File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1128/AEM.68.7.3545-3549.2002
- Scopus: eid_2-s2.0-0036306526
- PMID: 12089040
- WOS: WOS:000176631600048
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Binding rather than metabolism may explain the interaction of two food-grade Lactobacillus strains with zearalenone and its derivative ά-zearalenol
Title | Binding rather than metabolism may explain the interaction of two food-grade Lactobacillus strains with zearalenone and its derivative ά-zearalenol |
---|---|
Authors | |
Issue Date | 2002 |
Citation | Applied And Environmental Microbiology, 2002, v. 68 n. 7, p. 3545-3549 How to Cite? |
Abstract | The interaction between two Fusarium mycotoxins, zearalenone (ZEN) and its derivative ά-zearalenol (α-ZOL), with two food-grade strains of Lactobacillus was investigated. The mycotoxins (2 μg ml-1) were incubated with either Lactobacillus rhamnosus strain GG or L. rhamnosus strain LC705. A considerable proportion (38 to 46%) of both toxins was recovered from the bacterial pellet, and no degradation products of ZEN and ά-ZOL were detected in the high-performance liquid chromatograms of the supernatant of the culturing media and the methanol extract of the pellet. Both heat-treated and acid-treated bacteria were capable of removing the toxins, indicating that binding, not metabolism, is the mechanism by which the toxins are removed from the media. Binding of ZEN or α4́-ZOL by lyophilized L. rhamnosus GG and L. rhamnosus LC705 was a rapid reaction: approximately 55% of the toxins were bound instantly after mixing with the bacteria. Binding was dependent on the bacterial concentration, and coincubation of ZEN with ά-ZOL significantly affected the percentage of the toxin bound, indicating that these toxins may share the same binding site on the bacterial surface. These results can be exploited in developing a new approach for detoxification of mycotoxins from foods and feeds. |
Persistent Identifier | http://hdl.handle.net/10722/178765 |
ISSN | 2023 Impact Factor: 3.9 2023 SCImago Journal Rankings: 1.016 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | ElNezami, H | en_US |
dc.contributor.author | Polychronaki, N | en_US |
dc.contributor.author | Salminen, S | en_US |
dc.contributor.author | Mykkänen, H | en_US |
dc.date.accessioned | 2012-12-19T09:49:37Z | - |
dc.date.available | 2012-12-19T09:49:37Z | - |
dc.date.issued | 2002 | en_US |
dc.identifier.citation | Applied And Environmental Microbiology, 2002, v. 68 n. 7, p. 3545-3549 | en_US |
dc.identifier.issn | 0099-2240 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/178765 | - |
dc.description.abstract | The interaction between two Fusarium mycotoxins, zearalenone (ZEN) and its derivative ά-zearalenol (α-ZOL), with two food-grade strains of Lactobacillus was investigated. The mycotoxins (2 μg ml-1) were incubated with either Lactobacillus rhamnosus strain GG or L. rhamnosus strain LC705. A considerable proportion (38 to 46%) of both toxins was recovered from the bacterial pellet, and no degradation products of ZEN and ά-ZOL were detected in the high-performance liquid chromatograms of the supernatant of the culturing media and the methanol extract of the pellet. Both heat-treated and acid-treated bacteria were capable of removing the toxins, indicating that binding, not metabolism, is the mechanism by which the toxins are removed from the media. Binding of ZEN or α4́-ZOL by lyophilized L. rhamnosus GG and L. rhamnosus LC705 was a rapid reaction: approximately 55% of the toxins were bound instantly after mixing with the bacteria. Binding was dependent on the bacterial concentration, and coincubation of ZEN with ά-ZOL significantly affected the percentage of the toxin bound, indicating that these toxins may share the same binding site on the bacterial surface. These results can be exploited in developing a new approach for detoxification of mycotoxins from foods and feeds. | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | Applied and Environmental Microbiology | en_US |
dc.subject.mesh | Aflatoxins - Metabolism | en_US |
dc.subject.mesh | Chromatography, High Pressure Liquid | en_US |
dc.subject.mesh | Estrogens, Non-Steroidal - Metabolism | en_US |
dc.subject.mesh | Lactobacillus - Metabolism | en_US |
dc.subject.mesh | Trichothecenes - Metabolism | en_US |
dc.subject.mesh | Zearalenone - Metabolism | en_US |
dc.subject.mesh | Zeranol - Analogs & Derivatives - Metabolism | en_US |
dc.title | Binding rather than metabolism may explain the interaction of two food-grade Lactobacillus strains with zearalenone and its derivative ά-zearalenol | en_US |
dc.type | Article | en_US |
dc.identifier.email | ElNezami, H: elnezami@hkucc.hku.hk | en_US |
dc.identifier.authority | ElNezami, H=rp00694 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1128/AEM.68.7.3545-3549.2002 | en_US |
dc.identifier.pmid | 12089040 | en_US |
dc.identifier.scopus | eid_2-s2.0-0036306526 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0036306526&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 68 | en_US |
dc.identifier.issue | 7 | en_US |
dc.identifier.spage | 3545 | en_US |
dc.identifier.epage | 3549 | en_US |
dc.identifier.isi | WOS:000176631600048 | - |
dc.publisher.place | United States | en_US |
dc.identifier.scopusauthorid | ElNezami, H=6603690577 | en_US |
dc.identifier.scopusauthorid | Polychronaki, N=6505944468 | en_US |
dc.identifier.scopusauthorid | Salminen, S=7102912002 | en_US |
dc.identifier.scopusauthorid | Mykkänen, H=7003915985 | en_US |
dc.identifier.issnl | 0099-2240 | - |