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Journal articles on the topic 'Feruloil esterases'

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Published: 10 September 2021

Last updated: 29 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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8

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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9

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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10

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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Bäumker, P. A., S. Arendt, and R. Wiermann. "Metabolism of Ferulic Acid Sucrose Esters in Anthers of Tulipa cv. Apeldoorn: II. Highly Specific Degradation of the Esters by Different Esterase Activities." Zeitschrift für Naturforschung C 43, no. 9-10 (1988): 647–55. http://dx.doi.org/10.1515/znc-1988-9-1005.

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Abstract Protein extracts from anthers of Tulipa cv. Apeldoorn catalyze the degradation of ferulic acid sucrose esters. Different products are generated when triferuloyl sucrose (TFS) and diferuloyl sucrose (DFS) were applied as substrates. By the aid of reversed-phase HPLC , TLC and spectroscopy the products could be identified as free ferulic acid, monoferuloyl sucrose ester [feruloylsucrose(mono)] and two different diesters of ferulic acid and sucrose [feruloylsucrose(di) and the endogenously occurring diferuloylsucrose (DFS)]. By means of protein fractionation (chromatofocusing, anion exch

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12

Yang, Sheng, Miaofang Lin, Jiyang Chen, Min Liu, and Qi Chen. "Engineering of an Alkaline Feruloyl Esterase PhFAE for Enhanced Thermal Stability and Catalytic Efficiency Through Molecular Dynamics and FireProt." Catalysts 15, no. 1 (2025): 92. https://doi.org/10.3390/catal15010092.

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Feruloyl esterases (FAEs) play critical roles in industrial applications such as food processing, pharmaceuticals, and paper production by breaking down plant cell walls and releasing ferulic acid. However, most bacterial FAEs function optimally in acidic environments, limiting their use in alkaline industrial processes. Additionally, FAEs with alkaline activity often lack the thermal stability required for demanding industrial conditions. In this study, an alkaline feruloyl esterase, PhFAE, from Pandoraea horticolens was identified that exhibits high catalytic activity but suffers from therma

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13

Li, Jiabao, Shichun Cai, Yuanming Luo, and Xiuzhu Dong. "Three Feruloyl Esterases in Cellulosilyticum ruminicola H1 Act Synergistically To Hydrolyze Esterified Polysaccharides." Applied and Environmental Microbiology 77, no. 17 (2011): 6141–47. http://dx.doi.org/10.1128/aem.00657-11.

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ABSTRACTFeruloyl esterases (Faes) constitute a subclass of carboxyl esterases that specifically hydrolyze the ester linkages between ferulate and polysaccharides in plant cell walls. Until now, the described microbial Faes were mainly from fungi. In this study, we report thatCellulosilyticum ruminicolaH1, a previously described fibrolytic rumen bacterium, possesses three different active feruloyl esterases, FaeI, FaeII, and FaeIII. Phylogenetic analysis classified the described bacterial Faes into two types, FaeI and FaeII in type I and FaeIII in type II. Substrate specificity assays indicated

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14

Holck, Jesper, Folmer Fredslund, Marie S. Møller, et al. "A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan." Journal of Biological Chemistry 294, no. 46 (2019): 17339–53. http://dx.doi.org/10.1074/jbc.ra119.009523.

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Feruloyl esterases (EC 3.1.1.73), belonging to carbohydrate esterase family 1 (CE1), hydrolyze ester bonds between ferulic acid (FA) and arabinose moieties in arabinoxylans. Recently, some CE1 enzymes identified in metagenomics studies have been predicted to contain a family 48 carbohydrate-binding module (CBM48), a CBM family associated with starch binding. Two of these CE1s, wastewater treatment sludge (wts) Fae1A and wtsFae1B isolated from wastewater treatment surplus sludge, have a cognate CBM48 domain and are feruloyl esterases, and wtsFae1A binds arabinoxylan. Here, we show that wtsFae1B

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15

Nghi, Do Huu, Britta Bittner, Harald Kellner та ін. "The Wood Rot Ascomycete Xylaria polymorpha Produces a Novel GH78 Glycoside Hydrolase That Exhibits α-l-Rhamnosidase and Feruloyl Esterase Activities and Releases Hydroxycinnamic Acids from Lignocelluloses". Applied and Environmental Microbiology 78, № 14 (2012): 4893–901. http://dx.doi.org/10.1128/aem.07588-11.

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ABSTRACTSoft rot (type II) fungi belonging to the family Xylariaceae are known to substantially degrade hardwood by means of their poorly understood lignocellulolytic system, which comprises various hydrolases, including feruloyl esterases and laccase. In the present study, several members of the Xylariaceae were found to exhibit high feruloyl esterase activity during growth on lignocellulosic materials such as wheat straw (up to 1,675 mU g−1) or beech wood (up to 80 mU g−1). Following the ester-cleaving activity toward methyl ferulate, a hydrolase ofXylaria polymorphawas produced in solid-sta

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16

Hassan, S., and N. Hugouvieux-Cotte-Pattat. "Identification of Two Feruloyl Esterases in Dickeya dadantii 3937 and Induction of the Major Feruloyl Esterase and of Pectate Lyases by Ferulic Acid." Journal of Bacteriology 193, no. 4 (2010): 963–70. http://dx.doi.org/10.1128/jb.01239-10.

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17

Gherbovet, Olga, Fernando Ferreira, Apolline Clément, et al. "Regioselective chemoenzymatic syntheses of ferulate conjugates as chromogenic substrates for feruloyl esterases." Beilstein Journal of Organic Chemistry 17 (February 1, 2021): 325–33. http://dx.doi.org/10.3762/bjoc.17.30.

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Generally, carbohydrate-active enzymes are studied using chromogenic substrates that provide quick and easy color-based detection of enzyme-mediated hydrolysis. For feruloyl esterases, commercially available chromogenic ferulate derivatives are both costly and limited in terms of their experimental application. In this study, we describe solutions for these two issues, using a chemoenzymatic approach to synthesize different ferulate compounds. The overall synthetic routes towards commercially available 5-bromo-4-chloro-3-indolyl and 4-nitrophenyl 5-O-feruloyl-α-ʟ-arabinofuranosides were signif

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18

Chen, Shang-ke, Kui Wang, Yuhuan Liu, and Xiaopeng Hu. "Crystallization and preliminary X-ray analysis of a novel halotolerant feruloyl esterase identified from a soil metagenomic library." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 7 (2012): 767–70. http://dx.doi.org/10.1107/s1744309112017812.

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Feruloyl esterase cleaves the ester linkage formed between ferulic acid and polysaccharides in plant cell walls and thus has wide potential industrial applications. A novel feruloyl esterase (EstF27) identified from a soil metagenomic library was crystallized and a complete data set was collected from a single cooled crystal using an in-house X-ray source. The crystal diffracted to 2.9 Å resolution and belonged to space groupP212121, with unit-cell parametersa= 94.35,b= 106.19,c= 188.51 Å, α = β = γ = 90.00°. A Matthews coefficient of 2.55 Å3 Da−1, with a corresponding solvent content of 51.84

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19

Sun, Alberto, Craig B. Faulds, and Charles W. Bamforth. "Barley Contains Two Cationic Acetylxylan Esterases and One Anionic Feruloyl Esterase." Cereal Chemistry Journal 82, no. 6 (2005): 621–25. http://dx.doi.org/10.1094/cc-82-0621.

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20

Perez-Garcia, Pablo, Jennifer Chow, Elisa Costanzi, et al. "An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate." Communications Chemistry 6 (September 11, 2023): 193. https://doi.org/10.1038/s42004-023-00998-z.

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Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 80 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme had been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46 (RLI42440.1), an archaeal promiscuous feruloyl esterase exhibiting degradation activity on semi-crystalline PET powder comparable to IsPETase and LCC (wildtypes), and higher activity on bis-, and mono-(

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Dilokpimol, Adiphol, Miia R. Mäkelä, Maria Victoria Aguilar-Pontes, Isabelle Benoit-Gelber, Kristiina S. Hildén, and Vries Ronald P. de. "Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications." Biotechnology for Biofuels 9, no. 1 (2016): 231. https://doi.org/10.1186/s13068-016-0651-6.

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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 pharmaceutica

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Yu, P., J. J. McKinnon, D. D. Maenz, V. J. Racz, and D. A. Christensen. "The interactive effects of enriched sources of Aspergillus ferulic acid esterase and Trichoderma xylanase on the quantitative release of hydroxycinnamic acids from oat hulls." Canadian Journal of Animal Science 82, no. 2 (2002): 251–57. http://dx.doi.org/10.4141/a01-035.

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Oat hulls contain relatively high amounts of hydroxycinnamic acids, mainly ferulic (4-hydroxy-3-methoxycinnamic) and p-coumaric acids (4-hydroxy-cinnamic), which are inhibitory to cell wall biodegradability by rumen microorganisms. In this paper, a study of the interactive effects of enriched sources of Aspergillus ferulic acid esterase (A-FAE) and Trichoderma xylanase (T-XYL) at different levels on the quantitative release of ferulic acid and p-coumaric acid from oat hulls was carried out. The results show that relative to A-FAE alone, the combined action of A-FAE and T-XYL was superior in ca

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23

Gubler, F., and AE Ashford. "Release of Ferulic Acid Esters From Barley Aleurone. I. Time Course of Gibberellic-Acid-Induced Release From Isolated Layers." Functional Plant Biology 12, no. 3 (1985): 297. http://dx.doi.org/10.1071/pp9850297.

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Removal of ferulic acid from barley aleurone cell walls is closely correlated with wall hydrolysis. The ferulic acid content of isolated aleurone layers (Hordeum vulgare L. cv. Himalaya) falls progressively during incubation with gibberellic acid (GA3), to about one-third of the original content, by 72 h. At the same time an equivalent amount accumulates in the incubation medium, not as the free acid but still esterified to other components. The data show that there is no modification of the feruloyl group, or hydrolysis of the ester linkage prior to removal from the tissue, and therefore the

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PA, Kroon, and G. Williamson. "Release of ferulic acid from sugar‐beet pulp by using arabinanase, arabinofuranosidase and an esterase from Aspergillus niger." Biotechnology and Applied Biochemistry 23, no. 3 (1996): 263–67. http://dx.doi.org/10.1111/j.1470-8744.1996.tb00382.x.

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Aspergillus niger cinnamoyl esterase (CinnAE) is shown to be active towards a wide range of feruloylated oligosaccharides derived from sugar‐beet pulp (SBP). The esterase hydrolysed ferulic acid ester‐linked to either C‐2 of arabinose or C‐6 of galactose residues, and demonstrated the highest activity towards the feruloylated arabinose trisaccharide. However, CinnAE was able to release only 0.88% of total alkali‐extractable ferulic acid from SBP in 24 h when acting alone. To determine whether cell‐wall‐degrading enzymes could increase the release of ferulic acid by CinnAE, SBP was incubated wi

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Kroon, PA, MT Garcia-Conesa, IJ Fillingham, GP Hazlewood, and G. Williamson. "Release of ferulic acid dehydrodimers from plant cell walls by feruloyl esterases." Journal of the Science of Food and Agriculture 79, no. 3 (1999): 428–34. http://dx.doi.org/10.1002/(sici)1097-0010(19990301)79:3<428::aid-jsfa275>3.0.co;2-j.

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Watanabe, Masahiro, and Kazuhiko Ishikawa. "Crystallization and preliminary X-ray crystallographic analysis of a putative feruloyl esterase fromTalaromyces cellulolyticus." Acta Crystallographica Section F Structural Biology Communications 70, no. 12 (2014): 1664–67. http://dx.doi.org/10.1107/s2053230x14024650.

