Faulds CB

References (40)

Title : Characterization of the CAZy Repertoire from the Marine-Derived Fungus Stemphylium lucomagnoense in Relation to Saline Conditions - Ben Ali_2020_Mar.Drugs_18_
Author(s) : Ben Ali W , Navarro D , Kumar A , Drula E , Turbe-Doan A , Correia LO , Baumberger S , Bertrand E , Faulds CB , Henrissat B , Sciara G , Mechichi T , Record E
Ref : Mar Drugs , 18 : , 2020
Abstract : Even if the ocean represents a large part of Earth's surface, only a few studies describe marine-derived fungi compared to their terrestrial homologues. In this ecosystem, marine-derived fungi have had to adapt to the salinity and to the plant biomass composition. This articles studies the growth of five marine isolates and the tuning of lignocellulolytic activities under different conditions, including the salinity. A de novo transcriptome sequencing and assembly were used in combination with a proteomic approach to characterize the Carbohydrate Active Enzymes (CAZy) repertoire of one of these strains. Following these approaches, Stemphylium lucomagnoense was selected for its adapted growth on xylan in saline conditions, its high xylanase activity, and its improved laccase activities in seagrass-containing cultures with salt. De novo transcriptome sequencing and assembly indicated the presence of 51 putative lignocellulolytic enzymes. Its secretome composition was studied in detail when the fungus was grown on either a terrestrial or a marine substrate, under saline and non-saline conditions. Proteomic analysis of the four S. lucomagnoense secretomes revealed a minimal suite of extracellular enzymes for plant biomass degradation and highlighted potential enzyme targets to be further studied for their adaptation to salts and for potential biotechnological applications.
ESTHER : Ben Ali_2020_Mar.Drugs_18_
PubMedSearch : Ben Ali_2020_Mar.Drugs_18_
PubMedID: 32916905

Title : Feruloyl esterases: Biocatalysts to overcome biomass recalcitrance and for the production of bioactive compounds - Oliveira_2019_Bioresour.Technol_278_408
Author(s) : Oliveira DM , Mota TR , Oliva B , Segato F , Marchiosi R , Ferrarese-Filho O , Faulds CB , Dos Santos WD
Ref : Bioresour Technol , 278 :408 , 2019
Abstract : Ferulic acid and its hydroxycinnamate derivatives represent one of the most abundant forms of low molecular weight phenolic compounds in plant biomass. Feruloyl esterases are part of a microorganism's plant cell wall-degrading enzymatic arsenal responsible for cleaving insoluble wall-bound hydroxycinnamates and soluble cytosolic conjugates. Stimulated by industrial requirements, accelerating scientific discoveries and knowledge transfer, continuous improvement efforts have been made to identify, create and repurposed biocatalysts dedicated to plant biomass conversion and biosynthesis of high-added value molecules. Here we review the basic knowledge and recent advances in biotechnological characteristics and the gene content encoding for feruloyl esterases. Information about several enzymes is systematically organized according to their function, biochemical properties, substrate specificity, and biotechnological applications. This review contributes to further structural, functional, and biotechnological R&D both for obtaining hydroxycinnamates from agricultural by-products as well as for lignocellulose biomass treatments aiming for production of bioethanol and other derivatives of industrial interest.
ESTHER : Oliveira_2019_Bioresour.Technol_278_408
PubMedSearch : Oliveira_2019_Bioresour.Technol_278_408
PubMedID: 30704902

Title : A Two-Step Bioconversion Process for Canolol Production from Rapeseed Meal Combining an Aspergillus niger Feruloyl Esterase and the Fungus Neolentinus lepideus - Odinot_2017_Microorganisms_5_67
Author(s) : Odinot E , Fine F , Sigoillot JC , Navarro D , Laguna O , Bisotto A , Peyronnet C , Ginies C , Lecomte J , Faulds CB , Lomascolo A
Ref : Microorganisms , 5 : , 2017
Abstract : Rapeseed meal is a cheap and abundant raw material, particularly rich in phenolic compounds of biotechnological interest. In this study, we developed a two-step bioconversion process of naturally occurring sinapic acid (4-hydroxy-3,5-dimethoxycinnamic acid) from rapeseed meal into canolol by combining the complementary potentialities of two filamentous fungi, the micromycete Aspergillus niger and the basidiomycete Neolentinus lepideus. Canolol could display numerous industrial applications because of its high antioxidant, antimutagenic and anticarcinogenic properties. In the first step of the process, the use of the enzyme feruloyl esterase type-A (named AnFaeA) produced with the recombinant strain A. niger BRFM451 made it possible to release free sinapic acid from the raw meal by hydrolysing the conjugated forms of sinapic acid in the meal (mainly sinapine and glucopyranosyl sinapate). An amount of 39 nkat AnFaeA per gram of raw meal, at 55 degreesC and pH 5, led to the recovery of 6.6 to 7.4 mg of free sinapic acid per gram raw meal, which corresponded to a global hydrolysis yield of 68 to 76% and a 100% hydrolysis of sinapine. Then, the XAD2 adsorbent (a styrene and divinylbenzene copolymer resin), used at pH 4, enabled the efficient recovery of the released sinapic acid, and its concentration after elution with ethanol. In the second step, 3-day-old submerged cultures of the strain N. lepideus BRFM15 were supplied with the recovered sinapic acid as the substrate of bioconversion into canolol by a non-oxidative decarboxylation pathway. Canolol production reached 1.3 g/L with a molar yield of bioconversion of 80% and a productivity of 100 mg/L day. The same XAD2 resin, when used at pH 7, allowed the recovery and purification of canolol from the culture broth of N. lepideus. The two-step process used mild conditions compatible with green chemistry.
ESTHER : Odinot_2017_Microorganisms_5_67
PubMedSearch : Odinot_2017_Microorganisms_5_67
PubMedID: 29036919
Gene_locus related to this paper: aspni-FAEA

Title : Hydrolysis of Nonpolar n-Alkyl Ferulates by Feruloyl Esterases - Schar_2016_J.Agric.Food.Chem_64_8549
Author(s) : Schar A , Sprecher I , Topakas E , Faulds CB , Nystrom L
Ref : Journal of Agricultural and Food Chemistry , 64 :8549 , 2016
Abstract : Ferulic acid is one of the major phenolic acids in plants and can be found esterified to plant cell wall components, but also as long-chain n-alkyl and steryl esters. Microbial feruloyl esterases may play a role in the bioavailability of phenolic acids during human and animal digestion. It is therefore of interest if feruloyl esterases are capable of hydrolyzing nonpolar ferulic acid esters. A series of n-alkyl ferulates with increasing lipophilicity were enzymatically synthesized, and the kinetic constants of their hydrolysis by four feruloyl esterases and a lipase as control were determined. A decrease in Km and kcat could be observed with decreased substrate polarity for all of the feruloyl esterases. Only one feruloyl esterase and the control lipase showed hydrolytic activity toward octadecyl ferulate. These results led to the conclusion that lipophilic ferulates are poor substrates for known feruloyl esterases and more specific esterases/lipases need to be identified.
ESTHER : Schar_2016_J.Agric.Food.Chem_64_8549
PubMedSearch : Schar_2016_J.Agric.Food.Chem_64_8549
PubMedID: 27600375

