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Survey of enzyme activity responsible for phenolic off-flavour production by Dekkera and Brettanomyces yeast
Authors
A Coulter
A Goodey
+44 more
A Zago
CD Curtin
Christopher M. Ford
D Stead
DAN Edlin
DAN Edlin
E Coton
E Rangarajan
G Degrassi
H Kumara
H Rodríguez
IA Papayannopoulos
J Hammond
JA Barnett
JA Donaghy
JD Baranowski
JF Cavin
JF Cavin
JF Cavin
JL Licker
JP Cai
L Barthelmebs
L Barthelmebs
L Dias
M Clausen
M Fadda
M Fadda
M Karababa
M Pardo
M Stratford
MA Lachance
MT Smith
N Vanbeneden
P Chatonnet
P Chatonnet
Paul R. Grbin
R Grandori
S Fling
T Heresztyn
V Harris
Victoria Harris
Vladimir Jiranek
Y Hashidoko
ZX Huang
Publication date
1 January 2009
Publisher
'Springer Science and Business Media LLC'
Doi
Abstract
© Springer. Part of Springer Science+Business MediaVolatile phenols are produced by Dekkera yeasts and are of organoleptic importance in alcoholic beverages. The key compound in this respect is 4-ethylphenol, responsible for the medicinal and phenolic aromas in spoiled wines. The microbial synthesis of volatile phenols is thought to occur in two steps, beginning with naturally occurring hydroxycinnamic acids (HCAs). The enzyme phenolic acid decarboxylase (PAD) converts HCAs to vinyl derivatives, which are the substrates of a second enzyme, postulated to be a vinylphenol reductase (VPR), whose activity results in the formation of ethylphenols. Here, both steps of the pathway are investigated, using cell extracts from a number of Dekkera and Brettanomyces species. Dekkera species catabolise ferulic, caffeic and p-coumaric acids and possess inducible enzymes with similar pH and temperature optima. Brettanomyces does not decarboxylate HCAs but does metabolise vinylphenols. Dekkera species form ethylphenols but the VPR enzyme appears to be highly unstable in cell extracts. A partial protein sequence for PAD was determined from Dekkera anomala and may indicate the presence of a novel enzyme in this genusVictoria Harris, Christopher M. Ford, Vladimir Jiranek and Paul R. Grbi
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oai:eprints.soton.ac.uk:482572
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