Prevention of β-Glucosidase Inhibition by High Molecular Mass Compounds During Enzymatic Wine Aroma Enhancement Using a Hollow Fiber 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 tw...
Main Authors: | , , |
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Format: | Article |
Language: | English |
Published: |
University of Zagreb Faculty of Food Technology and Biotechnology
2014-01-01
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Series: | Food Technology and Biotechnology |
Subjects: | |
Online Access: | http://hrcak.srce.hr/file/186441 |
Summary: | 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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ISSN: | 1330-9862 1334-2606 |