Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters
This study focuses on the biochemical characterization of a new hydrolase (Thb) expressed from anaerobic Thermoanaerobacterales, which could be used to improve biogas plant efficiency for plastic waste treatment. The specificity of Thb for various polyesters, including polyethylene terephthalate (PE...
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| Format: | Article |
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Frontiers Media S.A.
2025-01-01
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| Series: | Frontiers in Bioengineering and Biotechnology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fbioe.2024.1520680/full |
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| author | Chiara Siracusa Chiara Siracusa Lisa Fohler Lukas Leibetseder Gerald Striedner Chris Oostenbrink Felice Quartinello Georg M. Guebitz Georg M. Guebitz Doris Ribitsch Doris Ribitsch |
| author_facet | Chiara Siracusa Chiara Siracusa Lisa Fohler Lukas Leibetseder Gerald Striedner Chris Oostenbrink Felice Quartinello Georg M. Guebitz Georg M. Guebitz Doris Ribitsch Doris Ribitsch |
| author_sort | Chiara Siracusa |
| collection | DOAJ |
| description | This study focuses on the biochemical characterization of a new hydrolase (Thb) expressed from anaerobic Thermoanaerobacterales, which could be used to improve biogas plant efficiency for plastic waste treatment. The specificity of Thb for various polyesters, including polyethylene terephthalate (PET), polybutylene adipate terephthalate (PBAT), polybutylene succinate (PBS), and polylactic acid (PLA), was compared to the well-studied cutinase HiC from Humicola insolens. Based on gravimetric analysis and quantification (high-performance liquid chromatography (HPLC)) of monomers solubilized upon enzymatic hydrolysis, Thb was found to be more active on aromatic polyesters, while HiC led to a higher amount of hydrolysis products on aliphatic polyesters (PBS and PLA). Polyester hydrolysis was further investigated by scanning electron microscopy and infrared spectroscopy. A comparison of the two enzyme structures indicated the higher aromatic character of specific regions of the Thb surface as a possible reason for these differences in specificity. |
| format | Article |
| id | doaj-art-70fc1b4cd3fe4117b6c929e7cb743ffd |
| institution | Kabale University |
| issn | 2296-4185 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioengineering and Biotechnology |
| spelling | doaj-art-70fc1b4cd3fe4117b6c929e7cb743ffd2025-01-17T09:55:11ZengFrontiers Media S.A.Frontiers in Bioengineering and Biotechnology2296-41852025-01-011210.3389/fbioe.2024.15206801520680Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyestersChiara Siracusa0Chiara Siracusa1Lisa Fohler2Lukas Leibetseder3Gerald Striedner4Chris Oostenbrink5Felice Quartinello6Georg M. Guebitz7Georg M. Guebitz8Doris Ribitsch9Doris Ribitsch10Department of Agrobiotechnology, Institute of Environmental Biotechnology, IFA-Tulln, BOKU University, Tulln an der Donau, Austriaacib GmbH, Tulln an der Donau, AustriaInstitute of Bioprocess Science and Engineering, BOKU University, Vienna, AustriaInstitute of Bioprocess Science and Engineering, BOKU University, Vienna, AustriaInstitute of Bioprocess Science and Engineering, BOKU University, Vienna, AustriaDepartment of Material Science and Process Engineering, Institute of Molecular Modeling and Simulation, BOKU University, Vienna, Austriaacib GmbH, Tulln an der Donau, AustriaDepartment of Agrobiotechnology, Institute of Environmental Biotechnology, IFA-Tulln, BOKU University, Tulln an der Donau, Austriaacib GmbH, Tulln an der Donau, AustriaDepartment of Agrobiotechnology, Institute of Environmental Biotechnology, IFA-Tulln, BOKU University, Tulln an der Donau, Austriaacib GmbH, Tulln an der Donau, AustriaThis study focuses on the biochemical characterization of a new hydrolase (Thb) expressed from anaerobic Thermoanaerobacterales, which could be used to improve biogas plant efficiency for plastic waste treatment. The specificity of Thb for various polyesters, including polyethylene terephthalate (PET), polybutylene adipate terephthalate (PBAT), polybutylene succinate (PBS), and polylactic acid (PLA), was compared to the well-studied cutinase HiC from Humicola insolens. Based on gravimetric analysis and quantification (high-performance liquid chromatography (HPLC)) of monomers solubilized upon enzymatic hydrolysis, Thb was found to be more active on aromatic polyesters, while HiC led to a higher amount of hydrolysis products on aliphatic polyesters (PBS and PLA). Polyester hydrolysis was further investigated by scanning electron microscopy and infrared spectroscopy. A comparison of the two enzyme structures indicated the higher aromatic character of specific regions of the Thb surface as a possible reason for these differences in specificity.https://www.frontiersin.org/articles/10.3389/fbioe.2024.1520680/fullenzyme-based recyclingpolymer processingbiochemical characterizationaromatic polyestersaliphatic polyesters |
| spellingShingle | Chiara Siracusa Chiara Siracusa Lisa Fohler Lukas Leibetseder Gerald Striedner Chris Oostenbrink Felice Quartinello Georg M. Guebitz Georg M. Guebitz Doris Ribitsch Doris Ribitsch Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters Frontiers in Bioengineering and Biotechnology enzyme-based recycling polymer processing biochemical characterization aromatic polyesters aliphatic polyesters |
| title | Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters |
| title_full | Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters |
| title_fullStr | Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters |
| title_full_unstemmed | Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters |
| title_short | Activity of an anaerobic Thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters |
| title_sort | activity of an anaerobic thermoanaerobacterales hydrolase on aliphatic and aromatic polyesters |
| topic | enzyme-based recycling polymer processing biochemical characterization aromatic polyesters aliphatic polyesters |
| url | https://www.frontiersin.org/articles/10.3389/fbioe.2024.1520680/full |
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