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Titolo:
Factors affecting the sequestration of aflatoxin by Lactobacillus rhamnosus strain GG
Autore:
Haskard, C; Binnion, C; Ahokas, J;
Indirizzi:
RMIT Univ, Key Ctr Appl & Nutr Toxicol, Melbourne, Vic 3001, Australia RMIT Univ Melbourne Vic Australia 3001 ol, Melbourne, Vic 3001, Australia
Titolo Testata:
CHEMICO-BIOLOGICAL INTERACTIONS
fascicolo: 1, volume: 128, anno: 2000,
pagine: 39 - 49
SICI:
0009-2797(20000815)128:1<39:FATSOA>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
LACTIC-ACID BACTERIA; MUTAGENIC HETEROCYCLIC AMINES; BIFIDOBACTERIUM-LONGUM; INVITRO BINDING; DAIRY STRAINS; GASSERI CELLS; ANTIMUTAGENICITY; FOOD; CARCINOGEN; FRACTIONS;
Keywords:
aflatoxin; lactic acid bacteria; binding; Lactobacillus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Haskard, C RMIT Univ, Key Ctr Appl & Nutr Toxicol, GPO Box 2476V, Melbourne, Vic 3001, Australia RMIT Univ GPO Box 2476V Melbourne Vic Australia 3001 Australia
Citazione:
C. Haskard et al., "Factors affecting the sequestration of aflatoxin by Lactobacillus rhamnosus strain GG", CHEM-BIO IN, 128(1), 2000, pp. 39-49

Abstract

The interaction of a potent carcinogen, aflatoxin B-1 (AFB(1)), with a probiotic strain of lactic acid bacteria, Luctobacillus rhamnosus strain GG (GG), has been investigated. The binding of AFB(1) to GG in the late exponential-early stationary phase was studied for viable, hr at-killed and acid-killed bacteria. In general, viable, heat-killed and acid-killed GG respondedin a similar manner. The effects of pronase E, lipase and m-periodate on AFB(1) binding and release were consistent with AFB(1) binding predominantlyto carbohydrate components of the bacteria. The effect of urea suggested hydrophobic interactions play a major role in binding. Increasing concentration (0.01-1 M) of NaCl or CaCl2 had minor effects on AFB(1) binding suggesting some involvement of electrostatic interactions. An increase in pH from 2.5 to 8.5 had no effect on AFB(1) binding but decreased binding of AFB(2a), possibly due to hydrogen bonding interactions. (C) 2000 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/20 alle ore 07:52:15