Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters

The gene lp-1002 from Lactobacillus plantarum WCFS1 encoding a putative lipase/esterase was cloned and overexpressed in Escherichia coli BL21(DE3). The purified Lp-1002 protein was biochemically characterized. Lp-1002 is an arylesterase which showed high hydrolytic activity on phenyl acetate. Althou...

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Autores: Esteban-Torres, María, Barcenilla Moraleda, José María, De Las Rivas, Blanca, Muñoz, Rosario
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2014
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/99870
Acceso en línea:http://hdl.handle.net/10261/99870
Access Level:acceso abierto
Palabra clave:Wine aroma
Lactic acid bacteria
flavor
Esterase
Ethyl acetate
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spelling Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine estersEsteban-Torres, MaríaBarcenilla Moraleda, José MaríaDe Las Rivas, BlancaMuñoz, RosarioWine aromaLactic acid bacteriaflavorEsteraseEthyl acetateThe gene lp-1002 from Lactobacillus plantarum WCFS1 encoding a putative lipase/esterase was cloned and overexpressed in Escherichia coli BL21(DE3). The purified Lp-1002 protein was biochemically characterized. Lp-1002 is an arylesterase which showed high hydrolytic activity on phenyl acetate. Although to a lesser extent, Lp-1002 also hydrolyzed most of the esters assayed including relevant wine aroma compounds. Importantly, Lp-1002 exhibited hydrolytic activity at winemaking conditions, although optimal catalytic activity is observed at 40 °C and pH 5-7. The effect of wine compounds on Lp-1002 activity was assayed. From the compounds assayed (ethanol, sodium metabisulfite, and malic, tartaric, lactic and citric acids), only malic acid slightly inhibited Lp-1002 activity. Lp-1002 is the first arylesterase described in a wine lactic acid bacteria and possessed suitable biochemical properties to be used during winemaking. © 2014 American Chemical Society.This work was financially supported by grants AGL2011-22745 and BFU2010-17929 (MINECO), S2009/AGR-1469 (ALIBIRD) (Comunidad de Madrid), and RM2012-00004 (INIA). M. Esteban-Torres is a recipient of a JAE predoctoral fellowship from the CSIC.Peer ReviewedAmerican Chemical SocietyMinisterio de Economía y Competitividad (España)Comunidad de MadridCSIC - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA)Consejo Superior de Investigaciones Científicas (España)European CommissionConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2014201420142014info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/99870reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#S2009/AGR-1469/ALIBIRDhttp://dx.doi.org/10.1021/jf500991mSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/998702026-05-22T06:33:51Z
dc.title.none.fl_str_mv Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
title Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
spellingShingle Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
Esteban-Torres, María
Wine aroma
Lactic acid bacteria
flavor
Esterase
Ethyl acetate
title_short Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
title_full Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
title_fullStr Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
title_full_unstemmed Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
title_sort Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters
dc.creator.none.fl_str_mv Esteban-Torres, María
Barcenilla Moraleda, José María
De Las Rivas, Blanca
Muñoz, Rosario
author Esteban-Torres, María
author_facet Esteban-Torres, María
Barcenilla Moraleda, José María
De Las Rivas, Blanca
Muñoz, Rosario
author_role author
author2 Barcenilla Moraleda, José María
De Las Rivas, Blanca
Muñoz, Rosario
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía y Competitividad (España)
Comunidad de Madrid
CSIC - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA)
Consejo Superior de Investigaciones Científicas (España)
European Commission
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Wine aroma
Lactic acid bacteria
flavor
Esterase
Ethyl acetate
topic Wine aroma
Lactic acid bacteria
flavor
Esterase
Ethyl acetate
description The gene lp-1002 from Lactobacillus plantarum WCFS1 encoding a putative lipase/esterase was cloned and overexpressed in Escherichia coli BL21(DE3). The purified Lp-1002 protein was biochemically characterized. Lp-1002 is an arylesterase which showed high hydrolytic activity on phenyl acetate. Although to a lesser extent, Lp-1002 also hydrolyzed most of the esters assayed including relevant wine aroma compounds. Importantly, Lp-1002 exhibited hydrolytic activity at winemaking conditions, although optimal catalytic activity is observed at 40 °C and pH 5-7. The effect of wine compounds on Lp-1002 activity was assayed. From the compounds assayed (ethanol, sodium metabisulfite, and malic, tartaric, lactic and citric acids), only malic acid slightly inhibited Lp-1002 activity. Lp-1002 is the first arylesterase described in a wine lactic acid bacteria and possessed suitable biochemical properties to be used during winemaking. © 2014 American Chemical Society.
publishDate 2014
dc.date.none.fl_str_mv 2014
2014
2014
2014
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/99870
url http://hdl.handle.net/10261/99870
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
S2009/AGR-1469/ALIBIRD
http://dx.doi.org/10.1021/jf500991m
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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