Expanding the feruloyl esterase gene family of Aspergillus niger by characterization of a feruloyl esterase, FaeC

Adiphol Dilokpimol, Miia R Mäkelä, Sadegh Mansouri, Olga Belova, Martin Waterstraat, Mirko Bunzel, Ronald P de Vries, Kristiina S Hildén

Research output: Contribution to journalArticleScientificpeer-review

25 Citations (Scopus)

Abstract

A feruloyl esterase (FAE) from Aspergillus niger N402, FaeC was heterologously produced in Pichia pastoris X-33 in a yield of 10mg/L. FaeC was most active at pH 7.0 and 50°C, and showed broad substrate specificity and catalyzed the hydrolysis of methyl 3,4-dimethoxycinnamate, ethyl ferulate, methyl ferulate, methyl p-coumarate, ethyl coumarate, methyl sinapate, and methyl caffeate. The enzyme released both ferulic acid and p-coumaric acid from wheat arabinoxylan and sugar beet pectin (up to 3mg/g polysaccharide), and acted synergistically with a commercial xylanase increasing the release of ferulic acid up to six-fold. The expression of faeC increased over time in the presence of feruloylated polysaccharides. Cinnamic, syringic, caffeic, vanillic and ferulic acid induced the expression of faeC. Overall expression of faeC was very low in all tested conditions, compared to two other A. niger FAE encoding genes, faeA and faeB. Our data showed that the fae genes responded differently towards the feruloylated polysaccharides and tested monomeric phenolic compounds suggesting that the corresponding FAE isoenzymes may target different substrates in a complementary manner. This may increase the efficiency of the degradation of diverse plant biomass.

Original languageEnglish
Pages (from-to)200-209
Number of pages10
JournalNew Biotechnology
Volume37
Issue numberPt B
DOIs
Publication statusPublished - 25 Jul 2017
MoE publication typeA1 Journal article-refereed

Keywords

  • Aspergillus niger
  • Ferulic acid
  • Feruloyl esterase
  • Pectin
  • Xylan

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