Abstract
Based on rational design, zearalenone degrading enzyme was evolved to improve the hydrolysis efficiency under acidic conditions. At pH 4.2 and 37 °C, the activity of the zearalenone degrading enzyme evolved with 8 mutation sites increased from 7.69 U/mg to 38.67 U/mg. Km of the evolved zearalenone degrading enzyme decreased from 283.61 μM to 75.33 μM. The evolved zearalenone degrading enzyme was found to effectively degrade zearalenone in pig stomach chyme. Molecular docking revealed an increase in the number of hydrogen bonds and π-sigma interactions between the evolved zearalenone degrading enzyme and zearalenone. The evolved zearalenone degrading enzyme was valuable for hydrolyzing zearalenone under acidic conditions.
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