Characterization of EstCOo8 and EstC34, intracellular esterases, from the wine-associated lactic acid bacteria Oenococcus oeni and Lactobacillus hilgardii
Characterization of EstCOo8 and EstC34, intracellular esterases, from the wine-associated lactic acid bacteria Oenococcus oeni and Lactobacillus hilgardii
Aim: To clone and characterize two related intracellular esterases from Oenococcus oeni and Lactobacillus hilgardii under wine-like conditions. Methods and Results: The published genome sequences for O. oeni and Lact. hilgardii were used to identify, clone and purify putative esterase genes from these species designated EstCOo8 and EstC34, respectively. Both esterases are members of family V of lipolytic enzymes. However, EstC34 contains an SGSLG nucleophilic elbow structural motif instead of the usual GGSLG motif which is conserved in other lactic acid bacteria. Both esterases exhibited greatest specificity for C2-C4 pNP-linked substrates and retained activity under wine-like conditions. EstCOo8 had an optimum temperature, pH, and ethanol concentration of 40°C, 5·5 and 6% (v/v), respectively. Whereas EstC34 had an optimum temperature, pH and ethanol concentration of 50°C, 5·0 and 10% (v/v), respectively. Conclusions: Both esterases were stable and retained activity under conditions that would be encountered in wine. They have the potential to reduce short-chain ethyl esters such as ethyl acetate. Significance and Impact of the Study: This study provides information that might help improve the performance of LAB during malolactic fermentation in wine in the future, either by strain selection, optimization or direct enzyme addition.
Esterase, Lactobacillus hilgardii, Oenococcus oeni, Wine
413-422
Sumby, K. M.
f54b8f1c-c29e-488b-ab5e-dbb9b2576ba9
Grbin, P. R.
e1cce428-cbfc-4cd2-aef0-c0e3a076a955
Jiranek, V.
8e5a8dfd-f5b2-43e3-928b-11dff324abc7
February 2013
Sumby, K. M.
f54b8f1c-c29e-488b-ab5e-dbb9b2576ba9
Grbin, P. R.
e1cce428-cbfc-4cd2-aef0-c0e3a076a955
Jiranek, V.
8e5a8dfd-f5b2-43e3-928b-11dff324abc7
Sumby, K. M., Grbin, P. R. and Jiranek, V.
(2013)
Characterization of EstCOo8 and EstC34, intracellular esterases, from the wine-associated lactic acid bacteria Oenococcus oeni and Lactobacillus hilgardii.
Journal of Applied Microbiology, 114 (2), .
(doi:10.1111/jam.12060).
Abstract
Aim: To clone and characterize two related intracellular esterases from Oenococcus oeni and Lactobacillus hilgardii under wine-like conditions. Methods and Results: The published genome sequences for O. oeni and Lact. hilgardii were used to identify, clone and purify putative esterase genes from these species designated EstCOo8 and EstC34, respectively. Both esterases are members of family V of lipolytic enzymes. However, EstC34 contains an SGSLG nucleophilic elbow structural motif instead of the usual GGSLG motif which is conserved in other lactic acid bacteria. Both esterases exhibited greatest specificity for C2-C4 pNP-linked substrates and retained activity under wine-like conditions. EstCOo8 had an optimum temperature, pH, and ethanol concentration of 40°C, 5·5 and 6% (v/v), respectively. Whereas EstC34 had an optimum temperature, pH and ethanol concentration of 50°C, 5·0 and 10% (v/v), respectively. Conclusions: Both esterases were stable and retained activity under conditions that would be encountered in wine. They have the potential to reduce short-chain ethyl esters such as ethyl acetate. Significance and Impact of the Study: This study provides information that might help improve the performance of LAB during malolactic fermentation in wine in the future, either by strain selection, optimization or direct enzyme addition.
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Published date: February 2013
Keywords:
Esterase, Lactobacillus hilgardii, Oenococcus oeni, Wine
Identifiers
Local EPrints ID: 482594
URI: http://eprints.soton.ac.uk/id/eprint/482594
ISSN: 1364-5072
PURE UUID: 52d12c5c-b730-4cef-9073-3c450b94f191
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Date deposited: 10 Oct 2023 17:00
Last modified: 18 Mar 2024 04:12
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Contributors
Author:
K. M. Sumby
Author:
P. R. Grbin
Author:
V. Jiranek
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