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Feruloyl esterase (FAE; EC 3.1.1.73) catalyzes the cleavage of the ester bond between ferulic acid and polysaccharides in plant cell walls, and thus holds significant potential for the industrial utilization of biomass saccharification. A feruloyl esterase was identified from the genome database ofTalaromyces cellulolyticus(formerly known asAcremonium cellulolyticus). The gene consists of the catalytic domain and a carbohydrate-binding module connected through a serine/threonine-rich linker region. The recombinant enzyme was prepared, purified and crystallized at 293 K using 0.1 Mimidazole pH

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Kaur, Baljinder, Debkumar Chakraborty, and Balvir Kumar. "Phenolic Biotransformations during Conversion of Ferulic Acid to Vanillin by Lactic Acid Bacteria." BioMed Research International 2013 (2013): 1–6. http://dx.doi.org/10.1155/2013/590359.

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Vanillin is widely used as food additive and as a masking agent in various pharmaceutical formulations. Ferulic acid is an important precursor of vanillin that is available in abundance in cell walls of cereals like wheat, corn, and rice. Phenolic biotransformations can occur during growth of lactic acid bacteria (LAB), and their production can be made feasible using specialized LAB strains that have been reported to produce ferulic acid esterases. The present study aimed at screening a panel of LAB isolates for their ability to release phenolics from agrowaste materials like rice bran and the

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Laszlo, Joseph A., David L. Compton, and Xin-Liang Li. "Feruloyl esterase hydrolysis and recovery of ferulic acid from jojoba meal." Industrial Crops and Products 23, no. 1 (2006): 46–53. http://dx.doi.org/10.1016/j.indcrop.2005.03.005.

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Palani Swamy, Sakthi kumaran, and Vijayalakshmi Govindaswamy. "Therapeutical properties of ferulic acid and bioavailability enhancement through feruloyl esterase." Journal of Functional Foods 17 (August 2015): 657–66. http://dx.doi.org/10.1016/j.jff.2015.06.013.

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Zerva, Anastasia, Io Antonopoulou, Josefine Enman, et al. "Optimization of Transesterification Reactions with CLEA-Immobilized Feruloyl Esterases from Thermothelomyces thermophila and Talaromyces wortmannii." Molecules 23, no. 9 (2018): 2403. http://dx.doi.org/10.3390/molecules23092403.

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Feruloyl esterases (FAEs, E.C. 3.1.1.73) are biotechnologically important enzymes with several applications in ferulic acid production from biomass, but also in synthesis of hydroxycinnamic acid derivatives. The use of such biocatalysts in commercial processes can become feasible by their immobilization, providing the advantages of isolation and recycling. In this work, eight feruloyl esterases, immobilized in cross-linked enzyme aggregates (CLEAs) were tested in regard to their transesterification performance, towards the production of prenyl ferulate (PFA) and arabinose ferulate (AFA). After

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Marquez-Escalante, Jorge A., and Elizabeth Carvajal-Millan. "Feruloylated Arabinoxylans from Maize Distiller’s Dried Grains with Solubles: Effect of Feruloyl Esterase on their Macromolecular Characteristics, Gelling, and Antioxidant Properties." Sustainability 11, no. 22 (2019): 6449. http://dx.doi.org/10.3390/su11226449.

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Distiller’s dried grains with solubles (DDGS) are co-products of the maize ethanol industry. DDGS contains feruloylated arabinoxylans (AXs), which can present gelling, antioxidant, and health-promoting effects. However, AXs presenting high ferulic acid (FA) content can exhibit delayed fermentation by the colonic microbiota. Therefore, partial deferuloylation of AXs from DDGS while preserving the polysaccharide gelling and antioxidant properties could add value and favor the sustainable development of bioethanol plants. The aim of this work was to partially deferuloylated AXs from DDGS using fe

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Faulds, Craig B., Ronald P. DeVries, Paul A. Kroon, Jaap Visser, and Gary Williamson. "Influence of ferulic acid on the production of feruloyl esterases by Aspergillus niger." FEMS Microbiology Letters 157, no. 2 (2006): 239–44. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12779.x.

