The study investigated the characteristics of aerobic degradation of tetrabromobisphenol A (TBBPA) by Irpex lacteus F17 (I. lacteus F17) under four different cometabolic substrates (phenol, glucose, sodium pyruvate, and sodium citrate). The biodegradation of TBBPA by I. lacteus F17 could be enhanced via cometabolism, and glucose (8 g/L) was confirmed to be the optimum carbon source. For different initial solution pH ranging from 3.0 to 8.0, the results showed that I. lacteus F17 could be applied to biodegrade TBBPA in a wide pH range of 4.0-8.0, and the degradation rate could reach the maximum 75.31%, while the debromination rate reached the maximum 12.40% under pH 5.0. In addition, it has been confirmed that Mn 2+ (50 μmol/L) could promote the secretion of manganese peroxidase and TBBPA biodegradation efficiency. Seven intermediates were identified by gas chromatography-mass spectrometry analysis, and the possible degradation pathways were proposed, which indicated the biodegradation of TBBPA might be subjected to debromination, β-scission, hydroxylation, deprotonation, and oxidation reactions.

Complex bacteria communities that comprised Brevibacillus sp. (M1) and Achromobacter sp. (M2) with effective abilities of degrading decabromodiphenyl ether (BDE-209) were investigated for their degradation characteristics and mechanisms under aerobic conditions. The experimental results indicated that 88.4% of 10 mg L−1 BDE-209 could be degraded after incubation for 120 h under the optimum conditions of pH 7.0, 30 °C and 15% of the inoculation volume, and the addition ratio of two bacterial suspensions was 1:1. Based on the identification of BDE-209 degradation products via liquid chromatography–mass spectrometry (LC–MS) analysis, the biodegradation pathway of BDE-209 was proposed. The debromination, hydroxylation, deprotonation, breakage of ether bonds and ring-opening processes were included in the degradation process. Furthermore, intracellular enzymes had the greatest contribution to BDE-209 biodegradation, and the inhibition of piperyl butoxide (PB) for BDE-209 degradation revealed that the cytochrome P450 (CYP) enzyme was likely the key enzyme during BDE-209 degradation by bacteria M (1+2). Our study provided alternative ideas for the microbial degradation of BDE-209 by aerobic complex bacteria communities in a water system.