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Purification and partial characterization of Oenococcus oeni exoprotease
M E Farías1, M C Manca de Nadra
1Centro de Referencia para Lactobacilos (CERELA), Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 145, 4000, Tucumán, Argentina.
FEMS Microbiology Letters
|April 8, 2000
Summary
This study purified an Oenococcus oeni exoprotease, identifying it as an aspartic protease active on grape proteins. Its properties suggest a role in wine elaboration.
Area of Science:
- Enzymology
- Microbiology
- Food Science
Background:
- Oenococcus oeni is a key bacterium in winemaking.
- Exoproteases play roles in food and beverage fermentation.
- Understanding microbial enzymes is crucial for process optimization.
Purpose of the Study:
- To purify and characterize an exoprotease from Oenococcus oeni.
- To investigate its enzymatic properties and potential role in wine elaboration.
- To determine optimal conditions for its activity.
Main Methods:
- Two-step purification of the exoprotease.
- Molecular mass determination using gel filtration and SDS-PAGE.
- Enzyme activity assays on grape juice under varying conditions (temperature, pH).
- Inhibition studies with pepstatin A.
Main Results:
- Purified exoprotease with 14-fold specific activity increase and 44% recovery.
- Molecular mass suggests a dimer of 17 kDa subunits.
- Optimal activity at 25°C and pH 4.5.
- Enzyme degraded grape juice proteins rapidly and was inhibited by pepstatin A, indicating it's an aspartic protease.
Conclusions:
- The Oenococcus oeni exoprotease is an aspartic protease.
- Its activity profile, particularly at acidic pH, suggests involvement in wine elaboration.
- Further research could explore its application in modifying wine characteristics.