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A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)
Open accessAbstract
A new esterase from Thermobifida halotolerans (Thh_Est) was cloned and expressed in E. coli and investigated for surface hydrolysis of polylactic acid (PLA) and polyethylene terephthalate (PET). Thh_Est is a member of the serine hydrolases superfamily containing the -GxSxG- motif with 85–87% homology to an esterase from T. alba, to an acetylxylan esterase from T. fusca and to various Thermobifida cutinases. Thh_Est hydrolyzed the PET model substrate bis(benzoyloxyethyl)terephthalate and PET releasing terephthalic acid and mono-(2-hydroxyethyl) terephthalate in comparable amounts (19.8 and 21.5 mmol/mol of enzyme) while no higher oligomers like bis-(2-hydroxyethyl) terephthalate were detected. Similarly, PLA was hydrolyzed as indicated by the release of lactic acid. Enzymatic surface hydrolysis of PET and PLA led to a strong hydrophilicity increase, as quantified with a WCA decrease from 90.8° and 75.5° to 50.4° and to a complete spread of the water drop on the surface, respectively.
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Cited by
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Metadata
- Authors
- Ribitsch, D., Herrero Acero, E., Greimel, K., Dellacher, A., Zitzenbacher, S., Marold, A., Rodriguez, R. D., Steinkellner, G., Gruber, K., Schwab, H., & Guebitz, G. M.
- Venue
- Polymers
- Publisher
- MDPI AG
- Published
- 2012-02-21
- Volume
- 4
- Issue
- 1
- Pages
- 617-629
- ISSN
- 2073-4360 (ISSN-L)
- OpenAlex
- W2168260741
- Cited by
- 193
- References
- 0
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- gold
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- The paper
- Ribitsch, D., Herrero Acero, E., Greimel, K., Dellacher, A., Zitzenbacher, S., Marold, A., Rodriguez, R. D., Steinkellner, G., Gruber, K., Schwab, H., & Guebitz, G. M. (2012). A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA). Polymers. https://doi.org/10.3390/polym4010617
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