Zearalenone reduction by commercial peroxidase enzyme and peroxidases from soybean bran and rice bran

Abstract

The peroxidase (POD) enzyme, obtained from different sources, has been described in the literature regarding its good results of reduction in concentration or degradation levels of mycotoxins, such as aflatoxin B1, deoxynivalenol and zearalenone (ZEA). This study aimed at evaluating the action of commercial POD and POD from soybean bran (SB) and rice bran (RB) in ZEA reduction in a model solution and the characterisation of the mechanism of enzyme action. POD was extracted from SB and RB in phosphate buffer by orbital agitation. Evaluation of the action of commercial POD and POD from SB and RB in ZEA reduction was carried out in phosphate buffer and aqueous solution, respectively. Parameters of (Michaelis-Menten constant) (K) and maximal rate (V) were determined in the concentration range from 0.16 to 6 µg mL. ZEA reduction was determined and the mechanism of enzyme action was characterised by FTIR and high-pressure liquid chromatography-electrospray tandem mass spectrometry. Commercial POD and POD from RB and SB reduced ZEA concentration by 69.9%, 47.4% and 30.6% in 24 h, respectively. K values were 39.61 and 8.90 µM, whereas V values were 0.170 and 0.011 µM min for commercial POD and POD from RB, respectively. The characterisation of the mechanism of enzyme action showed the oxidoreductive action of commercial POD in the mycotoxin. The use of commercial POD and POD from agro-industrial by-products, such as SB and RB, could be a promising alternative for ZEA biodegradation.

Aflatoxin biotransformation by commercial peroxidase and its application in contaminated food

“…The results reveal that, although AFB 1 is not an ideal substrate for POD, the enzyme still has high affinity for this toxin. Therefore, this commercial POD has the potential to be applied to AFB 1 biotransformation processes, since the K M found by this study is lower than those found in other studies (0.288 to 22.9 mmol L −1 ) …”

“…However, prior studies stated K M values for several other organic compounds, such as 22.9 µmol L −1 tricosan, 15.7 µmol L −1 endocrine disrupting compounds, 9.049 µmol L −1 bisphenol A, 8.41 mmol L −1 phenol, 13.9 µmol L −1 petroleum hydrocarbons, 7.32 mmol L −1 rutin and 0.288 mmol L −1 guaiacol . In addition, the affinity between commercial POD and other mycotoxin was verified by the K M and V MAX parameters, resulting in 39.51 µmol L −1 and 0.170 µmol L −1 min −1 , respectively, for Zearalenone …”

Enzymes for Detoxification of Various Mycotoxins: Origins and Mechanisms of Catalytic Action

“…Aflatoxin dialdehyde aldo-keto reductase AKR7A1 (Figure 2 [15,16], Table 1 [17,18,19,20,21,22,23,24,25,26,27,28,29,30,31,32,33,34,35,36,37,38,39,40,41,42,43,44,45,46,47,48,49,50,51,52,53,54,55,56,57,58]) was isolated from rat liver, and its structure in complex with NADP + was solved [59]. This enzyme is assumed to reduce both aldehyde groups of dialdehyde of hydroxy aflatoxin B 2a , forming from 8,9-dihydrodiol aflatoxin B 1 , resulted in dihydroxy derivative.…”

“…Other peroxidases (e.g., from horseradish, rice, etc.) could be even more active by order of magnitude [39]. Possibly, peroxiredoxin homologues were repeatedly identified, but not recognized by a proteomic analysis at the cell level [103].…”

Whole-Genome Sequencing and Bioinformatics Analysis of Apiotrichum mycotoxinivorans: Predicting Putative Zearalenone-Degradation Enzymes

“…However, the degradation products α– and β–zearalenol (ZOL) still remain estrogenic biotoxicity ( Vekiru et al, 2010 ). Peroxiredoxin and homologs were reported to non-specifically act on ZEA by oxidizing the double bond at C1’/C2’ and/or hydroxy-groups at C2 and C4 ( Yu et al, 2012 ; Tang et al, 2013 ; Garcia et al, 2018 ). Vekiru et al (2010) characterized the structural and estrogenic activity of the ZEA degradation products processed by Trichosporon mycotoxinivorans ( T. mycotoxinivorans ), a basidiomycete yeast used as a microbial feed additive against mycotoxins ( Molnar et al, 2004 ; Schatzmayr et al, 2006 ).…”