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Aflatoxin Detoxification by Manganese Peroxidase Purified from Pleurotus ostreatus

Summary

This research examined an enzyme from edible mushrooms that can break down dangerous toxins found in contaminated food. The enzyme, called manganese peroxidase, was extracted and purified from oyster mushrooms and shown to effectively destroy aflatoxin B1, a harmful compound produced by certain molds. Impact on everyday life: • Could lead to safer food products by providing a natural way to remove dangerous toxins • Demonstrates new applications for common edible mushrooms in food safety • Offers an environmentally friendly approach to dealing with food contamination • Could reduce food waste by providing ways to detoxify contaminated products • Shows potential for developing new food safety technologies using natural enzymes

Background

Manganese peroxidase (MnP) is an extracellular heme protein produced by wood rotting fungi that catalyzes the H2O2-dependent oxidation of Mn II to Mn III. The enzyme plays an important role in lignin degradation and has shown promise in detoxifying various compounds including mycotoxins. The mushroom genus Pleurotus has demonstrated capacity to degrade lignin while preserving cellulose, making it biotechnologically relevant for delignification processes.

Objective

This study aimed to purify and characterize manganese peroxidase from the edible mushroom Pleurotus ostreatus and evaluate its potential for detoxifying aflatoxin B1. The research focused on both biochemical characterization of the purified enzyme and molecular analysis of its encoding gene.

Results

The purified MnP showed a molecular mass of 42 kDa with optimal activity at pH 4-5 and 25°C. The enzyme activity was enhanced by Mn2+, Cu2+, Ca2+ and K+ ions while being inhibited by Hg2+ and Cd2+. The MnP-cDNA consisted of 497 bp encoding 165 amino acids. The enzyme demonstrated significant aflatoxin B1 detoxification capability, achieving 90% detoxification after 48 hours at 1.5 U/mL enzyme concentration.

Conclusion

The study successfully purified and characterized MnP from P. ostreatus, demonstrating its effectiveness in aflatoxin B1 detoxification. The enzyme showed optimal activity under mild conditions and maintained stability in the presence of various metal ions. The high detoxification rate of 90% suggests potential applications in mycotoxin remediation.
  • Published in:Brazilian Journal of Microbiology,
  • Study Type:Laboratory Research,
  • Source: 10.1590/S1517-83822014005000026
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