In vitro assessment on effect of duodenal contents on the lead (Pb(2+)) binding capacity of two probiotic bacterial strains

Xing S 1 , Song Y 1 , Liang JB 2 , Faseleh Jahromi M 3 , Shokryazda P 3 , Mi J 1 Show all authors , Zhu C 4 , Wang J 5 , Liao X 6

Affiliations 

  • 1 College of Animal Science, South China Agriculture University, Guangzhou 510642, China
  • 2 Institute of Tropical Agriculture and Food Security, Universiti Putra Malaysia, Serdang 43400, Malaysia
  • 3 Institute of Tropical Agriculture and Food Security, Universiti Putra Malaysia, Serdang 43400, Malaysia; Agriculture Biotechnology Research Institute of Iran (ABRII), East and North‑East Branch, P.O.B. 91735 844, Mashhad, Iran
  • 4 Agro-biological Gene Research Center, Guangdong Academy of Agricultural Sciences, Guangzhou 510640, China
  • 5 College of Food Science, South China Agriculture University, Guangzhou 510642, China
  • 6 College of Animal Science, South China Agriculture University, Guangzhou 510642, China. Electronic address: xdliao@scau.edu.cn
Ecotoxicol Environ Saf, 2017 May;139:78-82.
PMID: 28113114 DOI: 10.1016/j.ecoenv.2017.01.016

Abstract

In vitro Lead (Pb(2+)) binding capacity of two probiotic bacteria strains, namely Bifidobacterium longumBB79 and Lactobacillus pentosusITA23, was assessed following incubation with the intestinal contents (IC) of laying hens. Results of this study demonstrated that IC treatment significantly enhanced (P<0.01) Pb(2+) binding capacity of both bacterial strains. Fourier transform infrared analysis indicated that several functional groups (O-H or N-H, C-H, C˭O, C-O, and C-O-C) on the bacteria cell wall involved in metal ion binding were altered after IC incubation, and new groups appeared between the 3700cm(-1) and 4000cm(-1)bands. Transmission electron microscopy demonstrated that after incubation with IC, unidentified IC components created new binding sites on the bacterial cell surface. These particles also changed the mechanism of Pb(2+) binding of the two strains from intracellular accumulation to extracellular adsorption.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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