Prevention of β-Glucosidase Inhibition by High Molecular Mass Compounds During Enzymatic Wine Aroma Enhancement Using a Hollow Fiber Reactor

Alicia Graciela Cid*, Mirta Daz and Guillermo Ellenrieder

National Research Institute for Chemical Industry (National University of Salta, National Council of Scientific and Technical Research), Av. Bolivia 5150, 4400 Salta, Argentina

Article history

Received May 21, 2013
Accepted March 4, 2014

Key words

glycosidases, β-glucosidase inhibition and stability in wine, wine aroma, membrane reactor


Enzyme activity and stability in a membrane reactor for wine aroma enhancement can be higher than when the enzyme is present in a free state since the catalyst would only be in contact with the low molecular mass 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 mass fraction (<10 kDa) obtained by ultrafiltration. The relative activities of Endozym Rouge and Endozym β-split β-glucosidases 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 molecular mass fraction. Endozym β-split β-glucosidase retained about 75 % of its initial activity after 14 days in the low molecular mass 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.

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