Diaporthe/Phomopsis longicolla degrades an array of bisphenol analogues with secreted laccase

•Candidate endophytic fungus Diaporthe longicolla exhibits oxidase activity.•Oxidase activity is linked to secreted laccase enzyme capable of degrading BPA.•BPA-inducible laccase enzyme exhibits broad temperature and pH stability.•D. longicolla laccase enzyme efficiently degrades BPA and select BPA analogues. With recent initiatives to ban bisphenol A (BPA) in certain commercial products, manufacturers shifted to the production and use of BPA analogues. However, some of these BPA alternatives still possess endocrine disruptive activities. Many fungal enzymes are known to biodegrade phenolic compounds, such as BPA. However, the activity of these enzymes on BPA analogues remains unexplored. This study reports a secreted laccase from the endophytic fungus Diaporthe longicolla capable of degrading an impressive range of bisphenol analogues. The secreted crude enzymes are optimally active at pH 5 from 39 °C to 60 °C, efficiently degrading BPA as well as BPA analogues BPB, BPC, BPE and BPF. A purified form of laccase was identified from the crude fungal extract using FPLC and peptide sequencing. Furthermore, BPA induced the expression of this D. longicolla laccase gene. Overall, this paper demonstrated that the crude laccase enzyme from D. longicolla metabolizes BPA and select analogues, implicating the potential role of this fungus to remove environmental bisphenols.