Browsing by Subject "Ferulic acid"

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  • Yilmaz-Turan, Secil; Jiménez-Quero, Amparo; Menzel, Carolin; Morais de Carvalho, Danila; Lindström, Mikael E.; Sevastyanova, Olena; Moriana, Rosana; Vilaplana, Francisco (2020)
    This study demonstrates the potential of feruloylated arabinoxylan (AX) from wheat bran for the preparation of bioactive barrier films with antioxidant properties. We have comprehensively evaluated the influence of the structural features and chemical acetylation of feruloylated AX extracted by subcritical water on their film properties, in comparison with alkaline extracted AX and a reference wheat endosperm AX. The degree of substitution (DS) of AX had a large influence on film formation, higher DS yielded better thermal and mechanical properties. The barrier properties of AX films were significantly enhanced by external plasticization by sorbitol. Chemical acetylation significantly improved the thermal stability but not the mechanical or barrier properties of the films. The presence of bound ferulic acid in feruloylated AX films resulted in higher antioxidant activity compared to external addition of free ferulic acid, which demonstrates their potential use in active packaging applications for the preservation of oxygen-sensitive foodstuff.
  • Dilokpimol, Adiphol; Mäkelä, Miia R; Aguilar-Pontes, Maria V; Benoit-Gelber, Isabelle; Hildén, Kristiina S.; de Vries, Ronald P (BioMed Central, 2016)
    Abstract Feruloyl esterases (FAEs) represent a diverse group of carboxyl esterases that specifically catalyze the hydrolysis of ester bonds between ferulic (hydroxycinnamic) acid and plant cell wall polysaccharides. Therefore, FAEs act as accessory enzymes to assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass conversion. Their ability to release ferulic acid and other hydroxycinnamic acids from plant biomass makes FAEs potential biocatalysts in a wide variety of applications such as in biofuel, food and feed, pulp and paper, cosmetics, and pharmaceutical industries. This review provides an updated overview of the knowledge on fungal FAEs, in particular describing their role in plant biomass degradation, diversity of their biochemical properties and substrate specificities, their regulation and conditions needed for their induction. Furthermore, the discovery of new FAEs using genome mining and phylogenetic analysis of current publicly accessible fungal genomes will also be presented. This has led to a new subfamily classification of fungal FAEs that takes into account both phylogeny and substrate specificity.
  • Dilokpimol, Adiphol; Mäkelä, Miia R.; Mansouri, Sadegh; Belova, Olga; Waterstraat, Martin; Bunzel, Mirko; de Vries, Ronald P.; Hilden, Kristiina S. (2017)
    A feruloyl esterase (FAE) from Aspergillus niger N402, FaeC was heterologously produced in Pichia pastoris X-33 in a yield of 10 mg/L. FaeC was most active at pH 7.0 and 50 degrees 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 3 mg/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. (C) 2017 Elsevier B.V. All rights reserved.
  • Dilokpimol, Adiphol; Mäkelä, Miia Riitta; Varriale, Simona; Zhou, Miaomiao; Cerullo, Gabriella; Gidijala, Loknath; Hinkka, Harri Tapio; Brás, Joana L.A.; Jütten, Peter; Piechot, Alexander; Verhaert, Raymond; Hilden, Sari Kristiina; Faraco, Vincenza; de Vries, Ronald (2018)
    Feruloyl esterases (FAEs) are a diverse group of enzymes that specifically catalyze the hydrolysis of ester bonds between a hydroxycinnamic (e.g. ferulic) acid and plant poly- or oligosaccharides. FAEs as auxiliary enzymes significantly assist xylanolytic and pectinolytic enzymes in gaining access to their site of action during biomass saccharification for biofuel and biochemical production. A limited number of FAEs have been functionally characterized compared to over 1000 putative fungal FAEs that were recently predicted by similarity-based genome mining, which divided phylogenetically into different subfamilies (SFs). In this study, 27 putative and six characterized FAEs from both ascomycete and basidiomycete fungi were selected and heterologously expressed in Pichia pastoris and the recombinant proteins biochemically characterized to validate the previous genome mining and phylogenetical grouping and to expand the information on activity of fungal FAEs. As a result, 20 enzymes were shown to possess FAE activity, being active towards pNP-ferulate and/or methyl hydroxycinnamate substrates, and covering 11 subfamilies. Most of the new FAEs showed activities comparable to those of previously characterized fungal FAEs.
  • Lubbers, Ronnie J. M.; Dilokpimol, Adiphol; Nousiainen, Paula A.; Cioc, Razvan C.; Visser, Jaap; Bruijnincx, Pieter C. A.; de Vries, Ronald P. (2021)
    Background The aromatic compounds vanillin and vanillic acid are important fragrances used in the food, beverage, cosmetic and pharmaceutical industries. Currently, most aromatic compounds used in products are chemically synthesized, while only a small percentage is extracted from natural sources. The metabolism of vanillin and vanillic acid has been studied for decades in microorganisms and many studies have been conducted that showed that both can be produced from ferulic acid using bacteria. In contrast, the degradation of vanillin and vanillic acid by fungi is poorly studied and no genes involved in this metabolic pathway have been identified. In this study, we aimed to clarify this metabolic pathway in Aspergillus niger and identify the genes involved. Results Using whole-genome transcriptome data, four genes involved in vanillin and vanillic acid metabolism were identified. These include vanillin dehydrogenase (vdhA), vanillic acid hydroxylase (vhyA), and two genes encoding novel enzymes, which function as methoxyhydroquinone 1,2-dioxygenase (mhdA) and 4-oxo-monomethyl adipate esterase (omeA). Deletion of these genes in A. niger confirmed their role in aromatic metabolism and the enzymatic activities of these enzymes were verified. In addition, we demonstrated that mhdA and vhyA deletion mutants can be used as fungal cell factories for the accumulation of vanillic acid and methoxyhydroquinone from guaiacyl lignin units and related aromatic compounds. Conclusions This study provides new insights into the fungal aromatic metabolic pathways involved in the degradation of guaiacyl units and related aromatic compounds. The identification of the involved genes unlocks new potential for engineering aromatic compound-producing fungal cell factories.