Relevant bibliographies by topics / Feruloil esterases

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Academic literature on the topic 'Feruloil esterases'

Author: Grafiati
Published: 10 September 2021
Last updated: 29 July 2025

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Journal articles on the topic "Feruloil esterases"

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Yu, P., J. J. McKinnon, and D. A. Christensen. "Hydroxycinnamic acids and ferulic acid esterase in relation to biodegradation of complex plant cell walls." Canadian Journal of Animal Science 85, no. 3 (2005): 255–67. http://dx.doi.org/10.4141/a04-010.

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Ferulic acid (3-methoxy-4-hydroxycinnamic acid), present in complex plant cell walls, is covalently cross-linked to polysaccharides by ester bonds and to components of lignin mainly by ether bonds. Ferulic acid has also been shown to occur in dimer- and trimerized forms through oxidative coupling between esterified and/or etherified ferulic acid residues. These cross-links are among the factors most inhibitory to digestion of complex plant cell walls in ruminants. Recently obtained information on ferulic acid and ferulic acid esterases in relation to complex plant cell wall biodegradation is r
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de Vries, Ronald P., and Jaap Visser. "Regulation of the Feruloyl Esterase (faeA) Gene from Aspergillus niger." Applied and Environmental Microbiology 65, no. 12 (1999): 5500–5503. http://dx.doi.org/10.1128/aem.65.12.5500-5503.1999.

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ABSTRACT Feruloyl esterases can remove aromatic residues (e.g., ferulic acid) from plant cell wall polysaccharides (xylan, pectin) and are essential for complete degradation of these polysaccharides. Expression of the feruloyl esterase-encoding gene (faeA) fromAspergillus niger depends on d-xylose (expression is mediated by XlnR, the xylanolytic transcriptional activator) and on a second system that responds to aromatic compounds with a defined ring structure, such as ferulic acid and vanillic acid. Several compounds were tested, and all of the inducing compounds contained a benzene ring which
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CREPIN, Valerie F., Craig B. FAULDS, and Ian F. CONNERTON. "A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition." Biochemical Journal 370, no. 2 (2003): 417–27. http://dx.doi.org/10.1042/bj20020917.

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Feruloyl esterases, a subclass of the carboxylic acid esterases (EC 3.1.1.1), are able to hydrolyse the ester bond between the hydroxycinnamic acids and sugars present in the plant cell wall. The enzymes have been classified as type A or type B, based on their substrate specificity for aromatic moieties. We show that Neurospora crassa has the ability to produce multiple ferulic acid esterase activities depending upon the length of fermentation with either sugar beet pulp or wheat bran substrates. A gene identified on the basis of its expression on sugar beet pulp has been cloned and overexpres
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Blum, David L., Irina A. Kataeva, Xin-Liang Li, and Lars G. Ljungdahl. "Feruloyl Esterase Activity of the Clostridium thermocellum Cellulosome Can Be Attributed to Previously Unknown Domains of XynY and XynZ." Journal of Bacteriology 182, no. 5 (2000): 1346–51. http://dx.doi.org/10.1128/jb.182.5.1346-1351.2000.

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ABSTRACT The cellulosome of Clostridium thermocellum is a multiprotein complex with endo- and exocellulase, xylanase, β-glucanase, and acetyl xylan esterase activities. XynY and XynZ, components of the cellulosome, are composed of several domains including xylanase domains and domains of unknown function (UDs). Database searches revealed that the C- and N-terminal UDs of XynY and XynZ, respectively, have sequence homology with the sequence of a feruloyl esterase of strain PC-2 of the anaerobic fungusOrpinomyces. Purified cellulosomes from C. thermocellum were found to hydrolyze FAXX (O-{5-O-[(
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Nieter, Annabel, Paul Haase-Aschoff, Sebastian Kelle, et al. "A Chlorogenic Acid Esterase with a Unique Substrate Specificity from Ustilago maydis." Applied and Environmental Microbiology 81, no. 5 (2014): 1679–88. http://dx.doi.org/10.1128/aem.02911-14.

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ABSTRACTAn extracellular chlorogenic acid esterase fromUstilago maydis(UmChlE) was purified to homogeneity by using three separation steps, including anion-exchange chromatography on a Q Sepharose FF column, preparative isoelectric focusing (IEF), and, finally, a combination of affinity chromatography and hydrophobic interaction chromatography on polyamide. SDS-PAGE analysis suggested a monomeric protein of ∼71 kDa. The purified enzyme showed maximal activity at pH 7.5 and at 37°C and was active over a wide pH range (3.5 to 9.5). Previously described chlorogenic acid esterases exhibited a comp
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Bouzid, Ourdia, Eric Record, Michèle Asther, et al. "Exploration of members ofAspergillussectionsNigri,Flavi, andTerreifor feruloyl esterase production." Canadian Journal of Microbiology 52, no. 9 (2006): 886–92. http://dx.doi.org/10.1139/w06-046.