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Cai, Shichun, Jiabao Li, Fen Ze Hu, et al. "Cellulosilyticum ruminicola, a Newly Described Rumen Bacterium That Possesses Redundant Fibrolytic-Protein-Encoding Genes and Degrades Lignocellulose with Multiple Carbohydrate- Borne Fibrolytic Enzymes." Applied and Environmental Microbiology 76, no. 12 (2010): 3818–24. http://dx.doi.org/10.1128/aem.03124-09.

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ABSTRACT Cellulosilyticum ruminicola H1 is a newly described bacterium isolated from yak (Bos grunniens) rumen and is characterized by its ability to grow on a variety of hemicelluloses and degrade cellulosic materials. In this study, we performed the whole-genome sequencing of C. ruminicola H1 and observed a comprehensive set of genes encoding the enzymes essential for hydrolyzing plant cell wall. The corresponding enzymatic activities were also determined in strain H1; these included endoglucanases, cellobiohydrolases, xylanases, mannanase, pectinases, and feruloyl esterases and acetyl ester

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Abokitse, Kofi, Meiqun Wu, Hélène Bergeron, Stephan Grosse, and Peter C. K. Lau. "Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran." Applied Microbiology and Biotechnology 87, no. 1 (2010): 195–203. http://dx.doi.org/10.1007/s00253-010-2441-6.

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Yang, Zhihong, Guangzhuang Li, and Yunhua Hou. "Application of Feruloyl Esterase in Wheat Straw Pulp Bleaching." Highlights in Science, Engineering and Technology 66 (September 20, 2023): 197–200. http://dx.doi.org/10.54097/hset.v66i.11700.

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The pulp made from wheat straw fiber contains considerable natural cellulose, but there are more carbohydrate-ferulic acid ester-lignin cross-linking structure in the pulp. this cross-linking structure seriously hinders the recognition and binding of hemicellulase and substrate, thus affecting the efficiency of hemicellulose degradation. Feruloyl esterase, as one of hemicellulose degradation enzymes, can hydrolyze hemicellulose side chain branches. Make the plant grid structure loose, it is more important that it can enhance the accessibility of xylanase to the xylan trunk. Therefore, it is of

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Marmuse, Laurence, Michèle Asther, David Navarro, et al. "Chromogenic substrates for feruloyl esterases." Carbohydrate Research 342, no. 15 (2007): 2316–21. http://dx.doi.org/10.1016/j.carres.2007.06.004.

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C., Faulds, Sancho A., and Bartolomé B. "Mono- and dimeric ferulic acid release from brewer's spent grain by fungal feruloyl esterases." Applied Microbiology and Biotechnology 60, no. 4 (2002): 489–94. http://dx.doi.org/10.1007/s00253-002-1140-3.

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Ohlhoff, Colin W., Bronwyn M. Kirby, Leonardo Van Zyl, et al. "An unusual feruloyl esterase belonging to family VIII esterases and displaying a broad substrate range." Journal of Molecular Catalysis B: Enzymatic 118 (August 2015): 79–88. http://dx.doi.org/10.1016/j.molcatb.2015.04.010.

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Giannakopoulou, Archontoula, Georgia Tsapara, Anastassios N. Troganis, et al. "Development of a Multi-Enzymatic Approach for the Modification of Biopolymers with Ferulic Acid." Biomolecules 12, no. 7 (2022): 992. http://dx.doi.org/10.3390/biom12070992.

