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Ochratoxinase Is a Highly Specific, Metal-Dependent Amidohydrolase Suitable for OTA Biodetoxification in Food and Feed. | LitMetric

Ochratoxinase Is a Highly Specific, Metal-Dependent Amidohydrolase Suitable for OTA Biodetoxification in Food and Feed.

J Agric Food Chem

Bacterial Biotechnology, Institute of Food Science, Technology and Nutrition (ICTAN), CSIC, José Antonio Novais 6, 28040 Madrid, Spain.

Published: August 2024

Microbial enzymes can be used as processing aids or additives in food and feed industries. Enzymatic detoxification of ochratoxin A (OTA) is a promising method to reduce OTA content. Here, we characterize the full-length enzyme ochratoxinase (OTA), an amidohydrolase from . OTA hydrolyzes OTA and ochratoxin B (OTB) mycotoxins efficiently and also other substrates containing phenylalanine, alanine, or leucine residues at their C-terminal position, revealing a narrow specificity profile. OTA lacks endopeptidase or aminoacylase activities. The structural basis of the molecular recognition by OTA of OTA, OTB, and a wide array of model substrates has been investigated by molecular docking simulation. OTA shows maximal hydrolytic activity at neutral pH and high temperature (65 °C) and retained high activity after prolonged incubation at 45 °C. The reduction of OTA levels in food products by OTA has been investigated using several commercial plant-based beverages. The results showed complete degradation of OTA with no detectable modification of beverage proteins. Therefore, the addition of OTA seems to be a useful procedure to eliminate OTA in plant-based beverages. Moreover, computational predictions of in vivo characteristics indicated that OTA is neither an allergenic nor antigenic protein. All characteristics found for OTA supported the suitability of its use for OTA detoxification in food and feed.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11342369PMC
http://dx.doi.org/10.1021/acs.jafc.4c02944DOI Listing

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