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Screening of Bifidobacterium strains with assignment of functional groups to bind with benzo[a]pyrene under food
Sana Shoukat1, Yue Liu1, Abdul Rehman2
1College of Biological Sciences and Biotechnology, Beijing Forestry University, 100083 Beijing, China.
Abstract:
The purpose of this study was to find the component of the Bifidobacterium cell wall more particularly the functional groups from peptidoglycan involved in the mechanism of binding with Benzo[a]pyrene. Additionally, the effect of different stress factors (acid, heat, alkaline, oxidative, osmotic, enzymatic, and detergent factors) on the functional group and the overall binding mechanism of Bifidobacterium with B[a]p were also evaluated. Scanning electron microscopy (SEM) and Fourier-transform infrared spectroscopy (FTIR) were used to explain the binding mechanism of Bifidobacterium with B[a]p along with HPLC (high-performance liquid chromatography). The peptidoglycan-B[a]p complexes were highly stable after benzene washing. Peptidoglycan from Bifidobacterium infantis BY12 showed highest binding rate with B[a]p out of nine selected strains. FTIR spectra showed that the main functional groups involved in B[a]p binding were CO, OH and/or NH. FTIR spectrums along with SEM electrographs as a function of stress factors reveal that peptidoglycan structural integrity is important in B[a]p binding. Bifidobacterium longum subsp. infantis BY12 may be employed as a biological detoxification agent for the elimination of B[a]p from human diet and animal feed in the future.
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