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The ability of members of Aspergillus sections Nigri, Flavi, and Terrei to produce feruloyl esterases was studied according to their substrate specificity against synthetic methyl esters of hydroxycinnamic acids. Type A feruloyl esterases (FAEA), induced during growth on cereal-derived products, show a preference for the phenolic moiety of substrates that contain methoxy substitutions, as found in methyl sinapinate, whereas type B feruloyl esterases (FAEB) show a preference for the phenolic moiety of substrates that contain hydroxyl substitutions, as occurs in methyl caffeate. All the strains
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Williamson, G., C. B. Faulds, and P. A. Kroon. "Specificity of ferulic acid (feruloyl) esterases." Biochemical Society Transactions 26, no. 2 (1998): 205–10. http://dx.doi.org/10.1042/bst0260205.

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Kabel, Mirjam A., Carl J. Yeoman, Yejun Han, et al. "Biochemical Characterization and Relative Expression Levels of Multiple Carbohydrate Esterases of the Xylanolytic Rumen Bacterium Prevotella ruminicola 23 Grown on an Ester-Enriched Substrate." Applied and Environmental Microbiology 77, no. 16 (2011): 5671–81. http://dx.doi.org/10.1128/aem.05321-11.

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ABSTRACTWe measured expression and used biochemical characterization of multiple carbohydrate esterases by the xylanolytic rumen bacteriumPrevotella ruminicola23 grown on an ester-enriched substrate to gain insight into the carbohydrate esterase activities of this hemicellulolytic rumen bacterium. TheP. ruminicola23 genome contains 16 genes predicted to encode carbohydrate esterase activity, and based on microarray data, four of these were upregulated >2-fold at the transcriptional level during growth on an ester-enriched oligosaccharide (XOSFA,Ac) from corn relative to a nonesterified frac
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Wong, Dominic W. S., Victor J. Chan, and Hans Liao. "Hydrolysis of ferulic acids in corn fiber by a metagenomic feruloyl esterase." BioResources 16, no. 1 (2020): 825–34. http://dx.doi.org/10.15376/biores.16.1.825-834.

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A feruloyl esterase (FAE) gene was isolated from rumen microbial metagenome that consisted of 774 bp encoding 258 amino acid residues. The gene was subcloned into pET 32b vector, expressed in Escherichia. coli, and the enzyme was purified in active form. Homology modeling showed that the FAE contained the catalytic triad composed of Ser80-His236-Asp177, and a classical Gly-X-Ser-X-Gly nucleophile motif commonly found in esterases. Under optimum pH and temperature (pH 7.0, 40 °C), 1 nmole FAE catalyzed the release of 19.75 ± 0.24 µg ferulic acid (FA) from 100 mg corn fiber (CF) in 1 h, which re
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Esteban-Torres, María, Inés Reverón, José Miguel Mancheño, Blanca de las Rivas, and Rosario Muñoz. "Characterization of a Feruloyl Esterase from Lactobacillus plantarum." Applied and Environmental Microbiology 79, no. 17 (2013): 5130–36. http://dx.doi.org/10.1128/aem.01523-13.

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ABSTRACTLactobacillus plantarumis frequently found in the fermentation of plant-derived food products, where hydroxycinnamoyl esters are abundant.L. plantarumWCFS1 cultures were unable to hydrolyze hydroxycinnamoyl esters; however, cell extracts from the strain partially hydrolyze methyl ferulate and methylp-coumarate. In order to discover whether the protein Lp_0796 is the enzyme responsible for this hydrolytic activity, it was recombinantly overproduced and enzymatically characterized. Lp_0796 is an esterase that, among other substrates, is able to efficiently hydrolyze the four model substr
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Dissertations / Theses on the topic "Feruloil esterases"

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Lopes, Vânia Alexandra da Silva Cardoso. "High-Throughput production and characterization of Carbohydrate-Active enZYmes for animal nutrition." Doctoral thesis, Universidade de Lisboa, Faculdade de Medicina Veterinária, 2020. http://hdl.handle.net/10400.5/19760.

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Tese de Doutoramento em Ciências Veterinárias na especialidade Produção Animal<br>The biodegradation of plant cell wall (PCW) carbohydrates is performed by microbial enzymes that are generally referred to as CAZymes. In animal nutrition, it is now well established that the monogastric animals produce a limited repertoire of CAZymes and as such cannot use efficiently some dietary ingredients that sometimes display antinutritional properties. The dietary supplementation with exogenous CAZymes improves the nutritive value of diets and increases animal’s performance. In particular, this study demo
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Santos, Ana Paula Almeida dos. "Desenvolvimento de um método para a determinação da atividade de esterases usando material lignocelulósico como substrato." Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/97/97132/tde-07112014-154425/.

