Biocatalytic Degradation of Parabens Mediated by Cell Surface Displayed Cutinase

Parabens are emerging environmental contaminants with known endocrine-disrupting effects. This study created a novel biocatalyst (named as SDFsC) by expressing the enzyme Fusarium solani pisi cutinase (FsC) on the cell surface of Baker's yeast Sacchromycese cerevisiae and demonstrated successful enzyme-mediated removal of parabens for the first time. Parabens with different side chain structures had different degradation rates by the SDFsC. The SDFsC preferentially degraded the parabens with relatively long alkyl or aromatic side chains. The structure-dependent degradability was in a good agreement with the binding energy between the active site of FsC and different parabens. In real wastewater effluent solution, the SDFsC effectively degraded 800 μg/L of propylparaben, butylparaben, and benzylparaben, either as a single compound or as a mixture, within 48 h. The estrogenic activity of parabens was considerably reduced as the parent parabens were degraded into 4-hydroxybenzoic acid via hydrolysis pathway by the SDFsC. The SDFsC showed superior reusability and maintained 93% of its initial catalytic activity after six rounds of paraben degradation reaction. Results from this study provide scientific basis for developing biocatalysis as a green chemistry alternative for advanced treatment of parabens in sustainable water reclamation.