Title : Effects of enzymatic removal of plant cell wall acylation (acetylation, p-coumaroylation, and feruloylation) on accessibility of cellulose and xylan in natural (non-pretreated) sugar cane fractions - Varnai_2014_Biotechnol.Biofuels_7_153
Author(s) : Varnai A , Costa TH , Faulds CB , Milagres AM , Siika-aho M , Ferraz A
Ref : Biotechnol Biofuels , 7 :153 , 2014
Abstract : BACKGROUND: Sugar cane internodes can be divided diagonally into four fractions, of which the two innermost ones are the least recalcitrant pith and the moderately accessible pith-rind interface. These fractions differ in enzymatic hydrolyzability due to structural differences. In general, cellulose hydrolysis in plants is hindered by its physical interaction with hemicellulose and lignin. Lignin is believed to be linked covalently to hemicellulose through hydroxycinnamic acids, forming a compact matrix around the polysaccharides. Acetyl xylan esterase and three feruloyl esterases were evaluated for their potential to fragment the lignocellulosic network in sugar cane and to indirectly increase the accessibility of cellulose. RESULTS: The hydrolyzability of the pith and pith-rind interface fractions of a low-lignin-containing sugar cane clone (H58) was compared to that of a reference cultivar (RC). Acetyl xylan esterase enhanced the rate and overall yield of cellulose and xylan hydrolysis in all four substrates. Of the three feruloyl esterases tested, only TsFaeC was capable of releasing p-coumaric acid, while AnFaeA and NcFaeD released ferulic acid from both the pith and interface fractions. Ferulic acid release was higher from the less recalcitrant clone (H58)/fraction (pith), whereas more p-coumaric acid was released from the clone (RC)/fraction (interface) with a higher lignin content. In addition, a compositional analysis of the four fractions revealed that p-coumaroyl content correlated with lignin, while feruloyl content correlated with arabinose content, suggesting different esterification patterns of these two hydroxycinnamic acids. Despite the extensive release of phenolic acids, feruloyl esterases only moderately promoted enzyme access to cellulose or xylan. CONCLUSIONS: Acetyl xylan esterase TrAXE was more efficient in enhancing the overall saccharification of sugar cane, compared to the feruloyl esterases AnFaeA, TsFaeC, and NcFaeD. The hydroxycinnamic acid composition of sugar cane fractions and the hydrolysis data together suggest that feruloyl groups are more likely to decorate xylan, while p-coumaroyl groups are rather linked to lignin. The three different feruloyl esterases had distinct product profiles on non-pretreated sugar cane substrate, indicating that sugar cane pith could function as a possible natural substrate for feruloyl esterase activity measurements. Hydrolysis data suggest that TsFaeC was able to release p-coumaroyl groups esterifying lignin.
ESTHER : Varnai_2014_Biotechnol.Biofuels_7_153
PubMedSearch : Varnai_2014_Biotechnol.Biofuels_7_153
PubMedID: 25328538

Title : Cloning, overexpression in Escherichia coli, and characterization of a thermostable fungal acetylxylan esterase from Talaromyces emersonii - Waters_2012_Appl.Environ.Microbiol_78_3759
Author(s) : Waters DM , Murray PG , Miki Y , Martinez AT , Tuohy MG , Faulds CB
Ref : Applied Environmental Microbiology , 78 :3759 , 2012
Abstract : The gene encoding an acetylxylan esterase (AXE1) from the thermophilic ascomycete Talaromyces emersonii was cloned, expressed in Escherichia coli, and characterized. This form of AXE1, rTeAXE1, exhibits increased thermostability and activity at a higher temperature than other known fungal acetyl esterases, thus having huge potential application in biomass bioconversion to high value chemicals or biofuels.
ESTHER : Waters_2012_Appl.Environ.Microbiol_78_3759
PubMedSearch : Waters_2012_Appl.Environ.Microbiol_78_3759
PubMedID: 22407679

Title : Influence of organic co-solvents on the activity and substrate specificity of feruloyl esterases - Faulds_2011_Bioresour.Technol_102_4962
Author(s) : Faulds CB , Perez-Boada M , Martinez AT
Ref : Bioresour Technol , 102 :4962 , 2011
Abstract : Organic co-solvents can expand the use of enzymes in lignocellulose deconstruction through making substrates more soluble and thus more accessible. In choosing the most adequate co-solvent for feruloyl esterases, hydrolysis of methyl p-hydroxycinnamates by three pure enzymes (and a multi-enzyme preparation) was evaluated. Low concentrations of dimethylsulfoxide (DMSO) enhanced hydrolysis by two of the enzymes while at levels >20%, activity was reduced. DMSO also enhanced acetyl esterase-type activity of the enzymes. The co-solvent effect was different for each enzyme-substrate couple, indicating that other factors are also involved. Kinetic studies with a Talaromyces stipitatus feruloyl esterase showed low concentrations of dimethylsulfoxide enhanced the hydrolytic rate while K(m) also increased. Moreover, long-term incubation (96 h) of an Aspergillus niger feruloyl esterase in dimethylsulfoxide:water provided to the enzyme the ability to hydrolyze methyl p-coumarate, suggesting an active-site re-arrangement. Dimethylsulfoxide (10-30%) is proposed as an adequate co-solvent for feruloyl esterase treatment of water-insoluble substrates.
ESTHER : Faulds_2011_Bioresour.Technol_102_4962
PubMedSearch : Faulds_2011_Bioresour.Technol_102_4962
PubMedID: 21354789

