Computer-aided design of enzyme-polyelectrolyte complexes for mycotoxin degradation at acidic pH

The growing efforts towards preparation and investigation of supramolecular complexes formed by proteins and other polymers are determined by their promising biochemical and physical properties. In the current work, interaction of 6 enzymes, catalyzing transformation of various mycotoxins, with 8 polymers of variable structure and length was simulated to predict the best possible complex composition. The localization and portion of occupied areas on the enzyme surface varied widely, thus allowing the selection of those enzyme-polymer pairs for maximal retention of enzyme activity. Glucose oxidase (GOx) being active with a number of carbohydrates and mycotoxins was rationally selected to prepare complexes in vitro with some of these polyelectrolytes. Luckily, it was possible to determine enzymatic activity of these enzyme-polyelectrolyte complexes directly due to coupling reaction with horseradish peroxidase. A 180 nm-sized complex of GOx with Succinylated gelatin could be considered as a preferable one by its cumulative characteristics and especially by its turnover in the presence of methanol. This complex was active in patulin and zearalenone oxidation under low pH values and could be useful in practice for processes accompanied by acidification (like ensilaging, fermentation, etc.).