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Fantastic Ferulic Acid Esterases and Their Functions

Leontakianakou, Savvina LU ; Adlercreutz, Patrick LU orcid and Nordberg Karlsson, Eva LU orcid (2025) In International Journal of Molecular Sciences 26(15).
Abstract

Ferulic acid (FA) is one of the most abundant hydroxycinnamic acids found in plant cell walls. Its dehydrodimers play an important role in maintaining the structural rigidity of the plant cell wall. Ferulic acid esterases (FAEs) act as debranching enzymes, cleaving the ester bond between FA and the substituted carbohydrate moieties in FA-containing polysaccharides in the plant cell wall. This enzymatic reaction facilitates the degradation of lignocellulosic materials and is crucial for the efficient utilization of biomass resources. This review focuses on the occurrence of ferulic acid in nature and its different forms and outlines the various classification systems of FAEs, their substrate specificity, and the synergistic interactions... (More)

Ferulic acid (FA) is one of the most abundant hydroxycinnamic acids found in plant cell walls. Its dehydrodimers play an important role in maintaining the structural rigidity of the plant cell wall. Ferulic acid esterases (FAEs) act as debranching enzymes, cleaving the ester bond between FA and the substituted carbohydrate moieties in FA-containing polysaccharides in the plant cell wall. This enzymatic reaction facilitates the degradation of lignocellulosic materials and is crucial for the efficient utilization of biomass resources. This review focuses on the occurrence of ferulic acid in nature and its different forms and outlines the various classification systems of FAEs, their substrate specificity, and the synergistic interactions of these enzymes with other CAZymes. Additionally, it highlights the various methods that have been developed for detecting hydroxycinnamic acids and estimating the enzyme activity, as well as the versatile applications of ferulic acid.

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author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
bioconversion, catalysis, hydroxycinnamic acids
in
International Journal of Molecular Sciences
volume
26
issue
15
article number
7474
publisher
MDPI AG
external identifiers
  • pmid:40806602
  • scopus:105013330107
ISSN
1661-6596
DOI
10.3390/ijms26157474
language
English
LU publication?
yes
id
e86840d4-0bf1-4789-ad3f-48045b7e15f2
date added to LUP
2025-11-10 12:40:42
date last changed
2025-11-11 03:14:34
@article{e86840d4-0bf1-4789-ad3f-48045b7e15f2,
  abstract     = {{<p>Ferulic acid (FA) is one of the most abundant hydroxycinnamic acids found in plant cell walls. Its dehydrodimers play an important role in maintaining the structural rigidity of the plant cell wall. Ferulic acid esterases (FAEs) act as debranching enzymes, cleaving the ester bond between FA and the substituted carbohydrate moieties in FA-containing polysaccharides in the plant cell wall. This enzymatic reaction facilitates the degradation of lignocellulosic materials and is crucial for the efficient utilization of biomass resources. This review focuses on the occurrence of ferulic acid in nature and its different forms and outlines the various classification systems of FAEs, their substrate specificity, and the synergistic interactions of these enzymes with other CAZymes. Additionally, it highlights the various methods that have been developed for detecting hydroxycinnamic acids and estimating the enzyme activity, as well as the versatile applications of ferulic acid.</p>}},
  author       = {{Leontakianakou, Savvina and Adlercreutz, Patrick and Nordberg Karlsson, Eva}},
  issn         = {{1661-6596}},
  keywords     = {{bioconversion; catalysis; hydroxycinnamic acids}},
  language     = {{eng}},
  number       = {{15}},
  publisher    = {{MDPI AG}},
  series       = {{International Journal of Molecular Sciences}},
  title        = {{Fantastic Ferulic Acid Esterases and Their Functions}},
  url          = {{http://dx.doi.org/10.3390/ijms26157474}},
  doi          = {{10.3390/ijms26157474}},
  volume       = {{26}},
  year         = {{2025}},
}