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Article: Surface Binding of Aflatoxin B1 by Lactic Acid Bacteria

TitleSurface Binding of Aflatoxin B1 by Lactic Acid Bacteria
Authors
Issue Date2001
Citation
Applied And Environmental Microbiology, 2001, v. 67 n. 7, p. 3086-3091 How to Cite?
AbstractSpecific lactic acid bacterial strains remove toxins from liquid media by physical binding. The stability of the aflatoxin B1 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 B1 remained bound. Nonviable bacteria retained the highest amount of aflatoxin B1. Lactobacillus rhamnosus strain GG (ATCC 53103) and L. rhamnosus strain LC-705 (DSM 7061) removed aflatoxin B1 from solution most efficiently and were selected for further study. The accessibility of bound aflatoxin B1 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 B1. Variation in temperature (4 to 37°C) and pH (2 to 10) did not have any significant effect on the amount of aflatoxin B1 released. Binding of aflatoxin B1 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.
Persistent Identifierhttp://hdl.handle.net/10722/178749
ISSN
2015 Impact Factor: 3.823
2015 SCImago Journal Rankings: 1.891
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHaskard, CAen_US
dc.contributor.authorElNezami, HSen_US
dc.contributor.authorKankaanpää, PEen_US
dc.contributor.authorSalminen, Sen_US
dc.contributor.authorAhokas, JTen_US
dc.date.accessioned2012-12-19T09:49:29Z-
dc.date.available2012-12-19T09:49:29Z-
dc.date.issued2001en_US
dc.identifier.citationApplied And Environmental Microbiology, 2001, v. 67 n. 7, p. 3086-3091en_US
dc.identifier.issn0099-2240en_US
dc.identifier.urihttp://hdl.handle.net/10722/178749-
dc.description.abstractSpecific lactic acid bacterial strains remove toxins from liquid media by physical binding. The stability of the aflatoxin B1 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 B1 remained bound. Nonviable bacteria retained the highest amount of aflatoxin B1. Lactobacillus rhamnosus strain GG (ATCC 53103) and L. rhamnosus strain LC-705 (DSM 7061) removed aflatoxin B1 from solution most efficiently and were selected for further study. The accessibility of bound aflatoxin B1 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 B1. Variation in temperature (4 to 37°C) and pH (2 to 10) did not have any significant effect on the amount of aflatoxin B1 released. Binding of aflatoxin B1 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.en_US
dc.languageengen_US
dc.relation.ispartofApplied and Environmental Microbiologyen_US
dc.subject.meshAflatoxin B1 - Metabolismen_US
dc.subject.meshCulture Mediaen_US
dc.subject.meshEnzyme-Linked Immunosorbent Assayen_US
dc.subject.meshHot Temperatureen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshLactobacillus - Growth & Development - Metabolismen_US
dc.subject.meshLactococcus - Classification - Growth & Development - Metabolismen_US
dc.subject.meshProtein Bindingen_US
dc.titleSurface Binding of Aflatoxin B1 by Lactic Acid Bacteriaen_US
dc.typeArticleen_US
dc.identifier.emailElNezami, HS: elnezami@hkucc.hku.hken_US
dc.identifier.authorityElNezami, HS=rp00694en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1128/AEM.67.7.3086-3091.2001en_US
dc.identifier.pmid11425726-
dc.identifier.scopuseid_2-s2.0-0035406531en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035406531&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume67en_US
dc.identifier.issue7en_US
dc.identifier.spage3086en_US
dc.identifier.epage3091en_US
dc.identifier.isiWOS:000169605400030-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridHaskard, CA=6602356857en_US
dc.identifier.scopusauthoridElNezami, HS=6603690577en_US
dc.identifier.scopusauthoridKankaanpää, PE=6701573026en_US
dc.identifier.scopusauthoridSalminen, S=7102912002en_US
dc.identifier.scopusauthoridAhokas, JT=7006308329en_US

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