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| Autori principali: | , , , , , , , , , , , , , , , |
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| Natura: | Artículo científico |
| Lingua: | en |
| Pubblicazione: |
International journal of biological macromolecules
2026
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| Soggetti: | |
| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/41548779/ |
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| _version_ | 1868266097709416449 |
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| author | Zhang, Lurong Zhou, Xiaoyu Yuan, Yuxuan Li, Haoqing Li, Jiachen Zhou, Yibing Du, Siyu Wang, Ziyu Han, Yiting Fan, Xinze Han, Daiyi Wang, Lijie Zhu, Cheng Ye, Sheng Wang, Yaxin Xu, Binghong |
| author_facet | Zhang, Lurong Zhou, Xiaoyu Yuan, Yuxuan Li, Haoqing Li, Jiachen Zhou, Yibing Du, Siyu Wang, Ziyu Han, Yiting Fan, Xinze Han, Daiyi Wang, Lijie Zhu, Cheng Ye, Sheng Wang, Yaxin Xu, Binghong Zhang, Lurong Zhou, Xiaoyu Yuan, Yuxuan Li, Haoqing Li, Jiachen Zhou, Yibing Du, Siyu Wang, Ziyu Han, Yiting Fan, Xinze Han, Daiyi Wang, Lijie Zhu, Cheng Ye, Sheng Wang, Yaxin Xu, Binghong |
| collection | PubMed - marine biology |
| contents | Structural and functional characterization of dsPETase05 for the degradation of Polyethylene terephthalate. Zhang, Lurong Zhou, Xiaoyu Yuan, Yuxuan Li, Haoqing Li, Jiachen Zhou, Yibing Du, Siyu Wang, Ziyu Han, Yiting Fan, Xinze Han, Daiyi Wang, Lijie Zhu, Cheng Ye, Sheng Wang, Yaxin Xu, Binghong Polyethylene Terephthalates Hydrolases Biodegradation, Environmental Burkholderiales Models, Molecular Hydrolysis Structure-Activity Relationship Substrate Specificity The enzymatic degradation of polyethylene terephthalate (PET) represents a promising sustainable strategy to address global plastic pollution. Among various plastic-degrading enzymes, PETase has been one of the most extensively studied and widely applied. Discovering novel PETase variants and elucidating their structure-function relationships are essential for developing more efficient enzymes. Here, we studied dsPETase05, a deep-sea PET hydrolase that was previously reported, which exhibits significantly enhanced PET degradation activity compared to the wild-type Ideonella sakaiensis PETase (IsPETase). This improvement was corroborated by atomic force microscopy (AFM) analysis of PET surface erosion and high-performance liquid chromatography (HPLC) quantification of hydrolysis products. We heterologously expressed and biochemically characterized dsPETase05, and resolved its crystal structure at 1.93 Å resolution. Structural analysis revealed that dsPETase05 adopts the typical α/β-hydrolase architecture found in PET-degrading enzymes, with distinctive amino acid substitutions near the catalytic triad that may contribute to its elevated activity. Our findings highlight the potential of marine-derived PETase for enzymatic plastic waste remediation and expand the repertoire of biocatalysts available for sustainable PET degradation. |
| format | Artículo científico |
| id | pubmed_41548779 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | International journal of biological macromolecules |
| record_format | pubmed |
| spellingShingle | Structural and functional characterization of dsPETase05 for the degradation of Polyethylene terephthalate. Zhang, Lurong Zhou, Xiaoyu Yuan, Yuxuan Li, Haoqing Li, Jiachen Zhou, Yibing Du, Siyu Wang, Ziyu Han, Yiting Fan, Xinze Han, Daiyi Wang, Lijie Zhu, Cheng Ye, Sheng Wang, Yaxin Xu, Binghong Polyethylene Terephthalates Hydrolases Biodegradation, Environmental Burkholderiales Models, Molecular Hydrolysis Structure-Activity Relationship Substrate Specificity Structural and functional characterization of dsPETase05 for the degradation of Polyethylene terephthalate. Zhang, Lurong Zhou, Xiaoyu Yuan, Yuxuan Li, Haoqing Li, Jiachen Zhou, Yibing Du, Siyu Wang, Ziyu Han, Yiting Fan, Xinze Han, Daiyi Wang, Lijie Zhu, Cheng Ye, Sheng Wang, Yaxin Xu, Binghong Polyethylene Terephthalates Hydrolases Biodegradation, Environmental Burkholderiales Models, Molecular Hydrolysis Structure-Activity Relationship Substrate Specificity The enzymatic degradation of polyethylene terephthalate (PET) represents a promising sustainable strategy to address global plastic pollution. Among various plastic-degrading enzymes, PETase has been one of the most extensively studied and widely applied. Discovering novel PETase variants and elucidating their structure-function relationships are essential for developing more efficient enzymes. Here, we studied dsPETase05, a deep-sea PET hydrolase that was previously reported, which exhibits significantly enhanced PET degradation activity compared to the wild-type Ideonella sakaiensis PETase (IsPETase). This improvement was corroborated by atomic force microscopy (AFM) analysis of PET surface erosion and high-performance liquid chromatography (HPLC) quantification of hydrolysis products. We heterologously expressed and biochemically characterized dsPETase05, and resolved its crystal structure at 1.93 Å resolution. Structural analysis revealed that dsPETase05 adopts the typical α/β-hydrolase architecture found in PET-degrading enzymes, with distinctive amino acid substitutions near the catalytic triad that may contribute to its elevated activity. Our findings highlight the potential of marine-derived PETase for enzymatic plastic waste remediation and expand the repertoire of biocatalysts available for sustainable PET degradation. |
| title | Structural and functional characterization of dsPETase05 for the degradation of Polyethylene terephthalate. |
| topic | Polyethylene Terephthalates Hydrolases Biodegradation, Environmental Burkholderiales Models, Molecular Hydrolysis Structure-Activity Relationship Substrate Specificity |
| url | https://pubmed.ncbi.nlm.nih.gov/41548779/ |