Table 3.
Degradation of mycotoxin by recombinant enzymes.
| Enzyme | Gene Source | Target Toxin | Degrading Products | Expression System | Degrading Properties | Degradation Mechanism | Reference |
|---|---|---|---|---|---|---|---|
| Cytochrome P450 3A37 |
Turkey liver | AFB1 |
exo-AFBO aflatoxin Q1 |
E. coli |
exo-AFBO, Km: 287 ±21 µmol L−1 Vmax: 1.45 ± 0.07 nmol min−1 P450 aflatoxin Q1, Km: 302 ±51 µmol L−1 Vmax: 7.86 ±0.75 nmol min−1 |
Epoxidation | Rawal et al. (2010) |
| Peroxiredoxin (Prx) |
Acinetobacter sp. SM04 | ZEA | NM | E. coli | The optimum degradation pH and temperature was 9.0 and 70 °C in presence of H2O2 | Oxidation | Yu et al. (2012) |
| Lactonohydrolase Zhd518 |
Clonostachys rosea | ZEA | NM | E. coli | Activity of 207.0 U mg−1 with the optimal temperature and pH at 40 °C and 8.0 | NM | Wang et al. (2018) |
| Peroxiredoxin | Acinetobacter sp. SM04 | ZEA | NM | Saccharomyces cerevisiae | Optimal activity at pH 9.0, 80 °C and H2O2 concentration of 20 mmol L−1 Thermal stable, alkali resistance |
Oxidation | Tang et al. (2013) |
| Lactone hydrolase ZHD | Gliocladium roseum | ZEA | α-zearalenol and β-zearalenol | Pichia pastoris | Enzyme activity in shake flask fermentation was 22.5 U mL−1 with the specific activity of 4976.5 U mg−1 The maximum enzyme activity of the supernatant was 150.1 U mL−1 in 5-L fermenter |
Cleavage of lactone ring | Xiang et al. (2016) |
| Lactonohydrolase | Clonostachys rosea | ZEA | 1-(3,5-dihydroxy-phenyl)-10-hydroxy-1-undecen6-one | Lactobacillus reuteri Pg4 | Did not affect cell growth, acid and bile salt tolerance | Cleavage of lactone ring | Yang et al. (2017) |
| Lactonase | Neurospora crassa | ZEA | NM | Pichia pastoris | Optimal activity at pH 8.0 and 45 °C, highly stable at pH 6.0–8.0 for 1 h at 37 °C, the maximal enzyme activity reached 290.6 U mL−1 in 30-L fermenter |
NM | Bi et al. (2018) |
| Carboxylesterases, type B | Sphingopyxis sp. MTA144 | FB1 | NM | E. coli | NM | Deesterification | Heinl et al. (2010) |
| Aminotransferases, class III | HFB1 | Oxygen independence, temperature range 6–50 °C with an optimum at 35 °C, and pH adaptation 6–10 with an optimum at pH 8.5 | Deamination | ||||
| Aminotransferase FumI | Sphingopyxis sp. MTA144 | HFB1 | NM | E. coli | Optimal activity at pH 8.5 and 35 °C, low salt concentration, the kinetic parameters Km = 1.1 μmol L−1 and kcat = 104 min−1 | Eamination | Hartinger et al. (2011) |
| Putative amidase | Aspergillus niger | OTA | NM | NM | Thermostable, optimal activity at pH 6.0 and 66 °C | Hydrolysis | Dobritzsch et al. (2014) |
| N-acyl-L-amino acid amidohydrolase | Alcaligenes faecalis | OTA | β-phenylalanine | E. coli | Optimal activity at pH 6.5 and 50 °C | OTA amide bond hydrolysis | Zhang et al. (2019) |
| Dehydrogenase DepA |
Devosia mutans 17-2-E-8 | DON | 3-keto-DON | E. coli | NM | Oxidation of C3 position | Carere et al. (2017) |
| Cytochrome P450 | Sphingomonas sp. strain KSM1 | DON | 16-hydroxy-deoxynivalenol | E. coli | kcat/Km of 6.4 mmol L−1 s−1 | Hydroxylation | Ito et al. (2013) |
| Fusion ZHDCP enzyme |
Clonostachy rosea B. amyloliquefaciens ASAG |
ZEA OTA |
HZEA, DZEA, OTAα |
E. coli | 100% degradation rate at pH 7 and 30 °C in 2 h | Hydrolysis Removal of an amino acid from the end of a peptide chain |
Azam et al. (2019) |
| Manganese peroxidase |
Irpex lacteus, Phanerochaete chrysosporium, Ceriporiopsis subvermispora, Nematoloma frowardii |
AFB1 ZEA DON FB1 |
AFB1-8,9-epoxide | E. coli | In the presence of dicarboxylic acid malonate | Oxidoreduction | Wang et al. (2019) |
NM, not mentioned.