Detoxification of Aflatoxin B1 by Probiotic Yeasts and Bacteria Isolated From Dairy Products of Iran

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Abstract

Purpose: The present study was conducted to assess the ability of probiotic bacteria and yeasts strains to reduce aflatoxin B1 (AFB1) in gastrointestinal simulated conditions. Aflatoxins are potent carcinogenic and immunosuppressive agents. Acute exposure to a high level of aflatoxins leads to aflatoxicosis, which cause rapid death due to liver failure. It is anticipated that consumption of probiotic microorganisms capable of binding aflatoxins can reduce the risk of AFB1 on human health to a certain extent.

Methods: For this purpose, the bacteria (1 × 10 ¹⁰ cfu/mL) and yeasts count (2 × 10 ⁸ cells/mL) and AFB1 concentration (10 ppb) were adjusted. Then, the samples were incubated in the simulated medium, human gastric secretions and small intestine. The concentration of residual AFB1 was determined using enzyme-linked immunosorbent assay (ELISA). The results were statistically analyzed by SPSS 16 software.

Results: The native isolated bacteria and yeasts in the simulated gastrointestinal tract condition showed a significant effect on AFB1 reduction ( P <0.05). The AFB1 reduction ability of native probiotic microorganisms was strain dependent. The highest binding ability in bacteria belonged to Lactobacillus rhamnosus (31.14%) and at yeasts belonged to Saccharomyces cerevisiae (30.46%).

Conclusion: The use of probiotic strains is the appropriate biological method to reduce AFB1 in the human gastrointestinal tract. Probiotic bacteria could help to decrease the harmful effects of AFB1 in humans through enhancing the food safety.

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Surface binding of aflatoxin B(1) by lactic acid bacteria.

C Haskard, H El-Nezami, P E Kankaanpää … (2001)

Specific lactic acid bacterial strains remove toxins from liquid media by physical binding. The stability of the aflatoxin B(1) complexes formed with 12 bacterial strains in both viable and nonviable (heat- or acid-treated) forms was assessed by repetitive aqueous extraction. By the fifth extraction, up to 71% of the total aflatoxin B(1) remained bound. Nonviable bacteria retained the highest amount of aflatoxin B(1). Lactobacillus rhamnosus strain GG (ATCC 53103) and L. rhamnosus strain LC-705 (DSM 7061) removed aflatoxin B(1) from solution most efficiently and were selected for further study. The accessibility of bound aflatoxin B(1) to an antibody in an indirect competitive inhibition enzyme-linked immunosorbent assay suggests that surface components of these bacteria are involved in binding. Further evidence is the recovery of around 90% of the bound aflatoxin from the bacteria by solvent extraction. Autoclaving and sonication did not release any detectable aflatoxin B(1). Variation in temperature (4 to 37 degrees C) and pH (2 to 10) did not have any significant effect on the amount of aflatoxin B(1) released. Binding of aflatoxin B(1) appears to be predominantly extracellular for viable and heat-treated bacteria. Acid treatment may permit intracellular binding. In all cases, binding is of a reversible nature, but the stability of the complexes formed depends on strain, treatment, and environmental conditions.

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Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation

Matthew C. Taylor, Colin Jackson, David Tattersall … (2010)

Aflatoxins are polyaromatic mycotoxins that contaminate a range of food crops as a result of fungal growth and contribute to serious health problems in the developing world because of their toxicity and mutagenicity. Although relatively resistant to biotic degradation, aflatoxins can be metabolized by certain species of Actinomycetales. However, the enzymatic basis for their breakdown has not been reported until now. We have identified nine Mycobacterium smegmatis enzymes that utilize the deazaflavin cofactor F420H2 to catalyse the reduction of the α,β-unsaturated ester moiety of aflatoxins, activating the molecules for spontaneous hydrolysis and detoxification. These enzymes belong to two previously uncharacterized F420H2 dependent reductase (FDR-A and -B) families that are distantly related to the flavin mononucleotide (FMN) dependent pyridoxamine 5′-phosphate oxidases (PNPOxs). We have solved crystal structures of an enzyme from each FDR family and show that they, like the PNPOxs, adopt a split barrel protein fold, although the FDRs also possess an extended and highly charged F420H2 binding groove. A general role for these enzymes in xenobiotic metabolism is discussed, including the observation that the nitro-reductase Rv3547 from Mycobacterium tuberculosis that is responsible for the activation of bicyclic nitroimidazole prodrugs belongs to the FDR-A family.

