A novel enzyme for fumonisin detoxification

 BACKGROUND 

Fungi in grain and animal feed produce mycotoxins, posing a significant challenge for producers due to their harmful effects on humans and animals.

Among these mycotoxins, fumonisins contaminate a wide range of food and feed matrices, resulting in substantial economic losses for the agri-food sector.

While there are mechanical, thermal, and chemical methods to remove mycotoxins, they often generate hazardous by-products.

Enzymatic detoxification offers a promising, safer alternative.

However, current options for enzymatic fumonisin degradation are limited, and there is a lack of effective tools and benchmarks to guide the discovery of new enzymes.

 OBJETIVE 

The aim of this study was to:

1. Identify and characterize a novel enzyme capable of efficiently degrading fumonisins, using a metagenomic-based discovery pipeline.

2. Evaluate its potential application in real and industrial agri-food conditions.

 MATERIALS Y METHODS 

A metagenomic approach was used to search for candidate enzymes with fumonisin-degrading activity.

The selected enzyme was tested for its ability to degrade fumonisin B1 (FB1), B2 (FB2), and B3 (FB3) across various concentrations and conditions.

Assays were conducted under different pH levels (5.0–8.0), temperatures (30 °C to 90 °C), and fumonisin concentrations (1–90 ppm), both in pure solutions and in naturally contaminated maize matrices.

Sequence analysis was carried out to compare the enzyme with existing fumonisin-degrading enzymes.

 RESULTS 

The enzyme effectively degraded FB1, FB2, and FB3 under a broad range of conditions1.

Optimal activity is observed between pH 5.0 and 8.0, at temperatures ranging from 30 °C to 90 °C, and in fumonisin concentrations from 1 ppm to 90 ppm, both in pure form and in naturally contaminated maize matrices.

In terms of sequence similarity, it shares less than 15 % identity with the only previously known fumonisindegrading enzyme, FumD (WO2010031101A1).

 CONCLUSION 

This newly identified enzyme demonstrates strong potential as a fumonisin-degrading biocatalyst for application in food and feed processing.

Its robustness under industrially relevant pH and temperature conditions, along with its broad-spectrum activity, make it a strong candidate for the development of fumonisin-free animal feed.

Authors

Manuel Ferrer1, David Almendral1, Jog Raj2*, Hunor Farkaš2 and Marko Vasiljević2

1Instituto de Catálisis y Petroleoquímica, Consejo Superior de Investigaciones Científicas (CSIC), Españ
2Patent CO., DOO., Serbia

*Autor correspondiente: [email protected]

WMFmeetsSalzburg 7-9 April 2025, Salzburg, Austria

Reference

1. Ferrer et al., 2024. European Patent Application EP 4 357 460 A1.

Micotoxicosis prevention
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