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Published on: November 22, 2015
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Polyester hydrolysis is enhanced by a truncated esterase: Less is more.
Antonino Biundo1, Doris Ribitsch1,2, Georg Steinkellner2
1Institute of Environmental Biotechnology, University of Natural Resources and Life Science (BOKU), Tulln an der Donau, Austria.
Biotechnology Journal
|October 1, 2016
Summary
Researchers engineered an esterase enzyme from Clostridium botulinum (Cbotu_EstA) to enhance the hydrolysis of synthetic polyesters. The modified enzyme successfully degraded polyethylene terephthalate, a common plastic, opening new avenues for plastic modification.
Area of Science:
- Enzymology
- Polymer Science
- Biotechnology
Background:
- Clostridium botulinum esterase (Cbotu_EstA) can hydrolyze biodegradable polyesters.
- Modification of synthetic polyesters requires robust enzymatic solutions.
Purpose of the Study:
- To redesign Cbotu_EstA for improved hydrolysis of synthetic polyesters.
- To investigate the enzymatic degradation of polyethylene terephthalate (PET).
Main Methods:
- Protein engineering of Cbotu_EstA by N-terminal truncation (del71Cbotu_EstA).
- Enzymatic activity assays on various synthetic polyesters, including PET.
- 3D structural analysis of the wild-type and variant enzymes.
Main Results:
- The del71Cbotu_EstA variant exhibited enhanced hydrolytic activity compared to the wild-type enzyme.
- The engineered esterase successfully degraded polyethylene terephthalate (PET).
- Structural analysis revealed that N-terminal truncation exposed a hydrophobic surface, improving polymer sorption and active site access.
Conclusions:
- Enzyme redesign by N-terminal truncation is an effective strategy to enhance esterase activity on synthetic polyesters.
- This work provides a novel approach for enzymatic hydrolysis and modification of recalcitrant polymers like PET.
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