Biodegradation of sulfonamide antibiotics through the heterologous expression of laccases from bacteria and investigation of their potential degradation pathways

In this study, seven laccase genes from different bacteria were linked with the signal peptides PelB, Lpp or Ompa for heterologous expression in E. coli. The recombinant strains were applied for the removal of sulfadiazine (SDZ), sulfamethazine (SMZ), and sulfamethoxazole (SMX). The results obtained for different signal peptides did not provide insights into the removal mechanism. The removal ratios of SDZ, SMZ, and SMX obtained with the recombinant strain 6#P at 60 h were around 92.0%, 89.0%, and 88.0%, respectively. The degradation pathways of sulfonamides have been proposed, including SO2 elimination, hydroxylation, oxidation, pyrimidine ring cleavage, and N-S bond cleavage. Different mediators participate in the degradation of antibiotics through different mechanisms, and different antibiotics have different responses to the same mediator. The addition of 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) slightly promoted the removal of sulfonamides by most recombinant strains with different signal peptides, especially for the recombinant strain 2#O. The removal of sulfonamides by 1-hydroxybenzotriazole (HBT) varied with the recombinant strains. Syringaldehyde (SA) had a slight inhibitory effect on the removal of sulfonamides, with the most significant effect on strains 7#L and 7#O.

Automated summary

In this study, seven laccase genes were heterologously expressed in E.coli using different signal peptides, and applied for the removal of sulfadiazine, sulfamethazine, and sulfamethoxazole. Different mediators like ABTS and HBT were found to either slightly promote or inhibit the removal of sulfonamides by the recombinant strains. The study also proposed degradation pathways of sulfonamides involving various mechanisms such as SO2 elimination and N-S bond cleavage.