Survey of enzyme activity responsible for phenolic off-flavour production by Dekkera and Brettanomyces yeast
Survey of enzyme activity responsible for phenolic off-flavour production by Dekkera and Brettanomyces yeast
Volatile 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 genus.
4-Ethylguaiacol, 4-Ethylphenol, 4-Vinylguaiacol, 4-Vinylphenol, Hydroxycinnamic acid decarboxylase, Phenylacrylic decarboxylase, Spoilage
1117-1127
Harris, Victoria
b6d6e7b3-9a3b-48ea-a506-aa6716d5f973
Ford, Christopher M.
d52259d7-0d10-4fc3-91e5-6d2aedb973ed
Jiranek, Vladimir
8e5a8dfd-f5b2-43e3-928b-11dff324abc7
Grbin, Paul R.
e1cce428-cbfc-4cd2-aef0-c0e3a076a955
January 2009
Harris, Victoria
b6d6e7b3-9a3b-48ea-a506-aa6716d5f973
Ford, Christopher M.
d52259d7-0d10-4fc3-91e5-6d2aedb973ed
Jiranek, Vladimir
8e5a8dfd-f5b2-43e3-928b-11dff324abc7
Grbin, Paul R.
e1cce428-cbfc-4cd2-aef0-c0e3a076a955
Harris, Victoria, Ford, Christopher M., Jiranek, Vladimir and Grbin, Paul R.
(2009)
Survey of enzyme activity responsible for phenolic off-flavour production by Dekkera and Brettanomyces yeast.
Applied Microbiology and Biotechnology, 81 (6), .
(doi:10.1007/s00253-008-1708-7).
Abstract
Volatile 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 genus.
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More information
Accepted/In Press date: 2 September 2008
e-pub ahead of print date: 1 January 2009
Published date: January 2009
Additional Information:
Funding Information:
Acknowledgements The authors would like to thank Dr. Chris Curtin for supplying the yeast AWRI 1499 and Dr. Christopher Bagley for protein sequencing. This project was supported by Australia’s grapegrowers and winemakers through their investment body, the Grape and Wine Research and Development Corporation, with matching funds from the Australian Government (Project UA 03/01).
Keywords:
4-Ethylguaiacol, 4-Ethylphenol, 4-Vinylguaiacol, 4-Vinylphenol, Hydroxycinnamic acid decarboxylase, Phenylacrylic decarboxylase, Spoilage
Identifiers
Local EPrints ID: 482572
URI: http://eprints.soton.ac.uk/id/eprint/482572
ISSN: 0175-7598
PURE UUID: e3f5e6c3-d65f-4283-9adc-226a53497724
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Date deposited: 10 Oct 2023 16:58
Last modified: 18 Mar 2024 04:12
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Contributors
Author:
Victoria Harris
Author:
Christopher M. Ford
Author:
Vladimir Jiranek
Author:
Paul R. Grbin
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