title: Expanding the feruloyl esterase gene family of Aspergillus niger by characterization of a feruloyl esterase, FaeC.
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.
authors.affiliation: Fungal Physiology, CBS-KNAW Fungal Biodiversity Centre & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, Utrecht, The Netherlands.
authors.forename: Adiphol
authors.initials: A
authors.lastname: Dilokpimol
authors.affiliation: Department of Food and Environmental Sciences, Division of Microbiology and Biotechnology, Viikki Biocenter 1, University of Helsinki, Finland.
authors.forename: Miia R
authors.initials: MR
authors.lastname: Mäkelä
authors.affiliation: Department of Food and Environmental Sciences, Division of Microbiology and Biotechnology, Viikki Biocenter 1, University of Helsinki, Finland.
authors.forename: Sadegh
authors.initials: S
authors.lastname: Mansouri
authors.affiliation: Fungal Physiology, CBS-KNAW Fungal Biodiversity Centre & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, Utrecht, The Netherlands.
authors.forename: Olga
authors.initials: O
authors.lastname: Belova
authors.affiliation: Department of Food Chemistry and Phytochemistry, Institute of Applied Biosciences, Karlsruhe Institute of Technology (KIT), Adenauerring 20a, Building 50.41, 76131 Karlsruhe, Germany.
authors.forename: Martin
authors.initials: M
authors.lastname: Waterstraat
authors.affiliation: Department of Food Chemistry and Phytochemistry, Institute of Applied Biosciences, Karlsruhe Institute of Technology (KIT), Adenauerring 20a, Building 50.41, 76131 Karlsruhe, Germany.
authors.forename: Mirko
authors.initials: M
authors.lastname: Bunzel
authors.affiliation: Fungal Physiology, CBS-KNAW Fungal Biodiversity Centre & Fungal Molecular Physiology, Utrecht University, Uppsalalaan 8, Utrecht, The Netherlands.
authors.forename: Ronald P
authors.initials: RP
authors.lastname: de Vries
authors.affiliation: Department of Food and Environmental Sciences, Division of Microbiology and Biotechnology, Viikki Biocenter 1, University of Helsinki, Finland. Electronic address: Kristiina.S.Hilden@helsinki.fi.
authors.forename: Kristiina S
authors.initials: KS
authors.lastname: Hildén
mesh_terms: D000595:Amino Acid Sequence; D001234:Aspergillus niger / Q000201:enzymology* / Q000235:genetics*; D002265:Carboxylic Ester Hydrolases / Q000235:genetics* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010802:Phylogeny; D016415:Sequence Alignment; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D002265:Carboxylic Ester Hydrolases; C070196:feruloyl esterase
keywords: Aspergillus niger; Ferulic acid; Feruloyl esterase; Pectin; Xylan