Title : Feruloyl esterase-catalysed synthesis of glycerol sinapate using ionic liquids mixtures - Vafiadi_2009_J.Biotechnol_139_124
Author(s) : Vafiadi C , Topakas E , Nahmias VR , Faulds CB , Christakopoulos P
Ref : J Biotechnol , 139 :124 , 2009
Abstract : The ability of a feruloyl esterase (AnFaeA), either in free or immobilised (cross-linked enzyme aggregates) form, to catalyse the esterification of glycerol, a major by-product of the biodiesel industry, with sinapic acid was studied in four hexafluorophosphate anion-containing ionic liquids: ([Bmim][PF(6)], [Omim][PF(6)], [C(2)OHmim][PF(6)] and [C(5)O(2)mim][PF(6)]). Such ionic liquids are considered 'green' reaction systems. The synthetic reaction was optimised in [C(2)OHmim][PF(6)] and the highest conversion yield was 72.5+/-2.1%, while, at the same reaction conditions in [C(5)O(2)mim] [PF(6)], a similar conversion yield was obtained (76.7+/-1.5%). AnFaeA was active in its free and immobilised form, with the latter retaining a part of its synthetic activity after 5 consecutive 24h-period reaction cycles. Sinapic acid was esterified to one of the primary hydroxyl groups of glycerol and retained, after esterification, 63.1+/-0.3% and 89.5+/-1.1% of its antioxidant activity against low-density lipoprotein oxidation, when added at concentrations of 10 and 60muM, respectively, in the assay mixture.
ESTHER : Vafiadi_2009_J.Biotechnol_139_124
PubMedSearch : Vafiadi_2009_J.Biotechnol_139_124
PubMedID: 18822324
Gene_locus related to this paper: aspni-FAEA

Title : Enzymatic synthesis of butyl hydroxycinnamates and their inhibitory effects on LDL-oxidation - Vafiadi_2008_J.Biotechnol_133_497
Author(s) : Vafiadi C , Topakas E , Alissandratos A , Faulds CB , Christakopoulos P
Ref : J Biotechnol , 133 :497 , 2008
Abstract : The potential of the Aspergillus niger type A feruloyl esterase (AnFaeA) for the synthesis of various phenolic acid esters was examined using a ternary-organic reaction system consisting of a mixture of n-hexane, 1- or 2-butanol and water. Reaction parameters including the type of methyl hydroxycinnamate, the composition of the reaction media, the temperature, and the substrate concentration were investigated to evaluate their effect on initial rate and conversion to butyl esters of sinapic acids. Optimisation of the reaction parameters lead to 78% and 9% yield for the synthesis of 1-butyl and 2-butyl sinapate, respectively. For the first time, a feruloyl esterase was introduced in the reaction system as cross-linked enzyme aggregates (CLEAs), after optimisation of the immobilisation procedure, allowing the recycling and reuse of the biocatalyst. The inhibition of copper-induced LDL oxidation by hydroxycinnamic acids and their corresponding butyl esters was investigated in vitro. Kinetic analysis of the antioxidation process demonstrates that sinapate derivatives are effective antioxidants indicating that esterification increases the free acid's antioxidant activity especially on dimethoxylated compounds such as sinapic acid compared to methoxy-hydroxy-compounds such as ferulic acid.
ESTHER : Vafiadi_2008_J.Biotechnol_133_497
PubMedSearch : Vafiadi_2008_J.Biotechnol_133_497
PubMedID: 18155313

Title : Substrate and positional specificity of feruloyl esterases for monoferuloylated and monoacetylated 4-nitrophenyl glycosides - Puchart_2007_J.Biotechnol_127_235
Author(s) : Puchart V , Vrsanska M , Mastihubova M , Topakas E , Vafiadi C , Faulds CB , Tenkanen M , Christakopoulos P , Biely P
Ref : J Biotechnol , 127 :235 , 2007
Abstract : 4-Nitrophenyl glycosides of 2-, 3-, and 5-O-(E)-feruloyl- and 2- and 5-O-acetyl-alpha-L-arabinofuranosides and of 2-, 3-, and 4-O-(E)-feruloyl- and 2-, 3- and 4-O-acetyl-beta-D-xylopyranosides, compounds mimicking natural substrates, were used to investigate substrate and positional specificity of type-A, -B, and -C feruloyl esterases. All the feruloyl esterases behave as true feruloyl esterases showing negligible activity on sugar acetates. Type-A enzymes, represented by AnFaeA from Aspergillus niger and FoFaeII from Fusarium oxysporum, are specialized for deferuloylation of primary hydroxyl groups, with a very strong preference for hydrolyzing 5-O-feruloyl-alpha-L-arabinofuranoside. On the contrary, type-B and -C feruloyl esterases, represented by FoFaeI from F. oxysporum and TsFaeC from Talaromyces stipitatus, acted on almost all ferulates with exception of 4- and 3-O-feruloyl-beta-D-xylopyranoside. 5-O-Feruloyl-alpha-L-arabinofuranoside was the best substrate for both TsFaeC and FoFaeI, although catalytic efficiency of the latter enzyme toward 2-O-feruloyl-alpha-L-arabinofuranoside was comparable. In comparison with acetates, the corresponding ferulates served as poor substrates for the carbohydrate esterase family 1 feruloyl esterase from Aspergillus oryzae. The enzyme hydrolyzed all alpha-L-arabinofuranoside and beta-D-xylopyranoside acetates. It behaved as a non-specific acetyl esterase rather than a feruloyl esterase, with a preference for 2-O-acetyl-beta-D-xylopyranoside.
ESTHER : Puchart_2007_J.Biotechnol_127_235
PubMedSearch : Puchart_2007_J.Biotechnol_127_235
PubMedID: 16901567

Title : Diversity of plant cell wall esterases in thermophilic and thermotolerant fungi - Ghatora_2006_J.Biotechnol_125_434
Author(s) : Ghatora SK , Chadha BS , Saini HS , Bhat MK , Faulds CB
Ref : J Biotechnol , 125 :434 , 2006
Abstract : Fourteen thermophilic and thermotolerant fungal strains isolated from composting soils produced plant cell wall-acting esterases in a medium containing corn cobs and oat spelt xylan. The concentrated and dialyzed protein extracts of these fungi were fractionated using isoelectric-focusing, gels sliced and eluted protein in each slice was assayed for esterase activity against p-nitrophenyl acetate. A total of 84 esterases detected on the basis of pI were found to show distinct preferential substrate specificities towards p-nitrophenyl acetate, p-nitrophenyl ferulate and p-nitrophenyl butyrate, and were putatively classified as acetyl esterases and esterases types I and II. None of the esterases were active against p-nitrophenyl myristate. In addition, these esterases were characterized as acid, neutral or alkaline active.
ESTHER : Ghatora_2006_J.Biotechnol_125_434
PubMedSearch : Ghatora_2006_J.Biotechnol_125_434
PubMedID: 16713648

