Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: Specificity for the phenolic moiety and binding to microcrystalline cellulose

C. B. Faulds, G. Williamson

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An inducible ferulic acid esterase (FAE-III) has been isolated, purified and partially characterized from Aspergillus niger after growth on oat spelt xylan. The purification procedure utilized ammonium sulphate precipitation, hydrophobic interaction and anion-exchange chromatography. The purified enzyme appeared almost pure by SDS-PAGE, with an apparent M(r) of 36000. A single band, corresponding to a pl of 3.3 was observed on isoelectric focusing. With methyl ferulate as substrate, the enzyme had a specific activity of 67 IU (mg protein)-1, pH and temperature optima of 5 and 55-60°C, respectively, and a K(m) of 2.08 mM and a V(max) of 175 μmol min-1 (mg protein)-1. The enzyme was also active upon methyl sinapinate, methyl-3,4-dimethoxy cinnamate and methyl p-coumarate, but not benzoic acid methyl esters or methyl caffeate. Similarly, Streptomyces olivochromogenes FAE showed activity against methyl ferulate, methyl sinapinate and methyl p-coumarate, but at a level 420-fold less (on methyl ferulate) than the A. niger esterase. No activity was detected against the benzoate methyl esters. For both enzymes, this shows the necessity for C-3 on the phenol ring to be methoxylated and the aliphatic region of the substrate to be unsaturated. The specific activity of FAE-III on destarched wheat bran was 31 U (mg protein)-1 in the presence of Trichoderma viride xylanase and 3 U (mg protein)-1 in the absence. Apparent pH dependent binding of A. niger FAE-III to microcrystalline cellulose was also demonstrated.

Original languageEnglish
Pages (from-to)779-787
Number of pages9
Issue number4
Publication statusPublished - 1 Jan 1994
Externally publishedYes


  • Aspergillus niger
  • Ferulic acid esterase
  • Streptomyces olivochromogenes
  • Xylanase

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