Prevention of beta-Glucosidase Inhibition by High Molecular Weight Compounds during Enzymatic Wine Aroma Enhancement by using of a Hollow Fiber Reactor

Abstract

Enzyme activity and stability in a membrane reactor for wine aroma enhancement could be higher than when the enzyme is present in a free state since the catalyst would only be in contact with the low molecular weight components of this beverage. To test this hypothesis, the activity and stability of two commercial β-glucosidases were measured in the presence of Tannat wine and of its low molecular weight (MW) fraction (< 10 kDa) obtained by ultrafiltration. The relative activities of Endozym Rouge and Endozym β-split β-glucosidase were higher in this fraction (3.8 % and 7.6 %, respectively) than in the whole wine (0.9 % and 5.6 %, respectively). Both enzymes were also more stable in the low MW fraction. Endozym β-split β-glucosidase retained about 75 % of its initial activity after 14 days in the low MW fraction, as contrasted with only 37.5 % in the wine. The ability of Endozym Rouge β-glucosidase to hydrolyze the synthetic substrate p-nitrophenylglucoside was examined in a simple batch membrane reactor. A rate of hydrolysis comparable to that obtained with the free Endozym Rouge β-glucosidase was reached. Finally, Endozym β-split β-glucosidase was used to hydrolyze the synthetic substrate in a hollow fiber membrane reactor and a substrate conversion near 58 % was achieved.