Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis
| Autor: | Nelson Carrasco, María Angélica Ganga, Claudio Martínez, Liliana Godoy |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Carboxy-lyases
Carboxy-Lyases Brettanomyces Brettanomyces bruxellensis Wine Reductase Microbiology Cofactor chemistry.chemical_classification Ethanol biology Molecular mass Chemistry Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzyme assay Molecular Weight Kinetics Enzyme Biochemistry Food Microbiology biology.protein Electrophoresis Polyacrylamide Gel Oxidoreductases Food Science |
| Zdroj: | INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY Artículos CONICYT CONICYT Chile instacron:CONICYT |
| ISSN: | 0168-1605 |
| DOI: | 10.1016/j.ijfoodmicro.2008.05.011 |
| Popis: | The presence of Brettanomyces bruxellensis has been correlated with an increase of phenolic aromas in wine. The production of these aromas results from the metabolization of cinnamic acids, present in the wine, to their ethyl derivatives. Hence, the participation of two enzymes has been proposed: a p-coumarate decarboxylase (CD) and a vinylphenol reductase (VR). Both enzymes were purified and characterized from B. bruxellensis. In denaturing conditions, the CD enzyme had a molecular mass of 21 kDa, while in native conditions its mass was 41 kDa. The optimal activity was obtained at a temperature of 40 degrees C and a pH of 6.0. For p-coumaric acid, the Km value and Vmax were 1.22+/-0.08 mM and 98+/-0.15 micromol/min mg, respectively. The VR enzyme had a molecular mass of 37 kDa in SDS-PAGE, while in natural conditions its mass was 118 kDa. The Km value was > 3.37+/-2.05 mM and its Vmax was 107.62+/-50.38 micromol/min mg for NADPH used as a cofactor. Both enzymatic activities were stable at pH 3.4, but in the presence of ethanol the CD activity decreased drastically while the VR activity was more stable. This is the first report that shows the presence of a CD and a VR enzyme in B. bruxellensis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect