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Fungal Hydrophobin RolA Enhanced PETase Hydrolysis of Polyethylene Terephthalate
Abstract
Polyethylene terephthalate (PET) becomes one of the most well-known polyesters and is widely used as packaging material. Recently, polyethylene terephthalate hydrolase (PETase) has emerged as a potential biocatalyst demonstrating the ability to degrade polyethylene terephthalate (PET). We showed that the rate of PETase hydrolysis could be significantly increased in the presence of hydrophobin RolA. Hydrophobins represent a class of small fungal protein that has a high surface-active substance and can spontaneously self-assemble at hydrophilic-hydrophobic interfaces. In this work, a class I hydrophobin named RolA was extracted from the mycelium pellet collected from a fermentation culture of Aspergillus oryzae. The SDS-PAGE analysis of the isolated RolA showed the presence of 11 kDa polypeptide. Recombinant PETase from Ideonella sakaiensis was also successfully expressed in Escherichia coli as a soluble protein with molecular weight approximately 30 kDa. The hydrophobin RolA could enhance the PET hydrolysis in the presence of the recombinant PETase. The hydrolysis of PET bottle by RolA-PETase achieved the highest weight loss of 26% in 4 days. It is speculated that the wetting effect of RolA acts on PET surface converts PET to become hydrophilic that leads PETase easier to contact and attack the surface. Graphical Abstract.
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Lipases, cutinases, and esterases break down PET at high temperatures (50-70 °C) but not well at room temperature.
“They can do this at high temperatures (50-70 °C), but not very well at room temperature [289].”
From Harnessing bacterial consortia for effective bioremediation: targeted removal of heavy metals, hydrocarbons, and persistent pollutants (2025) · cites this paper as [289]
Lipases, cutinases, and esterases can break down PET.
“Lipases, cutinases, and esterases are some of the enzymes that can break down PET.”
From Harnessing bacterial consortia for effective bioremediation: targeted removal of heavy metals, hydrocarbons, and persistent pollutants (2025) · cites this paper as [289]
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Metadata
- Authors
- Puspitasari, N., Tsai, S.-L., & Lee, C.-K.
- Affiliations
- National Taiwan University of Science and Technology (TW)
- Corresponding author
- Lee, Cheng-Kang
- Venue
- Applied Biochemistry and Biotechnology
- Published
- 2020-06-06
- Volume
- 193
- Issue
- 5
- Pages
- 1284-1295
- ISSN
- 0273-2289 (ISSN-L)
- 1559-0291
- OpenAlex
- W3033189558
- Cited by
- 101
- References
- 0
- Citations by year
- 2026: 17 · 2025: 14 · 2024: 16 · 2023: 22 · 2022: 14 · 2021: 17 · 2020: 1
- FWCI
- 4.33
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Applied Biochemistry and Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
- Keywords
- polyethylene terephthalate, PETase, class I hydrophobins, PET hydrolysis, Aspergillus oryzae, Ideonella sakaiensis, surface wetting, polyester biodegradation, recombinant protein expression
- MeSH terms
- Aspergillus oryzae, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Fungal Proteins, Hydrolysis, Polyethylene Terephthalates, Hydrophobic and Hydrophilic Interactions
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