Characterization of a feruloyl esterase from Lactobacillus plantarum

Lactobacillus plantarum is frequently found in the fermentation of plant-derived food products, where hydroxycinnamoyl esters are abundant. L. plantarum WCFS1 cultures were unable to hydrolyze hydroxycinnamoyl esters; however, cell extracts from the strain partially hydrolyze methyl ferulate and methyl p-coumarate. In order to discover whether the protein Lp_0796 is the enzyme responsible for this hydrolytic activity, it was recombinantly overproduced and enzymatically characterized. Lp_0796 is an esterase that, among other substrates, is able to efficiently hydrolyze the four model substrates for feruloyl esterases (methyl ferulate, methyl caffeate, methyl p-coumarate, and methyl sinapinate). A screening test for the detection of the gene encoding feruloyl esterase Lp_0796 revealed that it is generally present among L. plantarum strains. The present study constitutes the description of feruloyl esterase activity in L. plantarum and provides new insights into the metabolism of hydroxycinnamic compounds in this bacterial species. © 2013, American Society for Microbiology.This work was supported by grants AGL2011-22745, BFU2010-17929/BMC, Consolider INGENIO 2010 CSD2007-00063 FUN-C-FOOD (MINECO), S2009/AGR-1469 (ALIBIRD) (Comunidad de Madrid), and RM2012-00004 (Instituto Nacional de Investigación Agraria y Alimentaría). We are grateful to M. V. Santamaría and J. M. Barcenilla. M. Esteban-Torres is a recipient of a JAE-predoctoral fellowship from the CSIC.Peer Reviewe