Brevibacterium enzymes as biological tools for ochratoxin A detoxification in dairy foods.

The origin of ochratoxin A (OTA) in cheeses is mainly due to mould growth during the ripening process, and to a lesser extent, to the use of OTA-contaminated milk in cheese production. Bacterial smear-ripened cheeses developed a smear microbiota on their rind during ripening that greatly contributes to its typical aroma and texture. Bacteria from the Brevibacterium genus belong to the typical smear microbiota of cheeses.

Ochratoxinase Is a Highly Specific, Metal-Dependent Amidohydrolase Suitable for OTA Biodetoxification in Food and Feed.

Microbial enzymes can be used as processing aids or additives in food and feed industries. Enzymatic detoxification of ochratoxin A (OTA) is a promising method to reduce OTA content. Here, we characterize the full-length enzyme ochratoxinase (OTA), an amidohydrolase from .

Structural and functional analysis of the key enzyme responsible for the degradation of ochratoxin A in the Alcaligenes genus.

The potential to degrade ochratoxin A (OTA), a highly poisonous mycotoxin, was investigated in cultures from Alcaligenes-type strains. Genome sequence analyses from different Alcaligenes species have permitted us to demonstrate a direct, causal link between the gene coding a known N-acyl-L-amino acid amidohydrolase from A. faecalis (AfOTH) and the OTA-degrading activity of this bacterium.

A new and promiscuous α/β hydrolase from Acinetobacter tandoii DSM 14970 inactivates the mycotoxin ochratoxin A.

The presence of ochratoxin A (OTA) in food and feed represents a serious concern since it raises severe health implications. Bacterial strains of the Acinetobacter genus hydrolyse the amide bond of OTA yielding non-toxic OTα and L-β-phenylalanine; in particular, the carboxypeptidase PJ15_1540 from Acinetobacter sp. neg1 has been identified as an OTA-degrading enzyme.

Food phenolics and Lactiplantibacillus plantarum.

Phenolic compounds are important constituents of plant food products. These compounds play a key role in food characteristics such as flavor, astringency and color. Lactic acid bacteria are naturally found in raw vegetables, being Lactiplantibacillus plantarum the most commonly used commercial starter for the fermentation of plant foods.

Dual 6Pβ-Galactosidase/6Pβ-Glucosidase GH1 Family for Lactose Metabolism in the Probiotic Bacterium WCFS1.

Intestinal lactic acid bacteria can help alleviate lactose maldigestion by promoting lactose hydrolysis in the small intestine. This study shows that protein extracts from probiotic bacterium WCFS1 possess two metabolic pathways for lactose metabolism, involving β-galactosidase (β-gal) and 6Pβ-galactosidase (6Pβ-gal) activities. As WCFS1 genome lacks a putative 6Pβ-gal gene, the 11 GH1 family proteins, in which their 6Pβ-glucosidase (6Pβ-glc) activity was experimentally demonstrated,, were assayed for 6Pβ-gal activity.

Non-redundant functionality of Lactiplantibacillus plantarum phospho-β-glucosidases revealed by carbohydrate utilization signatures associated to pbg2 and pbg4 gene mutants.

Aim: To increase our knowledge on the functionality of 6-phospho-β-glucosidases linked to phosphoenolpyruvate-dependent phosphotransferase systems (PTS) that are encountered in high redundancy in the Lactiplantibacillus plantarum WCFS1 genome.

Methods And Results: Two L. plantarum WCFS1 gene mutants that lacked one of the 6-phospho-β-glucosidases, ∆pbg2 (or ∆lp_0906) or ∆pbg4 (or ∆lp_2777) were constructed and the metabolic impact of these mutations assessed by high-throughput phenotyping (Omnilog).

Deciphering the Myrosinase-like Activity of WCFS1 among GH1 Family Glycoside Hydrolases.

The hydrolysis of plant glucosinolates by myrosinases (thioglucosidases) originates metabolites with chemopreventive properties. In this study, the ability to hydrolyze the glucosinolate sinigrin by cultures or protein extracts of WCFS1 was assayed. This strain possesses myrosinase-like activity as sinigrin was partly hydrolyzed by induced cultures but not by protein extracts.