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1.
Toxins (Basel) ; 6(7): 2127-36, 2014 Jul 18.
Article in English | MEDLINE | ID: mdl-25046082

ABSTRACT

Paralytic shellfish toxins (PSTs) are non-protein neurotoxins produced by saltwater dinoflagellates and freshwater cyanobacteria. The ability of Lactobacillus rhamnosus strains GG and LC-705 (in viable and non-viable forms) to remove PSTs (saxitoxin (STX), neosaxitoxin (neoSTX), gonyautoxins 2 and 3 (GTX2/3), C-toxins 1 and 2 (C1/2)) from neutral and acidic solution (pH 7.3 and 2) was examined using HPLC. Binding decreased in the order of STX ~ neoSTX > C2 > GTX3 > GTX2 > C1. Removal of STX and neoSTX (77%-97.2%) was significantly greater than removal of GTX3 and C2 (33.3%-49.7%). There were no significant differences in toxin removal capacity between viable and non-viable forms of lactobacilli, which suggested that binding rather than metabolism is the mechanism of the removal of toxins. In general, binding was not affected by the presence of other organic molecules in solution. Importantly, this is the first study to demonstrate the ability of specific probiotic lactic bacteria to remove PSTs, particularly the most toxic PST-STX, from solution. Further, these results warrant thorough screening and assessment of safe and beneficial microbes for their usefulness in the seafood and water industries and their effectiveness in vivo.


Subject(s)
Lacticaseibacillus rhamnosus/chemistry , Marine Toxins/chemistry , Neurotoxins/chemistry , Water Pollutants, Chemical/chemistry , Lactic Acid , Probiotics
2.
Toxicon ; 46(1): 111-4, 2005 Jul.
Article in English | MEDLINE | ID: mdl-15922388

ABSTRACT

Three human probiotics, Lactobacillus rhamnosus strains GG and LC-705, and Bifidobacterium lactis strain Bb12, were found to bind the cyanobacterial peptide toxin microcystin-LR from water solutions. The highest removal percentage was 46%, observed with heat-treated L. rhamnosus strain GG (10(10) cells/ml) and a microcystin-LR concentration of 0.5 microg/ml during an incubation of 7 h at 35 degrees C.


Subject(s)
Bifidobacterium/chemistry , Lactobacillus/chemistry , Peptides, Cyclic/chemistry , Probiotics/chemistry , Humans , Marine Toxins , Microcystins , Protein Binding , Time Factors
3.
Inorg Chem ; 35(4): 1059-1064, 1996 Feb 14.
Article in English | MEDLINE | ID: mdl-11666285

ABSTRACT

A pH titration study shows that 6(A)-((2-(bis(2-aminoethyl)amino)ethyl)amino)-6(A)-deoxy-beta-cyclodextrin (betaCDtren) forms binary metallocyclodextrins, [M(betaCDtren)](2+), for which log(K/dm(3) mol(-)(1)) = 11.65 +/- 0.06, 17.29 +/- 0.05, and 12.25 +/- 0.03, respectively, when M(2+) = Ni(2+), Cu(2+), and Zn(2+), where K is the stability constant in aqueous solution at 298.2 K and I = 0.10 mol dm(-)(3) (NaClO(4)). The ternary metallocyclodextrins [M(betaCDtren)Trp](+), where Trp(-) is the tryptophan anion, are characterized by log(K/dm(3) mol(-)(1)) = 8.2 +/- 0.2 and 8.1 +/- 0.2, 9.5 +/- 0.3 and 9.4 +/- 0.2, and 8.1 +/- 0.1 and 8.3 +/- 0.1, respectively, where the first and second values represent the stepwise stability constants for the complexation of (R)- and (S)-Trp(-), respectively, when M(2+) = Ni(2+), Cu(2+), and Zn(2+). From comparisons of stabilities and UV-visible spectra, the binary and ternary metallocyclodextrins appear to be six-coordinate when M(2+) = Ni(2+) and Zn(2+) and five-coordinate when M(2+) = Cu(2+). The factors affecting the stoichiometries and stabilities of the metallocyclodextrins, are discussed and comparisons are made with related systems.

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