Cu2+-assisted laccase from Trametes versicolor enhanced self-polyreaction of triclosan.

Trametes versicolor

OncologyImmune support

SpeciesTurkey Tail, Yun Zhi

JournalChemosphere

Year2019

Key points

However, the mechanism on Cu 2+ impacts the self-polymerization of multi-purpose antimicrobial agent triclosan during L-MHPs is less understood
It was found that Cu 2+ -assisted laccase was effective in transforming triclosan, and the enzymatic reaction kinetic constants increased from 0.28 to 0.73 h -1 as the Cu 2+ concentration increased (0-3.0 mM)
Identification of intermediate products revealed that laccase oxidation predominantly generated triclosan dimers, trimers, and tetramers
The presence of Cu 2+ reinforced self-polymerization of triclosan via forming more triclosan oligomers relative to the Cu 2+ -free, which likely attributed to the enhancement of laccase activity and stability with Cu 2+ present in L-MHPs
A possible transformation mechanism was proposed as follows: Laccase initially catalyzed the oxidation of triclosan to generate phenoxy radical intermediates, which self-coupled to each other subsequently by radical-mediated CC and COC covalent binding, forming oligomers and polymers
These findings implied that Cu 2+ -assisted laccase was an effective strategy for rapidly self-polyreaction and detoxication of triclosan from Cu 2+ -triclosan combined polluted wastewater

Metadata-grounded summary

Citation abstract

Laccase-mediated humification processes (L-MHPs) can be used to polymerize and transform phenolic pollutants in water. However, the mechanism on Cu 2+ impacts the self-polymerization of multi-purpose antimicrobial agent triclosan during L-MHPs is less understood. Here, the influence of divalent metal ions (DMIs) on Trametes versicolor laccase activity was investigated. Particularly, the performance of Cu 2+ -assisted laccase in polymerizing and transforming triclosan was systematically characterized. Compared with DMI-free, the activity of laccase was obviously accelerated with Cu 2+ present due to copper is a vital component of laccase catalytic center. It was found that Cu 2+ -assisted laccase was effective in transforming triclosan, and the enzymatic reaction kinetic constants increased from 0.28 to 0.73 h -1 as the Cu 2+ concentration increased (0-3.0 mM). Identification of intermediate products revealed that laccase oxidation predominantly generated triclosan dimers, trimers, and tetramers. The presence of Cu 2+ reinforced self-polymerization of triclosan via forming more triclosan oligomers relative to the Cu 2+ -free, which likely attributed to the enhancement of laccase activity and stability with Cu 2+ present in L-MHPs. A possible transformation mechanism was proposed as follows: Laccase initially catalyzed the oxidation of triclosan to generate phenoxy radical intermediates, which self-coupled to each other subsequently by radical-mediated CC and COC covalent binding, forming oligomers and polymers. The growth inhibitory assays of freshwater microalgae (Chlamydomonas reinhardtii and Scenedesmus obliquus) demonstrated that the self-polymerized triclosan by L-MHPs had lower toxicity than the parent compound. These findings implied that Cu 2+ -assisted laccase was an effective strategy for rapidly self-polyreaction and detoxication of triclosan from Cu 2+ -triclosan combined polluted wastewater.

Citation

Sun K, Li S, Yu J, Gong R, Si Y, Liu X, et al. (2019). Cu2+-assisted laccase from Trametes versicolor enhanced self-polyreaction of triclosan. Chemosphere https://doi.org/10.1016/j.chemosphere.2019.03.079 PMID: 30903848

Open citation