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A series of polymers, including chitosan (CS), carboxymethylcellulose (CMC) and a chitosan–gelatin (CS–GEL) hybrid polymer, were functionalized with ferulic acid (FA) derived from the enzymatic treatment of arabinoxylan through the synergistic action of two enzymes, namely, xylanase and feruloyl esterase. Subsequently, the ferulic acid served as the substrate for laccase from Agaricus bisporus (AbL) in order to enzymatically functionalize the above-mentioned polymers. The successful grafting of the oxidized ferulic acid products onto the different polymers was confirmed through ultraviolet–vis

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Zhang, Yao, Zhiping Feng, Hongzhu Xiang, Xian Zhang, and Lijuan Yang. "Characterization of Feruloyl Esterase from Klebsiella oxytoca Z28 and Its Application in the Release of Ferulic Acid from De-Starching Wheat Bran." Microorganisms 11, no. 4 (2023): 989. http://dx.doi.org/10.3390/microorganisms11040989.

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Feruloyl esterase (EC3.1.1.73; FAE) can degrade biomass to release ferulic acid (FA), which has a high application in bioprocessing, food, pharmaceutical, paper, feed, and other industrial fields. A strain of Klebsiella oxytoca Z28 with ferulic esterase activity was screened from Daqu. In addition, the FAE gene was expressed in Escherichia coli BL21 (DE3). The enzyme consists of 340 amino acids with a molecular mass of 37.7 kDa. The FAE enzyme activity was 463 U/L when the substrate was ethyl 4-hydroxy-3-methoxycinnamate and the optimum temperature and pH were 50 °C and 8.0, respectively. The

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He, Fuming, Song Zhang, and Xinli Liu. "Immobilization of feruloyl esterases on magnetic nanoparticles and its potential in production of ferulic acid." Journal of Bioscience and Bioengineering 120, no. 3 (2015): 330–34. http://dx.doi.org/10.1016/j.jbiosc.2015.01.006.

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Zhang, Jing, Shuangping Liu, Hailong Sun, et al. "Enzyme Production Potential of Penicillium oxalicum M1816 and Its Application in Ferulic Acid Production." Foods 10, no. 11 (2021): 2577. http://dx.doi.org/10.3390/foods10112577.

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The present study focused on isolating an efficient enzyme production microorganism for ferulic acid (FA) production from wheat bran. A wild-type cellulase-, xylanase-, and feruloyl esterase-producing strain was isolated and identified as Penicillium oxalicum M1816. The genome was sequenced and assembled into 30.5 Mb containing 8301 predicted protein-coding genes. In total, 553 genes were associated with carbohydrate metabolism. Genomic CAZymes analysis indicated that P. oxalicum M1816, comprising 39 cellulolytic enzymes and 111 hemicellulases (including 5 feruloyl esterase genes), may play a

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De Anda-Flores, Yubia, Elizabeth Carvajal-Millan, Jaime Lizardi-Mendoza, et al. "Conformational Behavior, Topographical Features, and Antioxidant Activity of Partly De-Esterified Arabinoxylans." Polymers 13, no. 16 (2021): 2794. http://dx.doi.org/10.3390/polym13162794.

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This study aimed to investigate the effect of arabinoxylans (AX) partial de-esterification with feruloyl esterase on the polysaccharide conformational behavior, topographical features, and antioxidant activity. After enzyme treatment, the ferulic acid (FA) content in AX was reduced from 7.30 to 5.48 µg FA/mg polysaccharide, and the molecule registered a small reduction in radius of gyration (RG), hydrodynamic radius (Rh), characteristic ratio (C∞), and persistence length (q). A slight decrease in α and a small increase in K constants in the Mark–Houwink–Sakurada equation for partially de-ester

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Jeon, Sangeun, Jisub Hwang, Hackwon Do, et al. "Feruloyl Esterase (LaFae) from Lactobacillus acidophilus: Structural Insights and Functional Characterization for Application in Ferulic Acid Production." International Journal of Molecular Sciences 24, no. 13 (2023): 11170. http://dx.doi.org/10.3390/ijms241311170.

