Study of the coumarate decarboxylase and vinylphenol reductase activities of Dekkera bruxellensis (anamorph Brettanomyces bruxellensis) isolates

GODOY, L.; Garrido, D.; Martínez C; Saavedra J.; Combina M.; GANGA, MA

Abstract

Aim: To evaluate the coumarate descarboxylase (CD) and vinylphenol reductase (VR) activities in Dekkera bruxellensis isolates and study their relationship to the growth rate, protein profile and random amplified polymorphic DNA (RAPD) molecular pattern. Methods and Results: CD and VR activities were quantified, as well, the growth rate, intracellular protein profile and molecular analysis (RAPD) were determined in 12 isolates of D. bruxellensis. All the isolates studied showed CD activity, but only some showed VR activity. Those isolates with the greatest growth rate did not present a different protein profile from the others. The FASC showed a relationship between RAPD molecular patterns and VR activity. Conclusion: CD activity is common to all of the D. bruxellensis isolates. This was not the case with VR activity, which was detected at a low percentage in the analysed micro-organisms. A correlation was observed between VR activity and the RAPD patterns. Significance and Impact of the Study: This is the first study that quantifies the CD and VR enzyme activities in D. bruxellensis, demonstrating that these activities are not present in all isolates of this yeast. © 2009 The Society for Applied Microbiology.

Más información

Título según WOS: Study of the coumarate decarboxylase and vinylphenol reductase activities of Dekkera bruxellensis (anamorph Brettanomyces bruxellensis) isolates
Título según SCOPUS: Study of the coumarate decarboxylase and vinylphenol reductase activities of Dekkera bruxellensis (anamorph Brettanomyces bruxellensis) isolates
Título de la Revista: LETTERS IN APPLIED MICROBIOLOGY
Volumen: 48
Número: 4
Editorial: Wiley
Fecha de publicación: 2009
Página de inicio: 452
Página final: 457
Idioma: English
URL: http://doi.wiley.com/10.1111/j.1472-765X.2009.02556.x
DOI:

10.1111/j.1472-765X.2009.02556.x

Notas: ISI, SCOPUS