Mycotoxins: Enzymatic inactivation of mycotoxins

The detoxification of mycotoxins has been studied for a long time; the first reports of mycotoxins biotransformation in microorganisms were published in the 1960s. From a practical perspective, the first important result was discovered in the mid-1980s, when the inactivation capacity of T-2 toxin was proved. It was also proved that some organisms secrete enzymes that can cleave mycotoxins in specific regions,
generating sub products with no toxicity or with low toxicity.

Enzymes are organic substances, with protein nature, with intra and extra cellular activity, which have catalytic functions. These allow the production of chemical reactions, making the metabolism of living beings possible. This capacity of catalyzing reactions stimulates the use of enzymes for different uses.

Since the study of these ruminal microorganisms, the first enzymatic products for mycotoxins control were developed. Through industrial fermentation methods, these enzymes started to be produced on a large scale, with high performance and economic viability of the mycotoxin’s detoxification method. Apart from its enzymatic functionality (pH, temperature, specialty, etc.), another important aspect in the development of a mycotoxin inactivator is the interference of microorganisms that produce the enzymes and their metabolites, which come from the biotransformation of sensory and nutritional properties of the final food ration.