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Ferulic acid and related hydroxycinnamic acids, used as antioxidants and preservatives in the food, cosmetic, pharmaceutical and biotechnology industries, are among the most abundant phenolic compounds present in plant biomass. Identification of novel compounds that can produce ferulic acid and hydroxycinnamic acids, that are safe and can be mass-produced, is critical for the sustainability of these industries. In this study, we aimed to obtain and characterize a feruloyl esterase (LaFae) from Lactobacillus acidophilus. Our results demonstrated that LaFae reacts with ethyl ferulate and can be

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Faulds, Craig B., Ronald de Vries, Jaap Visser, and Gary Williamson. "Stability of feruloyl esterases from Aspergillus." Biochemical Society Transactions 26, no. 2 (1998): S165. http://dx.doi.org/10.1042/bst026s165.

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Mastihuba, Vladimı́r, Lubomı́r Kremnický, Mária Mastihubová, J. L. Willett, and Gregory L. Côté. "A spectrophotometric assay for feruloyl esterases." Analytical Biochemistry 309, no. 1 (2002): 96–101. http://dx.doi.org/10.1016/s0003-2697(02)00241-5.

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Marmuse, Laurence, Michèle Asther, Emeline Fabre, et al. "New chromogenic substrates for feruloyl esterases." Organic & Biomolecular Chemistry 6, no. 7 (2008): 1208. http://dx.doi.org/10.1039/b717742a.

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Wang, Xiaokun, Xin Geng, Yukari Egashira, and Hiroo Sanada. "Purification and Characterization of a Feruloyl Esterase from the Intestinal Bacterium Lactobacillus acidophilus." Applied and Environmental Microbiology 70, no. 4 (2004): 2367–72. http://dx.doi.org/10.1128/aem.70.4.2367-2372.2004.

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ABSTRACT Dietary ferulic acid (FA), a significant antioxidant substance, is currently the subject of extensive research. FA in cereals exists mainly as feruloylated sugar ester. To release FA from food matrices, it is necessary to cleave ester cross-linking by feruloyl esterase (FAE) (hydroxycinnamoyl esterase; EC 3.1.1.73). In the present study, the FAE from a human typical intestinal bacterium, Lactobacillus acidophilus, was isolated, purified, and characterized for the first time. The enzyme was purified in successive steps including hydrophobic interaction chromatography and anion-exchange

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Mukdsi, M. C. Abeijón, E. Argañaraz Martínez, A. Perez Chaia, and R. B. Medina. "Feruloyl esterase activity is influenced by bile, probiotic intestinal adhesion and milk fat." Beneficial Microbes 7, no. 4 (2016): 597–607. http://dx.doi.org/10.3920/bm2015.0197.

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Cinnamoyl esterases (CE) are microbial and mammalian intestinal enzymes able to release antioxidant hydroxycinnamic acids from their non-digestible ester-linked forms naturally present in vegetable foods. Previous findings showed that oral administration of Lactobacillus fermentum CRL1446 increased intestinal CE activity and improved oxidative status in mice. The aim of this work was to evaluate the in vitro CE activity of L. fermentum CRL1446 and the effect of bile on this activity, as well as strain resistance to simulated gastrointestinal tract (GIT) conditions and its ability to adhere to

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Liu, Siqing, Kenneth M. Bischoff, Amber M. Anderson, and Joseph O. Rich. "Novel Feruloyl Esterase from Lactobacillus fermentum NRRL B-1932 and Analysis of the Recombinant Enzyme Produced in Escherichia coli." Applied and Environmental Microbiology 82, no. 17 (2016): 5068–76. http://dx.doi.org/10.1128/aem.01029-16.

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ABSTRACTA total of 33Lactobacillusstrains were screened for feruloyl esterase (FE) activity using agar plates containing ethyl ferulate as the sole carbon source, andLactobacillus fermentumNRRL B-1932 demonstrated the strongest FE activity among a dozen species showing a clearing zone on the opaque plate containing ethyl ferulate. FE activities were monitored using high-performance liquid chromatography with an acetonitrile-trifluoroacetic acid gradient. To produce sufficient purified FE fromL. fermentumstrain NRRL B-1932 (LfFE), the cDNA encoding LfFE (Lffae) was amplified and cloned by using

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