Characterization of a feruloyl esterase from Lactobacillus plantarum

Appl Environ Microbiol. 2013 Sep;79(17):5130-6. doi: 10.1128/AEM.01523-13. Epub 2013 Jun 21.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caffeic Acids / metabolism
  • Carboxylic Ester Hydrolases / genetics
  • Carboxylic Ester Hydrolases / metabolism*
  • Cinnamates / metabolism
  • Gene Expression
  • Lactobacillus plantarum / enzymology*
  • Lactobacillus plantarum / genetics
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism

Substances

  • Caffeic Acids
  • Cinnamates
  • Recombinant Proteins
  • methyl-p-coumarate
  • antithiamine factor
  • methyl caffeate
  • Carboxylic Ester Hydrolases
  • feruloyl esterase
  • methyl ferulate