Lactic acid bacteria binding

Gram-positive lactic acid bacteria possess several MDRs that excrete out of the cell a wide variety of mainly cationic lipophilic cytotoxic compotmds as well as many clinically relevant antibiotics. These MDRs are either proton/drug antiporters belonging to the major facilitator superfamily of secondary transporters or ATP-dependent primary transporters belonging to the ATP-binding cassette superfamily of transport proteins. 

Orrhage, K., Sillerstrom, E., Gustafsson, J.A., Nord, C.E., and Rafter, J., Binding of mutagenic heterocyclic amines by intestinal and lactic acid bacteria, Res., 311,239-248,1994. 

Thyagaraja, N. and Hosono, A., Binding properties of lactic acid bacteria from Idly towards food-borne mutagens, FooJ C/jera. Toxicol, 32, 805-809, 1994. 

Lactobacillus and Propionibacterium strains were evaluated by El-Nezami et al. (2002) regarding their ability to remove seven Fusarium toxins (trichothecenes) from solution. Results showed that L. rhamnosus GG and Propionibacterium freudenrei-chii spp. shermanii JS were able to bind 18-93% of the deoxynivalenol, diacetoxy-scirpenol, and fusarenon in solution, while L. rhamnosus LC-705 removed 10-64% of deoxynivalenol and diacetoxyscirpenol from liquid medium. When comparing the ability of lactic and propionic bacteria to remove toxin from solution, Niderkom, Boudra, and Morgavi (2006) found that deoxynivalenol and fumonisin removal was strain specific, and that in general propionic acid bacteria was less efficient than lactic acid bacteria. The best results were achieved with L. rhamnosus for ranoval of deoxynivalenol (55%), Leuconostoc mesenteroides for fumonisin Bi (about 82%), and L. lactis for fumonisin B2 (100%) (Niderkom et al., 2006). 

El-Nezami, H., Kankaanpaa, R, Safininen, S., Afiokas, J. (1998a). Ability of dairy strains of lactic acid bacteria to bind a common food carcinogen, aflatoxin Bj. Food and Chemical Toxicology, 36(4), 321-326. 

Peltonen, K., El-Nezami, H., Haskard, C., Ahokas, J., Salminen, S. (2001). Aflatoxin B, binding by dairy strains of lactic acid bacteria and bifidobacteria. Journal of Dairy Science, 84, 2152-2156. 

Gross proteolytic activity of lactic acid bacteria is the sum of proteinase and peptidase activity. Normally, proteinases are plasmid-encoded and the enzymes are, in most cases, associated with the cell wall by a calcium ion-dependent binding. The synthesis of proteinase seems to be regulated by the growth medium (Exterkate, 1985 Bruinenberg et al., 1992). Normally, milk as growth medium forces strains to produce a high level of proteinase. 

Narita, J., Tanaka, X, Fukuda, H., and Kondo, A. (2008) System using tandem repeats of the cA peptidoglycan-binding domain from Lactococcus lacUs for display of both N- and C-terminal fusions on cell surfaces of lactic acid bacteria. Appl. Environ. Microhid., H, 1117-1123. 

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