Abstract
Vinyl phenol reductase activity was assayed in extracts from 19 strains of Dekkera bruxellensis isolated from wine. In all strains, vinyl phenol reductase activity was insensitive to the presence/absence of 4-vinyl guaiacol, confirming that expression is not related to the presence of the substrate. D. bruxellensis CBS 4481 showed the highest vinyl phenol reductase activity toward 4-vinyl guaiacol. Vinyl phenol reductase from D. bruxellensis CBS 4481 was purified to mass spectrometric homogeneity, and sequenced by trypsinolysis and mass spectrometry. The sequence of the purified protein showed convincing homology with a Cu/Zn superoxide dismutase in the D. bruxellensis AWRI 1499 genome, and indeed it was found to possess both vinyl phenol reductase and superoxide dismutase activities. A bioinformatics analysis of the sequence of vinyl phenol reductase/superoxide dismutase from D. bruxellensis CBS 4481 reveals the presence in this protein of cofactor-binding structural features, that are absent in sequences of superoxide dismutases from related microorganisms, that do not display vinyl phenol reductase activity.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Agnolucci M, Scarano S, Rea F, Toffanin A, Nuti M (2007) Detection of Dekkera/Brettanomyces bruxellensis in pressed Sangiovese grapes by real time PCR. Ital J Food Sci 19:155–166
Agnolucci M, Vigentini I, Capurso G, Merico A, Tirelli A, Compagno C, Foschino R, Nuti M (2009) Genetic diversity and physiological traits of Brettanomyces bruxellensis strains isolated from Tuscan Sangiovese wines. Int J Food Microbiol 130:238–244
Aguilar Uscanga MG, Escudero Abarca BI, Gomez Rodriguez J, Cortes Garcia R (2007) Carbon sources and their effect on growth, acetic acid and ethanol production by Brettanomyces bruxellensis in batch culture. J Food Process Eng 30:13–23
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding, Anal Biochem72:248–254
Brandam C, Castro-Martinez C, Delia ML, Ramon-Portugal F, Strehaino P (2008) Effect of temperature on Brettanomyces bruxellensis: metabolic and kinetic aspects. Can J Microbiol 54:11–18
Chatonnet P, Dubourdieu D, Boidron JN, Pons M (1992) The origin of ethyl-phenols in wine. J Sci Food Agric 60:165–178
Conterno L, Joseph LCM, Arvik TJ, Bisson LF (2006) Genetic and physiological characterization of Brettanomyces bruxellensis strains isolated from wine. Am J Enol Vitic 57:139–147
Godoy L, Martinez C, Carrasco N, Angelica GM (2008) Purification and characterization of a p-coumarate decarboxylase and a vinylphenolreductase from Brettanomyces bruxellensis. Int J Food Microbiol 127:6–11
Harris V, Ford CM, Jiranek V, Corbin PR (2009) Survey of enzyme activity responsible for phenolic off-flavour production by Dekkera and Brettanomyces yeast. Appl Microbiol Biotechnol 81:1117–1127
Hodgson EK, Fridovich I (1975a) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 14:5294–5299
Hodgson EK, Fridovich I (1975b) The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry 14:5299–5303
Jçrnvall H, Persson B, Krook M, Atrian S, Gonzalez- Duarte R, Jeffery J, Ghosh D (1995) Short chain dehydrogenases/reductases (SDR). Biochemistry 34:6003–6013
Jourd'heuil D, Laroux FS, Miles AM, Wink DA, Grisham MB (1999) Effect of superoxide dismutase on the stability of S-nitrosothiols. Arch Biochem Biophys 361:323–330
Lesk AM (1995) NAD-binding domains of dehydrogenases. Curr Opin Struct Biol 5:775–783
Licker JL, Acree TE, Henick-Kling T (1999) What is ‘Brett’ (Brettanomyces) flavour? A preliminary investigation. ACS Symp Ser 714:96–115
Liochev SI, Fridovich I (2004) CO2, not HCO3−, facilitates oxidations by Cu-Zn superoxide dismutase plus H2O2. Proc Natl Acad Sci USA 101:743–744
Okado-Matsumoto A, Fridovich I (2007) Putative denitrosylase activity of Cu, Zn-superoxide dismutase. Free Radic Biol Med 43:830–836
Oppermann U, Filling C, Hult M, Shafqat N, Wu X, Lindh M, Shafqat J, Nordling E, Kallberg Y, Persson B, Jörnvall H (2003) Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem Biol Interact 143–144:247–253
Renouf V, Lonvaud-Funel A (2007) Development of an enrichment medium to detect Dekkera/Brettanomyces bruxellensis, a spoilage wine yeast, on the surface of the grape berries. Microbiol Res 162:154–167
Tchobanov I, Gal L, Guilloux-Benatier MF, Remize F, Nardi T, Guzzo J, Serpaggi V, Hervé A (2008) Partial vinylphenolreductase purification and characterization from Brettanomyces bruxellensis. FEMS Microbiol Lett 284:213–217
Vigentini I, Romano A, Compagno C, Merico A, Molinari F, Tirelli A, Foschino R, Volonterio G (2008) Physiological and oenological traits of different Dekkera/Brettanomyces bruxellensis strains under wine-model conditions. FEMS Yeast Res 8:1087–1096
Vigentini I, De Lorenzis G, Picozzi C, Imazio S, Merico A, Galafassi S, Piškur J, Foschino R (2012) Intraspecific variations of Dekkera/Brettanomyces bruxellensis genome studied by capillary electrophoresis separation of the intron splice site profiles. Int J Food Microbiol 157:6–15
Author information
Authors and Affiliations
Corresponding author
Electronic supplementary material
Below is the link to the electronic supplementary material.
ESM 1
(DOC 143 kb)
Rights and permissions
About this article
Cite this article
Granato, T.M., Romano, D., Vigentini, I. et al. New insights on the features of the vinyl phenol reductase from the wine-spoilage yeast Dekkera/Brettanomyces bruxellensis . Ann Microbiol 65, 321–329 (2015). https://doi.org/10.1007/s13213-014-0864-5
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13213-014-0864-5