Interaction between laccase and diethylstilbestrol based on multispectral and chromatography analyses
Xiaolian Lin1,2, Hongyan Liu1,2, Lin Tang1,2
1College of Chemistry and Bioengineering, Guilin University of Technology, Guangxi Key Laboratory of Electrochemical and Magneto-chemical Functional Materials, Guilin, China.
Journal of Molecular Recognition : JMR
|January 4, 2022
Summary
Laccase enzymes can degrade harmful environmental pollutant diethylstilbestrol (DES). This study elucidates the interaction mechanism, revealing laccase
Area of Science:
- Biochemistry
- Environmental Science
- Enzymology
Background:
- Diethylstilbestrol (DES) is a persistent synthetic estrogen with adverse health effects.
- Environmental contamination by DES poses significant risks.
- Understanding enzyme interactions with DES is crucial for remediation.
Purpose of the Study:
- To investigate the interaction mechanism between laccase and DES.
- To determine the degradation capability of laccase on DES.
- To provide a theoretical basis for DES bioremediation.
Main Methods:
- Fluorescence spectroscopy
- Förster non-radiative energy transfer (FRET) theory
- UV-Vis absorption spectroscopy
- FT-IR spectroscopy
- High-performance liquid chromatography (HPLC)
Main Results:
- Laccase's intrinsic fluorescence was quenched by DES, indicating static quenching and binding.
- FRET analysis yielded an energy transfer efficiency of 22.08%.
- Spectroscopic data revealed conformational and secondary structure changes in laccase upon DES interaction.
- Laccase demonstrated degradation of DES over time.
Conclusions:
- Laccase interacts with DES, leading to conformational changes and degradation.
- The study provides insights into the laccase-DES reaction mechanism.
- Findings support laccase as a potential agent for DES bioremediation and safety evaluations.