Title : Synergy between xylanases from glycoside hydrolase family 10 and family 11 and a feruloyl esterase in the release of phenolic acids from cereal arabinoxylan - Faulds_2006_Appl.Microbiol.Biotechnol_71_622
Author(s) : Faulds CB , Mandalari G , Lo Curto RB , Bisignano G , Christakopoulos P , Waldron KW
Ref : Applied Microbiology & Biotechnology , 71 :622 , 2006
Abstract : The bioconversion of waste residues (by-products) from cereal processing industries requires the cooperation of enzymes able to degrade xylanolytic and cellulosic material. The type A feruloyl esterase from Aspergillus niger, AnFaeA, works synergistically with (1-->4)-beta-D-xylopyranosidases (xylanases) to release monomeric and dimeric ferulic acid (FA) from cereal cell wall-derived material. The esterase was more effective with a family 11 xylanase from Trichoderma viride in releasing FA and with a family 10 xylanase from Thermoascus aurantiacus in releasing the 5,5' form of diferulic acid from arabinoxylan (AX) derived from brewers' spent grain. The converse was found for the release of the phenolic acids from wheat bran-derived AXs. This may be indicative of compositional differences in AXs in cereals.
ESTHER : Faulds_2006_Appl.Microbiol.Biotechnol_71_622
PubMedSearch : Faulds_2006_Appl.Microbiol.Biotechnol_71_622
PubMedID: 16292533

Title : The feruloyl esterase system of Talaromyces stipitatus: determining the hydrolytic and synthetic specificity of TsFaeC - Vafiadi_2006_J.Biotechnol_125_210
Author(s) : Vafiadi C , Topakas E , Christakopoulos P , Faulds CB
Ref : J Biotechnol , 125 :210 , 2006
Abstract : The active site of the recombinant Talaromyces stipitatus type-C feruloyl esterase (TsFaeC) was probed using a series of C1-C4 alkyl ferulates and methyl esters of phenylalkanoic and cinnamic acids. The enzyme was active on 23 of the 34 substrates tested. Lengthening or shortening the aliphatic side chain while maintaining the same aromatic substitutions completely abolished the enzyme activity. Maintaining the phenylpropenoate structure but altering the substitutions of the aromatic ring demonstrated the importance of hydroxyl groups on meta and/or para position of the benzoic ring. The highest catalytic efficiency of TsFaeC for methyl cinnamates was shown on methyl 3,4-dihydroxy cinnamate and on its hydro form (3,4-dihydroxy-phenyl-propionate). Maintaining the ferulate structure but altering the esterified alkyl group, the comparison of k(cat) and k(cat)/K(m) values showed that the enzyme hydrolysed faster and more efficiently than ethyl ferulate. Alkyl ferulates were applied also for substrate selectivity mapping of feruloyl esterase to catalyze feruloyl group transfer to l-arabinose, using as a reaction system a ternary water-organic mixture consisting of n-hexane, t-butanol and water. The reaction parameters affecting the feruloylation rate and the conversion of the enzymatic synthesis, such as the composition of the reaction media, temperature, substrate and enzyme concentration have been investigated.
ESTHER : Vafiadi_2006_J.Biotechnol_125_210
PubMedSearch : Vafiadi_2006_J.Biotechnol_125_210
PubMedID: 16584797

Title : Comparison of mesophilic and thermophilic feruloyl esterases: characterization of their substrate specificity for methyl phenylalkanoates - Topakas_2005_J.Biotechnol_115_355
Author(s) : Topakas E , Christakopoulos P , Faulds CB
Ref : J Biotechnol , 115 :355 , 2005
Abstract : The active sites of feruloyl esterases from mesophilic and thermophilic sources were probed using methyl esters of phenylalkanoic acids. Only 13 out of 26 substrates tested were significant substrates for all the enzymes. Lengthening or shortening the aliphatic side chain while maintaining the same aromatic substitutions completely abolished activity for both enzymes, which demonstrates the importance of the correct distance between the aromatic group and the ester bond. Maintaining the phenylpropanoate structure but altering the substitutions of the aromatic ring demonstrated that the type-A esterase from the mesophilic fungus Fusarium oxysporum (FoFaeA) showed a preference for methoxylated substrates, in contrast to the type-B esterase from the same source (FoFaeB) and the thermophilic type-B (StFaeB) and type-C (StFaeC) from Sporotrichum thermophile, which preferred hydroxylated substrates. All four esterases hydrolyzed short chain aliphatic acid (C2-C4) esters of p-nitrophenol, but not the C12 ester of laurate. All the feruloyl esterases were able to release ferulic acid from the plant cell wall material in conjunction with a xylanase, but only the type-A esterase FoFaeA was effective in releasing the 5,5' form of diferulic acid. The thermophilic type-B esterase had a lower catalytic efficiency than its mesophilic counterpart, but released more ferulic acid from plant cell walls.
ESTHER : Topakas_2005_J.Biotechnol_115_355
PubMedSearch : Topakas_2005_J.Biotechnol_115_355
PubMedID: 15639097

Title : Probing the determinants of substrate specificity of a feruloyl esterase, AnFaeA, from Aspergillus niger - Faulds_2005_Febs.J_272_4362
Author(s) : Faulds CB , Molina R , Gonzalez R , Husband F , Juge N , Sanz-Aparicio J , Hermoso JA
Ref : Febs J , 272 :4362 , 2005
Abstract : Feruloyl esterases hydrolyse phenolic groups involved in the cross-linking of arabinoxylan to other polymeric structures. This is important for opening the cell wall structure making material more accessible to glycoside hydrolases. Here we describe the crystal structure of inactive S133A mutant of type-A feruloyl esterase from Aspergillus niger (AnFaeA) in complex with a feruloylated trisaccharide substrate. Only the ferulic acid moiety of the substrate is visible in the electron density map, showing interactions through its OH and OCH(3) groups with the hydroxyl groups of Tyr80. The importance of aromatic and polar residues in the activity of AnFaeA was also evaluated using site-directed mutagenesis. Four mutant proteins were heterologously expressed in Pichia pastoris, and their kinetic properties determined against methyl esters of ferulic, sinapic, caffeic and p-coumaric acid. The k(cat) of Y80S, Y80V, W260S and W260V was drastically reduced compared to that of the wild-type enzyme. However, the replacement of Tyr80 and Trp260 with smaller residues broadened the substrate specificity of the enzyme, allowing the hydrolysis of methyl caffeate. The role of Tyr80 and Trp260 in AnFaeA are discussed in light of the three-dimensional structure.
ESTHER : Faulds_2005_Febs.J_272_4362
PubMedSearch : Faulds_2005_Febs.J_272_4362
PubMedID: 16128806
Gene_locus related to this paper: aspni-FAEA

