Ochratoxin A is a metabolite of microbial origin with a negative biological activity on human health. The aim of this work was the evaluation of four recombinant bacterial laccases from Lactobacillus paracasei (syn. Lacticaseibacillus paracasei) ENOLAB 4314, Lactococcus lactis ENOLAB 5298, Pediococcus parvulus ENOLAB 3909, and Companilactobacillus bobalius ENOLAB 4382 to degrade ochratoxin A (OTA) in wine. Several factors such as the presence and absence of redox mediators and copper, and the use of polyphenolic extracts from wine were addressed in sodium acetate buffer previously to the assays in wine. Ochratoxin A and oxidation products upon laccases action were analyzed by using high performance liquid chromatography coupled to mass spectrometry. Laccases were able to degrade ochratoxin A at different proportions depending on the enzyme origin and apparently its oxidation mechanism, rendering higher percentages of OTA oxidation in acetate buffer with (−)-epicatechin and copper than with ABTS, and without copper. In the experiments performed with natural red or white wines, the laccase of L. paracasei was the most OTA-degrading in red wine whereas in white wine was that of C. bobalius.
Thus, the presence and absence of redox mediators and copper played a pivotal role in the oxidation reaction of OTA. To our knowledge, this is the first time that the degradation of OTA by lactic acid bacterial laccases has been reported, as well as the influence of different mediators and copper. These findings provided better understanding of the biological removal mechanism of this health-risk mycotoxin in wine.
扫码关注我们
求助内容:
应助结果提醒方式:
