Theoretical study on the influence of three different surfactants on the binding of laccase with bisphenol A.

• Three surfactants aggregated and encapsulated Laccase in different degrees. • Effect of environment on Laccase activity was weakened and conformation of residues was changed. • The results explain the lower degradation rate of BPA by adding TX-100 than by adding CTAB and SDBS. Laccase catalyzes the formation of phenoxyl radicals as an intermediate in Bisphenol A (BPA) degradation, and certain surfactants can affect the effectiveness of laccase in removing BPA from various effluents, yet the specific molecular details remain unclear. In this study, based on laccase and BPA complex, three surfactants, cetyltrimethylammonium bromide (CTAB), sodium dodecylbenzene sulfonate (SDBS), and TritonX-100 (TX-100), were introduced to construct four systems. We applied MD simulation along with MM-PBSA method to investigate the effects of different surfactants on the binding of laccase with BPA. During the MD simulations, these three surfactants enveloped the enzyme surface to varying degrees, causing the solvent to separate from parts of the laccase surface. The addition of CTAB and SDBS suppressed BPA degradation mainly by influencing the polar solvation free energy and van der Waals (vdW) interactions between laccase and BPA. In contrast, TX-100 promoted the degradation of BPA by reducing polar solvation free energy. This explains why in the laccase-BPA complex system the addition of a certain concentration of TX-100 resulted in a higher degradation rate compared to CTAB or SDBS. Our work clarifies the molecular mechanisms of the interaction between laccase and BPA under the influence of CTAB, SDBS, and TX-100 surfactants, and provides some guidance for laccase degradation of BPA. [ABSTRACT FROM AUTHOR]