Title : The feruloyl esterase system of Talaromyces stipitatus: production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity - Garcia-Conesa_2004_J.Biotechnol_108_227
Author(s) : Garcia-Conesa MT , Crepin VF , Goldson AJ , Williamson G , Cummings NJ , Connerton IF , Faulds CB , Kroon PA
Ref : J Biotechnol , 108 :227 , 2004
Abstract : Several extracellular feruloyl esterases were produced by the mesophilic fungus Talaromyces stipitatus when grown on selective carbon sources in liquid media. Type-A and Type-B feruloyl esterases, as defined by their substrate specificity against methyl hydroxycinnamates, were produced during growth on wheat bran and sugar beet pulp, respectively. In addition, Tal. stipitatus produced a new type of esterase (TsFaeC) during growth on sugar beet pulp with a broader spectrum of activity (Type-C) against the (hydroxy)cinnamate esters than those previously described. All three enzymes were purified and N-terminal amino acid sequences and internal peptide sequences determined. The TsFaeC sequences were used to amplify a gene fragment from Tal. stipitatus genomic DNA. The flanking sequences were identified with the aid of RACE-RTPCR, and a full-length clone constructed. The faeC gene is present as a single copy and contains a single intron. The complete cDNA fragment contains an ORF of 1590bp, faeC, which is predicted to encode a 530 amino acid pre-protein, including a 25-residue signal peptide, and to produce a mature protein of M(R) 55 340Da. There was no evidence for a carbohydrate-binding domain in TsFaeC.
ESTHER : Garcia-Conesa_2004_J.Biotechnol_108_227
PubMedSearch : Garcia-Conesa_2004_J.Biotechnol_108_227
PubMedID: 15006424
Gene_locus related to this paper: talsn-faeb

Title : Identification of a type-D feruloyl esterase from Neurospora crassa - Crepin_2004_Appl.Microbiol.Biotechnol_63_567
Author(s) : Crepin VF , Faulds CB , Connerton IF
Ref : Applied Microbiology & Biotechnology , 63 :567 , 2004
Abstract : Feruloyl esterases 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 presence of feruoyl esterase genes present in the genome sequence of the filamentous fungus Neurospora crassa. We have identified an orphan gene (contig 3.544), the translation of which shows sequence identity with known feruloyl esterases. This gene was cloned and the corresponding recombinant protein expressed in Pichia pastoris to confirm that the enzyme (NcFaeD-3.544) exhibits feruloyl esterase activity. Unusually the enzyme was capable of p-coumaric acid release from untreated crude plant cell wall materials. The substrate utilisation preferences of the recombinant enzyme place it in the recently recognised type-D sub-class of feruloyl esterase.
ESTHER : Crepin_2004_Appl.Microbiol.Biotechnol_63_567
PubMedSearch : Crepin_2004_Appl.Microbiol.Biotechnol_63_567
PubMedID: 14595525
Gene_locus related to this paper: neucr-FAED

Title : The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family - Hermoso_2004_J.Mol.Biol_338_495
Author(s) : Hermoso JA , Sanz-Aparicio J , Molina R , Juge N , Gonzalez R , Faulds CB
Ref : Journal of Molecular Biology , 338 :495 , 2004
Abstract : As a component of the array of enzymes produced by micro-organisms to deconstruct plant cell walls, feruloyl esterases hydrolyze phenolic groups involved in the cross-linking of arabinoxylan to other polymeric structures. This is important for opening the cell wall structure, making material more accessible to glycosyl hydrolases. Here, we describe the first crystal structure of the non-modular type-A feruloyl esterase from Aspergillus niger (AnFaeA) solved at 2.5A resolution. AnFaeA displays an alpha/beta hydrolase fold similar to that found in fungal lipases and different from that reported for other feruloyl esterases. Crystallographic and site-directed mutagenesis studies allow us to identify the catalytic triad (Ser133-His247-Asp194) that forms the catalytic machinery of this enzyme. The active-site cavity is confined by a lid (residues 68-80), on the analogy of lipases, and by a loop (residues 226-244) that confers plasticity to the substrate-binding site. The lid presents a high ratio of polar residues, which in addition to a unique N-glycosylation site stabilises the lid in an open conformation, conferring the esterase character to this enzyme. A putative model for bound 5,5'-diferulic acid-linked arabinoxylan has been built, pointing to the more relevant residues involved in substrate recognition. Comparison with structurally related lipases reveals that subtle amino acid and conformational changes within a highly conserved protein fold may produce protein variants endowed with new enzymatic properties, while comparison with functionally related proteins points to a functional convergence after evolutionary divergence within the feruloyl esterases family.
ESTHER : Hermoso_2004_J.Mol.Biol_338_495
PubMedSearch : Hermoso_2004_J.Mol.Biol_338_495
PubMedID: 15081808
Gene_locus related to this paper: aspni-FAEA

Title : Functional classification of the microbial feruloyl esterases - Crepin_2004_Appl.Microbiol.Biotechnol_63_647
Author(s) : Crepin VF , Faulds CB , Connerton IF
Ref : Applied Microbiology & Biotechnology , 63 :647 , 2004
Abstract : Feruloyl esterases have potential uses over a broad range of applications in the agri-food industries. In recent years, the number of microbial feruloyl esterase activities reported has increased and, in parallel, even more related protein sequences may be discerned in the growing genome databases. Based on substrate utilisation data and supported by primary sequence identity, four sub-classes have been characterised and termed type-A, B, C and D. The proposed sub-classification scheme is discussed in terms of the evolutionary relationships existing between carbohydrate esterases.
ESTHER : Crepin_2004_Appl.Microbiol.Biotechnol_63_647
PubMedSearch : Crepin_2004_Appl.Microbiol.Biotechnol_63_647
PubMedID: 14661116

Title : Regioselective deacetylation of cellulose acetates by acetyl xylan esterases of different CE-families - Altaner_2003_J.Biotechnol_105_95
Author(s) : Altaner C , Saake B , Tenkanen M , Eyzaguirre J , Faulds CB , Biely P , Viikari L , Siika-aho M , Puls J
Ref : J Biotechnol , 105 :95 , 2003
Abstract : Cellulose acetate (CA) was found to be a substrate of several acetyl xylan esterases (AXE). Eight AXE from different carbohydrate esterase (CE) families were tested on their activity against CA with a degree of substitution of 0.7 and 1.4. The classification of the AXEs into CE families according to their structure by hydrophobic cluster analysis followed clearly their activity against CA. Within the same CE family similar, and between the CE families different deacetylation behaviours could be observed. Furthermore, each esterase family showed a distinct regioselective mode of action. The CE 1 family enzymes regioselectively cleaved the substituents in C2- and C3-position, while CE 5 family enzymes only cleaved the acetyl groups in C2-position. CE 4 family enzymes seemed to interact only with the substituents in C3-position. Evidence was found that the deacetylation reaction of the CE 1 family enzymes proceeded faster in C2- than in C3-position of CA. The enzymes were able to cleave acetyl groups from fully substituted anhydroglucose units.
ESTHER : Altaner_2003_J.Biotechnol_105_95
PubMedSearch : Altaner_2003_J.Biotechnol_105_95
PubMedID: 14511913

