Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger

Carbohydr Res. 1994 Oct 17;263(2):257-69. doi: 10.1016/0008-6215(94)00177-4.


The activity of two forms of ferulic acid esterase (FAE) from Aspergillus niger on a synthetic feruloylated substrate (methyl ferulate) and on 11 different feruloylated oligosaccharides from sugar-beet pulp and wheat bran was determined. The enzymes exhibited different specificities for the various feruloylated substrates and were more active on certain substrates of cell-wall origin than on methyl ferulate. Both enzymes preferred the arabinose residue to which ferulic acid is attached in the furanose form. FAE-I had no clear preference for the type of linkage involved between the ferulic acid units and the oligosaccharide chain. In contrast, FAE-III had a clear requirement for ferulic acid to be attached to O-5 of the Ara f ring while no catalysis was observed when ferulic acid was attached to O-2. Both enzymes showed maximum activity on feruloylated trisaccharides. An increase in the length of the oligosaccharide chain did not preclude catalysis, but feruloylated oligosaccharides of a dp > 3 were hydrolysed at a reduced rate. Our results support the hypothesis that different kinds of ferulic acid esterases exist with different specificities for the oligosaccharide chain of the feruloylated substrates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus niger / enzymology*
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Carboxylic Ester Hydrolases / isolation & purification
  • Carboxylic Ester Hydrolases / metabolism*
  • Coumaric Acids / analysis*
  • Dietary Fiber / analysis*
  • Kinetics
  • Molecular Sequence Data
  • Oligosaccharides / chemistry*
  • Oligosaccharides / isolation & purification
  • Plants, Edible / chemistry*


  • Coumaric Acids
  • Dietary Fiber
  • Oligosaccharides
  • ferulic acid
  • Carboxylic Ester Hydrolases
  • feruloyl esterase