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.
| Main Authors: | , , , , |
|---|---|
| Other Authors: | |
| Format: | artículo biblioteca |
| Language: | English |
| Published: |
American Society for Microbiology
2013-09
|
| Online Access: | http://hdl.handle.net/10261/83794 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/100007652 http://dx.doi.org/10.13039/501100003339 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/100012818 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|