Title : Production and characterization of the Talaromyces stipitatus feruloyl esterase FAEC in Pichia pastoris: identification of the nucleophilic serine - Crepin_2003_Protein.Expr.Purif_29_176
Author(s) : Crepin VF , Faulds CB , Connerton IF
Ref : Protein Expr Purif , 29 :176 , 2003
Abstract : Feruloyl esterases constitute an interesting group of enzymes that have the potential for use over a broad range of applications in the agri-food industries. We report the over-expression and characterization of a novel feruloyl esterase exhibiting broad substrate specificity from Talaromyces stipitatus (FAEC) in Pichia pastoris. Using various gene constructions, we have investigated the use of alternative signal peptides to produce an authentic feruloyl esterase featuring the N-terminal sequence determined for the native enzyme. We demonstrate that additional amino acids at the N-terminus of the FAEC sequence do not influence the catalytic capacity of the enzyme, and that the nature of the signal sequence has a limited effect on the yield of the secreted enzyme, with the T. stipitatus FAEC signal sequence producing 297 mgL(-1), the Neurospora crassa Fae-1 260 mgL(-1), and the Saccharomyces cerevisiae alpha-factor secretion signal 214 mgL(-1). Mature FAEC contains two internal peptide sequences that correspond with the consensus motif G-X-S-X-G that contains the catalytic serine nucleophile, which is conserved in the esterase enzyme superfamily. The serine residues at the center of these peptide motifs have been independently mutated and the corresponding enzymes have been over-expressed in P. pastoris to identify the candidate nucleophilic residue responsible for catalyzing the enzymatic reaction. Purified recombinant FAEC containing S465A retained the esterase activity and appeared unaffected by the amino acid modification. In contrast, FAEC activity containing S166A was below the HPLC detection limit, suggesting that serine 166 constitutes the nucleophile.
ESTHER : Crepin_2003_Protein.Expr.Purif_29_176
PubMedSearch : Crepin_2003_Protein.Expr.Purif_29_176
PubMedID: 12767807

Title : A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition - Crepin_2003_Biochem.J_370_417
Author(s) : Crepin VF , Faulds CB , Connerton IF
Ref : Biochemical Journal , 370 :417 , 2003
Abstract : 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 overexpressed in Pichia pastoris. The gene encodes a single-domain ferulic acid esterase, which represents the first report of a non-modular type B enzyme (fae-1 gene; GenBank accession no. AJ293029). The purified recombinant protein has been shown to exhibit concentration-dependent substrate inhibition (K(m) 0.048 mM, K (i) 2.5 mM and V(max) 8.2 units/mg against methyl 3,4-dihydroxycinnamate). The kinetic behaviour of the non-modular enzyme is discussed in terms of the diversity in the roles of the feruloyl esterases in the mobilization of plant cell wall materials and their respective modes of action.
ESTHER : Crepin_2003_Biochem.J_370_417
PubMedSearch : Crepin_2003_Biochem.J_370_417
PubMedID: 12435269
Gene_locus related to this paper: neucr-faeb

Title : High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris - Juge_2001_FEMS.Yeast.Res_1_127
Author(s) : Juge N , Williamson G , Puigserver A , Cummings NJ , Connerton IF , Faulds CB
Ref : FEMS Yeast Res , 1 :127 , 2001
Abstract : The cDNA encoding Aspergillus niger cinnamoyl esterase (FAEA) with its native signal sequence was isolated by reverse transcriptase-polymerase chain reaction, sequenced, and expressed in Pichia pastoris. Secretion yields up to 300 mg l(-1) were obtained in buffered medium. The recombinant FAEA was purified to homogeneity using a one-step purification protocol and found to be identical to the native enzyme with respect to size, pI, immunoreactivity and N-terminal sequence. Specific activity, pH and temperature optimum, and kinetic parameters were also found similar to the native esterase. FAEA is thus the first fungal esterase efficiently produced using a heterologous system.
ESTHER : Juge_2001_FEMS.Yeast.Res_1_127
PubMedSearch : Juge_2001_FEMS.Yeast.Res_1_127
PubMedID: 12702357

Title : Specificity of ferulic acid (feruloyl) esterases -
Author(s) : Williamson G , Faulds CB , Kroon PA
Ref : Biochemical Society Transactions , 26 :205 , 1998
PubMedID: 9649748

Title : Hairy plant polysaccharides: a close shave with microbial esterases -
Author(s) : Williamson G , Kroon PA , Faulds CB
Ref : Microbiology , 144 ( Pt 8) :2011 , 1998
PubMedID: 9720023

Title : Stability of feruloyl esterases from Aspergillus -
Author(s) : Faulds CB , de Vries RP , Visser J , Williamson G
Ref : Biochemical Society Transactions , 26 :S165 , 1998
PubMedID: 9649840

Title : Methyl phenylalkanoates as substrates to probe the active sites of esterases - Kroon_1997_Eur.J.Biochem_248_245
Author(s) : Kroon PA , Faulds CB , Brezillon C , Williamson G
Ref : European Journal of Biochemistry , 248 :245 , 1997
Abstract : We have used methyl esters of phenylalkanoic acids to probe the active site of two esterases (FAE-III and CinnAE) from Aspergillus niger. Only methyl 4-hydroxy-3-methoxycinnamate and 4-hydroxy-3-methoxyphenylpropionate out of 19 substrates tested were significant substrates for both enzymes (k(cat) values about 10(2) s(-1) and 10(3) s(-1), respectively). Lengthening or shortening the aliphatic side chain while maintaining the same aromatic substitutions completely abolished activity for both enzymes, which demonstrates the importance of the correct distance between the aromatic group and the ester bond. Differences in Km values for FAE-III were small (0.45-2.08 mM) but there were two orders of magnitude difference in k(cat) values (12.1-1063 s(-1)), whereas for CinnAE, there were large differences in values for both Km (0.014-1.32 mM) and k(cat) (41.3-1410 s(-1)). Lability of the ester bonds, as estimated from second-order rate constants (k2) for chemical reaction with sodium hydroxide, did not correlate to k(cat) for CinnAE (r = 0.33) or for FAE-III (r = 0.43). Maintaining the phenylpropenoate structure but altering the substitutions on the aromatic ring demonstrated the following: a 3-methoxy group is essential for FAE-III activity, whereas a 3-methoxy group precluded activity of CinnAE, with the exception of methyl 4-hydroxy-3-methoxycinnamate which was a relatively poor substrate for CinnAE; (b) increasing the number of methoxy substitutions increased the activity of FAE-III, and decreased the activity of CinnAE; (c) 4-hydroxy substituents, and additional hydroxy substituents, increased the activity of CinnAE, but decreased that of FAE-III; (d) the rate of hydrolysis with sodium hydroxide of the methyl esters in general is decreased by hydroxy substitutions on the aromatic ring but increased by methoxy substitutions. Analysis of kinetic data obtained in the presence of inhibitors indicated that substrate analogs were able to bind to both free CinnAE and to a CinnAE-substrate complex, but conversely, were only able to bind to free FAE-III. The results show that the specificities of the two A. niger esterases are complementary. The rate of hydrolysis by this class of carboxylic ester hydrolase does not depend on the intrinsic lability of the ester bond, but depends on both the distance between the aromatic ring and the ester bond, and the substitutions on the aromatic ring.
ESTHER : Kroon_1997_Eur.J.Biochem_248_245
PubMedSearch : Kroon_1997_Eur.J.Biochem_248_245
PubMedID: 9310385
Gene_locus related to this paper: aspng-faeb , aspni-FAEA

Title : The faeA genes from Aspergillus niger and Aspergillus tubingensis encode ferulic acid esterases involved in degradation of complex cell wall polysaccharides - de Vries_1997_Appl.Environ.Microbiol_63_4638
Author(s) : de Vries RP , Michelsen B , Poulsen CH , Kroon PA , van den Heuvel RH , Faulds CB , Williamson G , van den Hombergh JP , Visser J
Ref : Applied Environmental Microbiology , 63 :4638 , 1997
Abstract : We report the cloning and characterization of a gene encoding a ferulic acid esterase, faeA, from Aspergillus niger and Aspergillus tubingensis. The A. niger and A. tubingensis genes have a high degree of sequence identity and contain one conserved intron. The gene product, FAEA, was overexpressed in wild-type A. tubingensis and a protease-deficient A. niger mutant. Overexpression of both genes in wild-type A. tubingensis and an A. niger protease-deficient mutant showed that the A. tubingensis gene product is more sensitive to degradation than the equivalent gene product from A. niger. FAEA from A. niger was identical to A. niger FAE-III (C. B. Faulds and G. Williamson, Microbiology 140:779-787, 1994), as assessed by molecular mass, pH and temperature optima, pI, N-terminal sequence, and activity on methyl ferulate. The faeA gene was induced by growth on wheat arabinoxylan and sugar beet pectin, and its gene product (FAEA) released ferulic acid from wheat arabinoxylan. The rate of release was enhanced by the presence of a xylanase. FAEA also hydrolyzed smaller amounts of ferulic acid from sugar beet pectin, but the rate was hardly affected by addition of an endo-pectin lyase.
ESTHER : de Vries_1997_Appl.Environ.Microbiol_63_4638
PubMedSearch : de Vries_1997_Appl.Environ.Microbiol_63_4638
PubMedID: 9406381
Gene_locus related to this paper: aspni-FAEA , asptu-FAEA

Title : Influence of ferulic acid on the production of feruloyl esterases by Aspergillus niger - Faulds_1997_FEMS.Microbiol.Lett_157_239
Author(s) : Faulds CB , de Vries RP , Kroon PA , Visser J , Williamson G
Ref : FEMS Microbiology Letters , 157 :239 , 1997
Abstract : Extracellular feruloyl esterases from the filamentous fungus Aspergillus niger are induced by growth on oat spelt xylan (OSX), which contains no detectable esterified ferulic acid. FAE-III accounted for most of the feruloyl esterase activity. Addition of free ferulic acid to OSX at the start of the culture induced FAE-III secretion a further 2.3-fold, and also induced other feruloyl esterases which could not be ascribed to FAE-III. Wheat bran-(WB)-grown cultures, containing 1% (m/v) esterlinked ferulic acid, gave almost identical FAE-III and total feruloyl esterase activities as the cultures grown on OSX plus ferulic acid. De-esterification of WB yielded less total feruloyl esterase, and 2.4-fold less FAE-III, compared to untreated WB. A slightly modified form of FAE-III was produced on de-esterified WB. These results show that production of FAE-III does not absolutely require ferulic acid. However, production is stimulated by the presence of free ferulic acid through increased expression, and is reduced by the removal of esterified ferulic acid from the growth substrate.
ESTHER : Faulds_1997_FEMS.Microbiol.Lett_157_239
PubMedSearch : Faulds_1997_FEMS.Microbiol.Lett_157_239
PubMedID: 9435103

Title : An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (Xy1D) release a 5-5' ferulic dehydrodimer (diferulic acid) from barley and wheat cell walls - Bartolome_1997_Appl.Environ.Microbiol_63_208
Author(s) : Bartolome B , Faulds CB , Kroon PA , Waldron K , Gilbert HJ , Hazlewood G , Williamson G
Ref : Applied Environmental Microbiology , 63 :208 , 1997
Abstract : Diferulate esters strengthen and cross-link primary plant cell walls and help to defend the plant from invading microbes. Phenolics also limit the degradation of plant cell walls by saprophytic microbes and by anaerobic microorganisms in the rumen. We show that incubation of wheat and barley cell walls with ferulic acid esterase from Aspergillus niger (FAE-III) or Pseudomonas fluorescens (Xy1D), together with either xylanase I from Aspergillus niger, Trichoderma viride xylanase, or xylanase from Pseudomonas fluorescens (XylA), leads to release of the ferulate dimer 5-5' diFA [(E,E)-4,4'-dihydroxy-5,5'-dimethoxy-3,3'-bicinnamic acid]. Direct saponification of the cell walls without enzyme treatment released the following five identifiable ferulate dimers (in order of abundance): (Z)-beta-(4-[(E)-2-carboxyvinyl]-2-methoxyphenoxy)-4-hydroxy-3-methoxycinnamic acid, trans-5-[(E)-2-carboxyvinyl]-2-(4-hydroxy-3-methoxy-phenyl) -7-methoxy-2, 3-dihydrobenzofuran-3-carboxylic acid, 5-5' diFA, (E,E)-4, 4'-dihydroxy-3, 5'-dimethoxy-beta, 3'-bicinnamic acid, and trans-7-hydroxy-1-(4-hydroxy-3-methoxyphenyl) -6-methoxy-1, 2-dihydronaphthalene-2, 3-dicarboxylic acid. Incubation of the wheat or barley cell walls with xylanase, followed by saponification of the solubilized fraction, yielded 5-5'diFA and, in some cases, certain of the above dimers, depending on the xylanase used. These experiments demonstrate that FAE-III and XYLD specifically release only esters of 5-5'diFA from either xylanase-treated or insoluble fractions of cell walls, even though other esterified dimers were solubilized by preincubation with xylanase. It is also concluded that the esterified dimer content of the xylanase-solubilized fraction depends on the source of the xylanase.
ESTHER : Bartolome_1997_Appl.Environ.Microbiol_63_208
PubMedSearch : Bartolome_1997_Appl.Environ.Microbiol_63_208
PubMedID: 8979352
Gene_locus related to this paper: aspni-FAEA , celju-b3pei5

