Simultaneous degradation of aflatoxin B1 and zearalenone by Porin and Peroxiredoxin enzymes cloned from Acinetobacter nosocomialis Y1

Mycotoxin contamination can cause severe health issues for both humans and animals. This study examined the potential of enzymes derived from Acinetobacter nosocomialis Y1 to simultaneously degrade aflatoxin B1 (AFB1) and zearalenone (ZEN), which could have significant implications in reducing mycotoxin contamination. Two enzymes, Porin and Peroxiredoxin, were identified with molecular weights of 27.8 and 20.8 kDa, respectively. Porin could completely degrade 2 µg/mL of AFB1 and ZEN within 24 h at 80 °C and 60 °C, respectively. Peroxiredoxin could completely degrade 2 µg/mL of AFB1 and reduce ZEN by 91.12% within 24 h. The addition of Na+, Cu2+, and K+ ions enhanced the degradation activities of both enzymes. LC-MS/MS analysis revealed that the molar masses of the degradation products of AFB1 and ZEN were 286 g/mol and 322.06 g/mol, and the products were identified as AFD1 and α or β-ZAL, respectively. Vibrio fischeri bioluminescence assays further confirmed that the cytotoxicity of the two degradation products was significantly lower than that of AFB1 and ZEN. Based on these results, it can be inferred that the degradation product of ZEN is β-ZAL. These findings suggest that both enzymes have the potential to be utilized as detoxification enzymes in food and feed. [Display omitted] •Expressed Porin and Peroxiredoxin simultaneously degraded AFB1 and ZEN.•Na+, Cu2+, and K+ions enhanced the degradation activity of these two enzymes.•Porin and peroxiredoxin were thermostable and alkali resistant enzymes.•The degradation products were identified as aflatoxin D1 and β zearalanol.•The cytotoxicity of degradation products was significantly reduced.