Abstract
The aim of this study was to investigate the influence of bovine serum albumin (BSA) on the Lactobacillus-strain-mediated removal of benzo[a]pyrene (BaP). A combination of 0.5 mg/mL of BSA with 1.0 × 1010 CFU/mL bacterial cells had a removal of 49.61% BaP for strain 121, while a combination of 0.4 mg/mL of BSA with 1.0 × 1010 CFU/mL bacterial cells had a removal of 66.09% BaP for strain ML32. The results indicated that the binding of BaP to Lactobacillus-BSA was stable. BSA maintains Lactobacillus activity and BaP removal in the gastrointestinal environment. Heat and ultrasonic treatment of BSA reduced the BaP-binding ability of Lactobacillus-BSA. With the addition of BSA, the surface properties of the two strains affected BaP binding. The Fourier-transform infrared (FTIR) data demonstrated that O-H, N-H, C=O, and P=O groups were involved in the binding of BaP to Lactobacillus-BSA. Scanning electron microscopy (SEM) results revealed that the morphology of Lactobacillus-BSA bound to BaP was maintained. The adsorption of BaP by Lactobacillus-BSA was appropriately described by the pseudo-second-order kinetic model and Freundlich isotherm model. BSA enhances the affinity between the bacterial cells and BaP.