Deciphering ligninolytic enzymes in the secretome of Pycnoporus sp. and their potential in degradation of 2-chlorophenol

Chlorophenols and their derivatives are persistent environmental pollutants, posing a threat to terrestrial and aquatic life. The biological approach for eliminating toxic contaminants is an effective, sustainable, and environmental friendly method. In this study, the crude enzymes present in the secretome of white-rot fungus (Pycnoporus sp.) were explored for the degradation of 2-chlorophenol. The activity of ligninolytic enzymes in the secretome was analyzed and characterized for their kinetics and thermodynamic properties. Laccase and manganese peroxidase were prevalent ligninolytic enzymes and exhibited temperature stability in the range of 50-65 & DEG;C and pH 4-5, respectively. The kinetic parameters Michaelis constant (K-m) and turnover number (K-cat) for Lac were 42.54 & mu;M and 45 s(-1) for 2,2 & PRIME;-azino-bis (3-ethylben- zothiazoline-6-sulfonic acid), and 93.56 & mu;M and 48 s(-1) towards 2,6-dimethoxyphenol whereas K-m and K-cat for MnP were 2039 & mu;M and 294 s(-1) for guaiacol as substrate. Treatment with the crude enzymes laccase and manganese peroxidase results in the reduction of 2-chlorophenol concentration, confirmed by UV-visible absorption spectra and high-performance liquid chromatography analysis. The detoxification of 2-chlorophenol into less toxic forms was confirmed by the plate toxicity assay. This study demonstrated that crude enzymes produced by Pycnoporus sp. could potentially minimize the toxicity of phenolic compounds in a sustainable way.