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  • Title: Characterization of a versatile arylesterase from Lactobacillus plantarum active on wine esters.
    Author: Esteban-Torres M, Barcenilla JM, Mancheño JM, de las Rivas B, Muñoz R.
    Journal: J Agric Food Chem; 2014 Jun 04; 62(22):5118-25. PubMed ID: 24856385.
    Abstract:
    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.
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