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| Main Authors: | , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Applied and environmental microbiology
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40810542/ |
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Table of Contents:
- Highly efficient degradation of polybutylene succinate (PBS) and polycaprolactone (PCL) by a recombinant marine fungal cutinase. Lang, Fengjuan Fei, Fan Sun, Chaomin Wu, Shimei Polyesters Carboxylic Ester Hydrolases Biodegradation, Environmental Fungal Proteins Biodegradable Plastics Polyenes Recombinant Proteins Butylene Glycols Polymers Biodegradable plastics, such as polybutylene succinate (PBS) and polycaprolactone (PCL), pose potential ecological risks due to their slow degradation rates in natural environments. Therefore, there is an urgent need to develop efficient enzymatic degradation technologies for the end-of-life management of PBS and PCL. In this study, we identified a marine fungal cutinase, Cut10, which exhibits significant degradation activity on PBS and PCL films under mild conditions. Cut10 can achieve degradation rates of 26.33% for PBS and 85.67% for PCL films within 20 min at 37°C, corresponding to degradation efficiencies of 315.96 kg PBS·(mol Cut10·h)⁻¹ and 1028.04 kg PCL·(mol Cut10·h)⁻¹, respectively. Notably, Cut10 showed even higher degradation efficiency on PBS and PCL emulsions, achieving degradation rates of 81.88% for PBS and 99.45% for PCL after just 1 min at room temperature. Product analysis showed that Cut10 degrades PBS into monomers and dimers and completely degrades PCL into monomers. The optimal degradation temperature for Cut10 was 23°C for both PBS and PCL. Even at 4°C, Cut10 retained high degradation activity, with relative activities of 60.58% for PBS emulsion and 81.41% for PCL emulsion. Additionally, Ca, Mg, and Mn significantly enhanced the degradation activity of Cut10, and the enzyme remained stable in the presence of chemicals such as methanol, ethanol, and glycerol. Finally, we identified that the amino acids Leu209 and Leu216 in Cut10 play key roles in its degradation functions toward both PBS and PCL.IMPORTANCEAlthough biodegradable plastics can be degraded, their degradation rates in natural environments are slower than expected. To address this issue, we identified a marine fungal cutinase, Cut10, which efficiently degrades various polyesters, including PBS and PCL, into their corresponding monomers, thereby facilitating subsequent recycling and remanufacturing. Notably, Cut10 achieves maximum degradation efficiency at ambient temperature (23°C) and retains high activity even at 4°C, meeting the energy efficiency requirements of industrial applications. Furthermore, Cut10 exhibits high stability in the presence of chemicals, making it suitable for multiphase catalytic systems while the enhancing effects of metal ions on its activity provide tunable targets for process optimization. The catalytic properties of Cut10 not only establish a theoretical framework for designing high-performance degrading enzymes but also offer essential support for developing eco-friendly plastic recycling systems.