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

AuthorsEsteban-Torres, María ; Barcenilla Moraleda, José María ; Rivas, Blanca de las ; Muñoz, Rosario
KeywordsWine aroma
Lactic acid bacteria
Ethyl acetate
Issue Date2014
PublisherAmerican Chemical Society
CitationJournal of agricultural and food chemistry 62(22): 5118-5125 (2014)
AbstractThe 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.
Publisher version (URL)http://dx.doi.org/10.1021/jf500991m
Identifiersissn: 1520-5118
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