Transformation of 17ß-Estradiol Mediated by Lignin Peroxidase: The Role of Veratryl Alcohol

Abstract

Lignin peroxidases (LiPs) are a group of extracellular enzymes excreted by certain fungi, e.g., Phanerochaete chrysosporium. These fungi also produce veratryl alcohol (VA) as a secondary metabolite to regulate the performance of LiP. 17ss-Estradiol (E2) is a natural female hormone that is strongly endocrine disruptive when released to the natural environment. The widespread occurrence of E2 and related hormonal chemicals in soil and water environments has been identified, representing an emerging contamination of concern. We report in this study that E2 can be effectively transformed and removed through reactions mediated by LiP and such reactions are significantly enhanced in the presence of VA. We systematically investigated LiP activity and enzymatic reaction kinetics in systems having VA absent or present. The results suggest that VA enhanced the transformation and removal of E2 by the combination of two effects: (i) mitigating LiP inactivation and (ii) modifying the enzyme catalytic kinetics. These findings provide insights into an important pathway that may govern the environmental transformation of E2 and other emerging endocrine-disrupting contaminants of similar nature in the environment, and provide a basis for potential development and optimization of enzyme-based processes for remediation and removal of these contaminants.