ArticleThe Biochemical journal2002
The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 144 citations in OpenAlex.
- Fantastic Ferulic Acid Esterases and Their Functions.International journal of molecular sciences · 2025Review
- An Updated Perspective on the Aromatic Metabolic Pathways of Plant-Derived Homocyclic Aromatic Compounds inMicroorganisms · 2025Review
- The bZIP transcription factor BIP1 of the rice blast fungus is essential for infection and regulates a specific set of appressorium genes.PLoS pathogens · 2024Article
- Effects of Fermentation on Bioactivity and the Composition of Polyphenols Contained in Polyphenol-Rich Foods: A Review.Foods (Basel, Switzerland) · 2023Review
- Feruloyl esterase Fae1 is required specifically for host colonisation by the rice-blast fungus Magnaporthe oryzae.Current genetics · 2022Article
- Utilization of ferulic acid inFrontiers in fungal biology · 2022Article
- CreA-mediated repression of gene expression occurs at low monosaccharide levels during fungal plant biomass conversion in a time and substrate dependent manner.Cell surface (Amsterdam, Netherlands) · 2021Article
- Loss of function of the carbon catabolite repressor CreA leads to low but inducer-independent expression from the feruloyl esterase B promoter in Aspergillus niger.Biotechnology letters · 2021Article
- Production of Protocatechuic Acid frommBio · 2021Article
- Evolutionary adaptation of Aspergillus niger for increased ferulic acid tolerance.Journal of applied microbiology · 2020Article
- Does glucose affect the de-esterification of methyl ferulate by Lactobacillus buchneri?MicrobiologyOpen · 2020Article
- Feruloyl Esterases for Biorefineries: Subfamily Classified Specificity for Natural Substrates.Frontiers in bioengineering and biotechnology · 2020Article
- Article
- Genomic analyses of Burkholderia cenocepacia reveal multiple species with differential host-adaptation to plants and humans.BMC genomics · 2019Article
- Cinnamic Acid and Sorbic acid Conversion Are Mediated by the Same Transcriptional Regulator inFrontiers in bioengineering and biotechnology · 2019Article
- Characterization of a feruloyl esterase from Aspergillus terreus facilitates the division of fungal enzymes from Carbohydrate Esterase family 1 of the carbohydrate-active enzymes (CAZy) database.Microbial biotechnology · 2018Article
- The fungus Aspergillus niger consumes sugars in a sequential manner that is not mediated by the carbon catabolite repressor CreA.Scientific reports · 2018Article
- Article
- The MADS-box Transcription Factor PsMAD1 Is Involved in Zoosporogenesis and Pathogenesis ofFrontiers in microbiology · 2018Article
- Expression-based clustering of CAZyme-encoding genes of Aspergillus niger.BMC genomics · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The faeB gene encoding a second feruloyl esterase from Aspergillus niger has been cloned and characterized. It consists of an open reading frame of 1644 bp containing one intron. The gene encodes a protein of 521 amino acids that has sequence similarity to that of an Aspergillus oryzae tannase. However, the encoded enzyme, feruloyl esterase B (FAEB), does not have tannase activity. Comparison of the physical characteristics and substrate specificity of FAEB with those of a cinnamoyl esterase from A. niger [Kroon, Faulds and Williamson (1996) Biotechnol. Appl. Biochem. 23, 255-262] suggests that they are in fact the same enzyme. The expression of faeB is specifically induced in the presence of certain aromatic compounds, but not in the presence of other constituents present in plant-cell-wall polysaccharides such as arabinoxylan or pectin. The expression profile of faeB in the presence of aromatic compounds was compared with the expression of A. niger faeA, encoding feruloyl esterase A (FAEA), and A. niger bphA, the gene encoding a benzoate-p-hydroxylase. All three genes have different subsets of aromatic compounds that induce their expression, indicating the presence of different transcription activating systems in A. niger that respond to aromatic compounds. Comparison of the activity of FAEA and FAEB on sugar-beet pectin and wheat arabinoxylan demonstrated that they are both involved in the degradation of both polysaccharides, but have opposite preferences for these substrates. FAEA is more active than FAEB towards wheat arabinoxylan, whereas FAEB is more active than FAEA towards sugar-beet pectin.
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