Abstract
Different fungal laccases were used as biocatalysts for the biotransformation of bisphenol A (BPA). The quantitative analysis by gas chromatography-mass spectrometry (GC MS) showed that BPA is more rapidly oxidized by Coriolopsis gallica laccase among the different fungal laccases tested. Carboxylic acid derivatives such as tartaric acid was found as BPA degradation products resulting from reactions catalyzed by 1 U ml(-1) of laccase from C. gallica in the presence of 1 mM of the laccase-mediator 1-hydroxybenzotriazole (HBT), while beta-hydroxybutyric acid resulted from oxidative reactions without HBT. BPA was completely removed within 3 h and pyroglutamic acid was found as a supplementary oxidative degradation product from HBT when identified by GC MS. Laccase played a critical role in BPA biodegradation and catalyzed a cross-coupling reaction. (C) 2016 Elsevier Ltd. All rights reserved.