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As feruloil esterases são enzimas relevantes para o processo de hidrólise de materiais lignocelulósicos oriundos de gramíneas. Estas enzimas são tradicionalmente determinadas com o emprego de substratos sintéticos de baixa massa molar. Entretanto, as atividades determinadas a partir desses ensaios não se correlacionam adequadamente com a ação das enzimas em substratos complexos e insolúveis como os materiais lignocelulósicos. Neste sentido, o presente trabalho visou desenvolver um método apropriado para medir a atividade de feruloil esterases utilizando um material lignocelulósico como substra
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Braga, Cleiton Márcio Pinto. "Produção das enzimas acessórias feruloil esterase e xilanase por fungos filamentosos isolados da região amazônica e sua aplicação na hidrólise do bagaço de canade-açúcar." Universidade Federal de São Carlos, 2013. https://repositorio.ufscar.br/handle/ufscar/7038.

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Made available in DSpace on 2016-08-17T18:39:51Z (GMT). No. of bitstreams: 1 6317.pdf: 1890056 bytes, checksum: dc49c9c95213e912864488dff97a859c (MD5) Previous issue date: 2013-12-13<br>Financiadora de Estudos e Projetos<br>Xylanase and feruloyl esterase (FAE) are two enzymes of great importance for plant biomass decomposition. The hemicellulose, one of the biomass constituents, has a great structural variety, so that for its complete deconstruction, several groups of enzymes are required, including mainly xylanases. These enzymes act on the &#946;-1,4 glycosidic bonds between the xylose res
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Alves, Luana de Fátima. "Criação de uma enzima multifuncional feruloil esterase/acetil-xilano esterase por desenho racional." Universidade de São Paulo, 2016. http://www.teses.usp.br/teses/disponiveis/17/17131/tde-21072016-153003/.

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A parede celular das plantas inclui componentes polissacarídeos complexos, e a sacarificação destes polímeros necessita da ação de conjuntos de enzimas que atuem em sinergia. Enzimas podem formar complexos multi-enzimáticos que possuem mais de uma atividade catalítica derivada de domínios distintos de uma mesma cadeia polipeptídica. O objetivo deste trabalho foi construir uma enzima bifuncional com os domínios catalíticos: acetilxilano esterase (Axe) e feruloil esterase (Fae) para desconstrução de material lignocelulósico de cana-de-açúcar. Para isso, dois diferentes domínios catalíticos: acet
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Antonopoulou, Io. "Use of feruloyl esterases for chemoenzymatic synthesis of bioactive compounds." Licentiate thesis, Luleå tekniska universitet, Kemiteknik, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:ltu:diva-62836.

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Feruloyl esterases (FAEs, EC 3.1.1.73) represent a subclass of carboxylic acid esterases that under normal conditions catalyze the hydrolysis of the ester bond between hydroxycinnamic acids (ferulic acid, sinapic acid, caffeic acid, p-coumaric acid) and arabinose residues in plant cell walls. Based on their specificity towards monoferulates and diferulates, substitutions on the phenolic ring and on their amino acid sequence identity, they have been classified into four types (A-D). The use of FAEs as accessory enzymes for the degradation of lignocellulosic biomass and their synergism with othe
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Crepin, Valérie. "Ferulic acid esterases for effective processing of plant carbohydrates." Thesis, University of Nottingham, 2003. http://eprints.nottingham.ac.uk/28964/.

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Feruloyl esterases (E.C. 3.1.1.73), a subclass of the carboxylic acid esterases (E.C. 3.1.1.1), are able to hydrolyse the ester bond between the hydroxycinnamic acids and sugars present in the plant cell walls, and have been classified as Types A or B based on their substrate specificity for aromatic moieties. They constitute an interesting group of enzymes that have the potential for use over a broad range of applications in the agri-food industries. In order to expand the range of available enzymes, we have examined the production of feruloyl esterases by the filamentous fungi Talaromyces sl
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Rumbold, Karl 1973. "Isolation and properties of a feruloyl esterase from Aureobasidium pullulans and its mechanism in lignocellulose degradation." Thesis, Stellenbosch : Stellenbosch University, 2003. http://hdl.handle.net/10019.1/53480.

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Dissertation (PhD)--University of Stellenbosch, 2003.<br>ENGLISH ABSTRACT: The production, purification and functional characterisation of feruloyl esterase from Aureobasidium pullulans were set as the primary objectives of this study. A further objective was to investigate a possible co-operative effect with other selected lignocellulolytic enzymes on substrates relevant to industry. In a comprehensive review, feruloyl esterases from various micro-organisms were compared both functionally and with regard to their primary structure, where applicable. Feruloyl esterases show intriguing
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Aliwan, Fraj O. "Mechanism, structure and specificity of a feruloyl esterase from Aspergillus niger." Thesis, University of East Anglia, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267727.

