/pubmed/36246227 http://dx.doi.org/10.3389/fmicb.2022.1005480 |
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author | Jia, Yunpu Samak, Nadia A. Hao, Xuemi Chen, Zheng Wen, Qifeng Xing, Jianmin |
author_facet | Jia, Yunpu Samak, Nadia A. Hao, Xuemi Chen, Zheng Wen, Qifeng Xing, Jianmin |
author_sort | Jia, Yunpu |
collection | PubMed |
description | Remarkably, a hydrolase from Ideonella sakaiensis 201-F6, termed PETase, exhibits great potential in polyethylene terephthalate (PET) waste management due to it can efficiently degrade PET under moderate conditions. However, its low yield and poor accessibility to bulky substrates hamper its further industrial application. Herein a multigene fusion strategy is introduced for constructing a hydrophobic cell surface display (HCSD) system in Escherichia coli as a robust, recyclable, and sustainable whole-cell catalyst. The truncated outer membrane hybrid protein FadL exposed the PETase and hydrophobic protein HFBII on the surface of E. coli with efficient PET accessibility and degradation performance. E. coli containing the HCSD system changed the surface tension of the bacterial solution, resulting in a smaller contact angle (83.9 ± 2° vs. 58.5 ± 1°) of the system on the PET surface, thus giving a better opportunity for PETase to interact with PET. Furthermore, pretreatment of PET with HCSD showed rougher surfaces with greater hydrophilicity (water contact angle of 68.4 ± 1° vs. 106.1 ± 2°) than the non-pretreated ones. Moreover, the HCSD system showed excellent sustainable degradation performance for PET bottles with a higher degradation rate than free PETase. The HCSD degradation system also had excellent stability, maintaining 73% of its initial activity after 7 days of incubation at 40°C and retaining 70% activity after seven cycles. This study indicates that the HCSD system could be used as a novel catalyst for efficiently accelerating PET biodegradation. |
format | Online Article Text |
id | pubmed-9559558 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-95595582022-10-14 Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation Jia, Yunpu Samak, Nadia A. Hao, Xuemi Chen, Zheng Wen, Qifeng Xing, Jianmin Front Microbiol Microbiology Remarkably, a hydrolase from Ideonella sakaiensis 201-F6, termed PETase, exhibits great potential in polyethylene terephthalate (PET) waste management due to it can efficiently degrade PET under moderate conditions. However, its low yield and poor accessibility to bulky substrates hamper its further industrial application. Herein a multigene fusion strategy is introduced for constructing a hydrophobic cell surface display (HCSD) system in Escherichia coli as a robust, recyclable, and sustainable whole-cell catalyst. The truncated outer membrane hybrid protein FadL exposed the PETase and hydrophobic protein HFBII on the surface of E. coli with efficient PET accessibility and degradation performance. E. coli containing the HCSD system changed the surface tension of the bacterial solution, resulting in a smaller contact angle (83.9 ± 2° vs. 58.5 ± 1°) of the system on the PET surface, thus giving a better opportunity for PETase to interact with PET. Furthermore, pretreatment of PET with HCSD showed rougher surfaces with greater hydrophilicity (water contact angle of 68.4 ± 1° vs. 106.1 ± 2°) than the non-pretreated ones. Moreover, the HCSD system showed excellent sustainable degradation performance for PET bottles with a higher degradation rate than free PETase. The HCSD degradation system also had excellent stability, maintaining 73% of its initial activity after 7 days of incubation at 40°C and retaining 70% activity after seven cycles. This study indicates that the HCSD system could be used as a novel catalyst for efficiently accelerating PET biodegradation. Frontiers Media S.A. 2022-09-29 /pmc/articles/PMC9559558/ /pubmed/36246227 http://dx.doi.org/10.3389/fmicb.2022.1005480 Text en Copyright © 2022 Jia, Samak, Hao, Chen, Wen and Xing. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Jia, Yunpu Samak, Nadia A. Hao, Xuemi Chen, Zheng Wen, Qifeng Xing, Jianmin Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation |
title | Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation |
title_full | Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation |
title_fullStr | Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation |
title_full_unstemmed | Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation |
title_short | Hydrophobic cell surface display system of PETase as a sustainable biocatalyst for PET degradation |
title_sort | hydrophobic cell surface display system of petase as a sustainable biocatalyst for pet degradation |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9559558/ https://www.ncbi.nlm.nih.gov/pubmed/36246227 http://dx.doi.org/10.3389/fmicb.2022.1005480 |
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