Fungal Hydrophobin RolA Enhanced PETase Hydrolysis of Polyethylene Terephthalate


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.

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Correspondence to Cheng-Kang Lee.

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The presenting author of this manuscript in ACB2019 is Nathania Puspitasari.

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Puspitasari, N., Tsai, SL. & Lee, CK. Fungal Hydrophobin RolA Enhanced PETase Hydrolysis of Polyethylene Terephthalate. Appl Biochem Biotechnol 193, 1284–1295 (2021).

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  • Hydrophobin
  • PETase
  • Recombinant
  • Self-assemble
  • PET degradation