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Castanares, Arantza. "Xylan-degrading enzymes from Penicillium pinophilum : purification and characterization of a feruloyl/ρ-coumaroylester esterase". Thesis, University of Aberdeen, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.314624.

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Growth of <i>Penicillium pinophilum</i> in solid state culture on oat straw and wheat bran mixtures was found suitable for the production of xylan-degrading enzymes. An extracellular phenolic acid esterase and a xylanase were purified to homogeneity by a combination of anion-exchange and hydrophobic interaction chromatography. The physicochemical properties and the mode of action of the esterase on various xylan polysaccharides were investigated. The esterase had an apparent molecular mass of 57 kDa by SDS-PAGE and an isoelectric pH of 4.6. The enzyme released ferulic and ρ-coumaric acid from
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Faulds, C. B. "Ferulic acid esterases from Aspergillus niger : their application in the biotransformation of agricultural residues." Thesis, University of East Anglia, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.338044.

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Book chapters on the topic "Feruloil esterases"

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Rumbold, Karl, Georg Gübitz, and Bernard A. Prior. "Microbial Feruloyl Esterases." In ACS Symposium Series. American Chemical Society, 2004. http://dx.doi.org/10.1021/bk-2004-0889.ch015.

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Diarsa, Meghna, and Akshaya Gupte. "New Insights into Feruloyl Esterase." In Sustainable Microbial Technologies for Valorization of Agro-Industrial Wastes. CRC Press, 2022. http://dx.doi.org/10.1201/9781003191247-8.

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Pinto, Cristabell. "Feruloyl Esterase: A Principal Biodegradative Enzyme." In Bioprospects of Coastal Eubacteria. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-12910-5_12.

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Katsimpouras, Constantinos, Io Antonopoulou, Paul Christakopoulos, and Evangelos Topakas. "Role and Applications of Feruloyl Esterases in Biomass Bioconversion." In Biofuel and Biorefinery Technologies. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-43679-1_5.

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Rumbold, Karl, Georg Gübitz, Karl-Heinz Robra, and Bernard Prior. "Influence of Growth Substrate and Free Ferulic Acid on the Production of Feruloyl Esterase byAureobasidium pullulans." In ACS Symposium Series. American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0855.ch015.

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Faulds, Craig B., Paul A. Kroon, Begoña Bartolomé, and Gary Williamson. "Hydrolysis of Hemicelluloses Using Combinations of Xylanases and Feruloyl Esterases." In Carbohydrate Biotechnology Protocols. Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-261-6_15.

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Knoshaug, Eric P., Michael J. Selig, John O. Baker, Stephen R. Decker, Michael E. Himmel, and William S. Adney. "Heterologous Expression of Two Ferulic Acid Esterases from Penicillium funiculosum." In Biotechnology for Fuels and Chemicals. Humana Press, 2007. http://dx.doi.org/10.1007/978-1-60327-526-2_22.

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Singh, Surabhi, Om Prakash Dwivedi, and Shashank Mishra. "Recent Development in Ferulic Acid Esterase for Industrial Production." In Bioprocessing for Biomolecules Production. John Wiley & Sons, Ltd, 2019. http://dx.doi.org/10.1002/9781119434436.ch17.

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Sánchez-González, Mónica, Allan Blanco-Gámez, Roberto Parra-Saldívar, Juan Carlos Mateos-Díaz, and María Isabel Estrada-Alvarado. "Study of New Feruloyl Esterases to Understand Lipase Evolution: The Case of Bacillus flexus." In Lipases and Phospholipases. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-600-5_3.

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Buanafina, Marcia M. de O., Tim Langdon, Barbara Hauck, Sue J. Dalton, and Phil Morris. "Manipulating the Phenolic Acid Content and Digestibility of Italian Ryegrass (Lolium multiflorum) by Vacuolar-Targeted Expression of a Fungal Ferulic Acid Esterase." In Twenty-Seventh Symposium on Biotechnology for Fuels and Chemicals. Humana Press, 2006. http://dx.doi.org/10.1007/978-1-59745-268-7_34.

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Conference papers on the topic "Feruloil esterases"

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Tarbouriech, Nicolas, Jose A. M. Prates, Simon J. Charnock, Carlos M. G. A. Fontes, Luis M. A. Ferreira, and Gideon J. Davies. "STRUCTURAL SPECIFICITY OF XYN10B FERULIC ACID ESTERASE DOMAIN FROM CLOSTRIDIUM THERMOCELLUM." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.764.

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