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Binding of aflatoxin B1 to cell wall components of Lactobacillus rhamnosus strain GG.

J T Ahokas, A W Ouwehand, S Lahtinen … (2004)

The surface of Lactobacillus rhamnosus strain GG (LGG) has previously been shown to bind aflatoxin B(1) (AFB(1)) effectively, it being a food-borne carcinogen produced by certain species of Aspergillus fungi. To establish which components of the cell envelope are involved in the AFB(1) binding process, exopolysaccharides and a cell wall isolate containing peptidoglycan were extracted from LGG and its AFB(1) binding properties were tested. LGG was also subjected to various enzymatic and chemical treatments and their effects on the binding of AFB(1) by LGG were examined. No evidence was found for exopolysaccharides, cell wall proteins, Ca(2+) or Mg(2+) being involved in AFB(1) binding. The AFB(1) binding activity of the cell wall isolate indicates that AFB(1) binds to the cell wall peptidoglycan of LGG or compounds tightly associated with the peptidoglycan.

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Journal

Journal ID (nlm-ta): Adv Pharm Bull

Journal ID (iso-abbrev): Adv Pharm Bull

Journal ID (publisher-id): Adv Pharm Bull

Journal ID (pmc): APB

Journal ID (publisher-id): TBZMED

Title: Advanced Pharmaceutical Bulletin

Publisher: Tabriz University of Medical Sciences

ISSN (Print): 2228-5881

ISSN (Electronic): 2251-7308

Publication date (Print): July 2020

Publication date (Electronic): 11 May 2020

Volume: 10

Issue: 3

Pages: 482-487

Affiliations

¹Department of Food Science and Technology, Nutrition and Food Science Faculty, Tabriz University of Medical Sciences, Tabriz, Iran.

²Student Research Committee, Department of Food Science and Technology, Tabriz University of Medical Sciences, Tabriz, Iran.

³Food and Drug Safety Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.

⁴Drug Applied Research Center, Tabriz University of Medical Sciences, Tabriz, Iran.

⁵Department of Medical Nanotechnology, Faculty of Advanced Medical Science, Tabriz University of Medical Sciences, Tabriz, Iran.

Author notes

[* ] Corresponding Authors: Ali Ehsani and Ahmad Yari Khosroushahi, Tel. +98 41 33363234, Fax. +98 41 33363231, Email: ehsani@ 123456tbzmed.ac.ir , Email: yarikhosroushahia@ 123456tbzmed.ac.ir

Author information

Hajar Zolfaghari https://orcid.org/0000-0003-0594-9883

Arezou Khezerlou https://orcid.org/0000-0002-6976-7280

Ali Ehsani https://orcid.org/0000-0003-0391-9218

Ahmad Yari Khosroushahi https://orcid.org/0000-0003-3854-7311

Article

DOI: 10.34172/apb.2020.060

PMC ID: 7335981

PubMed ID: 32665910

SO-VID: 868b3a6d-8a3e-4f62-954c-c55be16eff68

License:

This is an Open Access article distributed under the terms of the Creative Commons Attribution (CC BY), which permits unrestricted use, distribution, and reproduction in any medium, as long as the original authors and source are cited. No permission is required from the authors or the publishers.

History

Date received : 20 May 2019

Date revision received : 09 November 2019

Date accepted : 02 December 2019

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Figures: 4, Tables: 1, References: 37, Pages: 6

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Detoxification of Aflatoxin B1 by Probiotic Yeasts and Bacteria Isolated From Dairy Products of Iran

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Most cited references 32

Surface binding of aflatoxin B(1) by lactic acid bacteria.

Identification and characterization of two families of F420H2-dependent reductases from Mycobacteria that catalyse aflatoxin degradation

Binding of aflatoxin B1 to cell wall components of Lactobacillus rhamnosus strain GG.

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