Peroxidase as a simultaneous degradation agent of ochratoxin A and zearalenone applied to model solution and beer

Zearalenone (ZEN) is one of the most common mycotoxin contaminants in food. For food safety, an efficient and environmental-friendly approach to ZEN degradation is significant. In this study, an Aspergillus niger strain, FS10, was stimulated with 1.0 μg/mL ZEN for 24 h, repeating 5 times to obtain a stressed strain, Zearalenone-Stressed-FS10 (ZEN-S-FS10), with high degradation efficiency. The results show that the degradation rate of ZEN-S-FS10 to ZEN can be stabilized above 95%. Through metabolomics analysis of the metabolome difference of FS10 before and after ZEN stimulation, it was found that the change of metabolic profile may be the main reason for the increase in the degradation rate of ZEN. The optimization results of degradation conditions of ZEN-S-FS10 show that the degradation efficiency is the highest with a concentration of 104 CFU/mL and a period of 28 h. Finally, we analyzed the degradation products by UPLC-q-TOF, which shows that ZEN was degraded into two low-toxicity products: C18H22O8S (Zearalenone 4-sulfate) and C18H22O5 ((E)-Zearalenone). This provides a wide range of possibilities for the industrial application of this strain.

Section: Conclusion and Prospectmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Exploration on the Enhancement of Detoxification Ability of Zearalenone and Its Degradation Products of Aspergillus niger FS10 under Directional Stress of Zearalenone

Yang

et al. 2021

“…Since ZEN is a feed and food contaminant of a considerable concern, the development of methods for its effective detoxification, which would provide keeping the quality of the treated feedstuffs and minimally affect the environment, is of a special attention. A large cluster of such investigations is focused on ZEN transformation or degradation to non-estrogenic derivatives [10,13] using microbes [16][17][18][19][20] or isolated enzymes [1,[21][22][23][24], especially lactonase (lactonohydrolase) from Clonostachys rosea [25][26][27]. The enzyme ability to open the lactone ring in a toxin molecule and to deprive the ZEN of the estrogenic activity is well documented [19,[28][29][30].…”

Section: Introductionmentioning

confidence: 99%

Effective Zearalenone Degradation in Model Solutions and Infected Wheat Grain Using a Novel Heterologous Lactonohydrolase Secreted by Recombinant Penicillium canescens

Щербакова

Рожкова

Осипов

et al. 2020

This paper reports the first results on obtaining an enzyme preparation that might be promising for the simultaneous decontamination of plant feeds contaminated with a polyketide fusariotoxin, zearalenone (ZEN), and enhancing the availability of their nutritional components. A novel ZEN-specific lactonohydrolase (ZHD) was expressed in a Penicillium canescens strain PCA-10 that was developed previously as a producer of different hydrolytic enzymes for feed biorefinery. The recombinant ZHD secreted by transformed fungal clones into culture liquid was shown to remove the toxin from model solutions, and was able to decontaminate wheat grain artificially infected with a zearalenone-producing Fusarium culmorum. The dynamics of ZEN degradation depending on the temperature and pH of the incubation media was investigated, and the optimal values of these parameters (pH 8.5, 30 °C) for the ZHD-containing enzyme preparation (PR-ZHD) were determined. Under these conditions, the 3 h co-incubation of ZEN and PR-ZHD resulted in a complete removal of the toxin from the model solutions, while the PR-ZHD addition (8 mg/g of dried grain) to flour samples prepared from the infected ZEN-polluted grain (about 16 µg/g) completely decontaminated the samples after an overnight exposure.

“…Although these methods achieved reduction in ZEN concentration, there were many disadvantages, such as non-selectivity, destruction of nutrients, and introduction of pollution in the feeds [21,22]. In comparison, microbial strains [23][24][25][26] or isolated enzymes [27][28][29] are always used as the biological methods to degrade ZEN to non-estrogenic derivatives, among which ZEN-degrading enzymes were a more attractive alternative due to their safety, efficiency, and irreversibility. It was reported that ZEN-degrading enzyme ZHD101 isolated from Clonostachys rosea cleaved to the lactone ring of ZEN and yielded non-toxic alkylresorcinol product [30][31][32][33].…”

Section: Introductionmentioning

confidence: 99%

Cloning and Characterization of Three Novel Enzymes Responsible for the Detoxification of Zearalenone

Liu¹,

Zhang²,

Zhang³

et al. 2022

Zearalenone is a common mycotoxin contaminant in cereals that causes severe economic losses and serious risks to health of human and animals. Many strategies have been devised to degrade ZEN and keep food safe. The hydrolase ZHD101 from Clonostachys rosea, which catalyzes the hydrolytic degradation of ZEN, has been studied widely. In the current research, three new enzymes that have the capacity to detoxify ZEN were identified, namely CLA, EXO, and TRI, showing 61%, 63%, and 97% amino acids identities with ZHD101, respectively. Three coding genes was expressed as heterologous in Escherichia coli BL21. Through biochemical analysis, the purified recombinant CLA, EXO, TRI, and ZHD101 exhibited high activities of degrading ZEN with the specific activity of 114.8 U/mg, 459.0 U/mg, 239.8 U/mg, and 242.8 U/mg. The optimal temperatures of CLA, EXO, TRI, and ZHD101 were 40 °C, 40 °C, 40 °C, and 45 °C, and their optimum pH were 7.0, 9.0, 9.5, and 9.0, respectively. Our study demonstrated that the novel enzymes CLA, EXO, and TRI possessed high ability to degrade ZEN from the model solutions and could be the promising candidates for ZEN detoxification in practical application.