Title : Purification and characterization of a novel esterase induced by growth of Aspergillus niger on sugar-beet pulp - Kroon_1996_Biotechnol.Appl.Biochem_23 ( Pt 3)_255
Author(s) : Kroon PA , Faulds CB , Williamson G
Ref : Biotechnol Appl Biochem , 23 ( Pt 3) :255 , 1996
Abstract : An inducible esterase has been isolated from a liquid culture of Aspergillus niger grown on sugar-beet pulp. The enzyme was active on methyl esters of cinnamic acids, caffeic > p-coumaric > ferulic, and is therefore termed a cinnamoyl esterase. The enzyme was not active on methyl sinapinate, a good substrate for ferulic acid esterase III, which was purified previously from A. niger [Faulds and Williamson (1994) Microbiology 140, 779-787]. With methyl caffeate as substrate the enzyme had temperature and pH optima of 50 degrees C and 6.0 respectively, and a specific activity of 96.9 units per mg of protein. The purified protein (native molecular mass 145 000 Da) gave a single heavily stained band on SDS/PAGE, suggesting the protein was a dimer, and seemed to be heavily glycosylated. Isoelectric focusing gave a single band corresponding to a pl of 4.80. The pure enzyme was free of other carbohydrase activities. The activity of the pure enzyme was inhibited by more than 99% after treatment with the serine-specific protease inhibitor aminoethylbenzenesulphonylfluoride (1 mM) for 12 h. The enzyme was capable of releasing ferulic acid from sugar beet pulp.
ESTHER : Kroon_1996_Biotechnol.Appl.Biochem_23 ( Pt 3)_255
PubMedSearch : Kroon_1996_Biotechnol.Appl.Biochem_23 ( Pt 3)_255
PubMedID: 8679110
Gene_locus related to this paper: aspng-faeb

Title : A major bioactive component of plant cell walls, ferulic acid, influences feruloyl esterase production in Aspergillus niger -
Author(s) : Faulds CB , Williamson G
Ref : Biochemical Society Transactions , 24 :386S , 1996
PubMedID: 8878930

Title : Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger - Faulds_1995_Appl.Microbiol.Biotechnol_43_1082
Author(s) : Faulds CB , Williamson G
Ref : Applied Microbiology & Biotechnology , 43 :1082 , 1995
Abstract : Ferulic acid was efficiently released from a wheat bran preparation by a ferulic acid esterase from Aspergillus niger (FAE-III) when incubated together with a Trichoderma viride xylanase (a maximum of 95% total ferulic acid released after 5 h incubation). FAE-III by itself could release ferulic acid but at a level almost 24-fold lower than that obtained in the presence of the xylanase (2 U). Release of ferulic acid was proportional to the FAE-III concentration between 0.1 U and 1.3 U, but the presence of low levels of xylanase (0.1 U) increased the amount of ferulic acid released 6-fold. Total sugar release was not influenced by the action of FAE-III on the wheat bran, but the rate of release of the apparent end-products of xylanase action (xylose and xylobiose) was elevated by the presence of the esterase. The results show that FAE-III and the xylanase act together to break down feruloylated plant cell-wall polysaccharides to give a high yield of ferulic acid.
ESTHER : Faulds_1995_Appl.Microbiol.Biotechnol_43_1082
PubMedSearch : Faulds_1995_Appl.Microbiol.Biotechnol_43_1082
PubMedID: 8590660
Gene_locus related to this paper: aspni-FAEA

Title : Release of the antioxidant, ferulic acid, from plant material by specific esterases -
Author(s) : Faulds CB , Williamson G
Ref : Biochemical Society Transactions , 23 :253S , 1995
PubMedID: 7672277

Title : Specificity of an esterase (XYLD) from Pseudomonas fluorescens subsp. cellulosa - Faulds_1995_Biochim.Biophys.Acta_1243_265
Author(s) : Faulds CB , Ralet MC , Williamson G , Hazlewood GP , Gilbert HJ
Ref : Biochimica & Biophysica Acta , 1243 :265 , 1995
Abstract : Activity of an esterase from Pseudomonas fluorescens subsp. cellulosa (XYLD) on an insoluble feruloylated hemicellulose substrate (de-starched wheat bran) was dependent on the source of added endo-xylanase. The esterase exhibited high selectivity for the nature, position of linkage and size of the feruloylated oligosaccharides generated by hydrolysis of the hemicellulose. Increased affinity of XYLD with increasing size of the oligosaccharide substrate suggests that optimal activity is observed on substrates with at least 4 sugars.
ESTHER : Faulds_1995_Biochim.Biophys.Acta_1243_265
PubMedSearch : Faulds_1995_Biochim.Biophys.Acta_1243_265
PubMedID: 7873572

Title : Isolation and purification of feruloylated oligosaccharides from cell walls of sugar-beet pulp - Ralet_1994_Carbohydr.Res_263_227
Author(s) : Ralet MC , Thibault JF , Faulds CB , Williamson G
Ref : Carbohydr Res , 263 :227 , 1994
Abstract : Cell walls from sugar-beet pulp contain some feruloyl groups linked to the pectic neutral side-chains. Enzymic as well as chemical hydrolysis of the pulp yielded a series of feruloylated oligosaccharides, which have been purified by Sephadex LH-20 and Biogel P-2 chromatography in aqueous solvents. Feruloylated arabinose di-, tri-, hexa-, hepta-, and octa-saccharides as well as feruloylated galactose disaccharides were obtained after hydrolysis of the pulp with a mixture of fungal carbohydrases (Driselase). Feruloylated arabinose and galactose monosaccharides were obtained through mild acid hydrolyses. Both arabinose and galactose residues in the side-chains are feruloylated, 50-55% of the feruloyl groups being linked to arabinose residues and 45-50% to galactose residues. It is concluded that 1 out of 56 arabinose residues and 1 out of 16 galactose residues present as pectic side-chains in sugar-beet pulp carry a feruloyl group.
ESTHER : Ralet_1994_Carbohydr.Res_263_227
PubMedSearch : Ralet_1994_Carbohydr.Res_263_227
PubMedID: 7805051

Title : Degradation of feruloylated oligosaccharides from sugar-beet pulp and wheat bran by ferulic acid esterases from Aspergillus niger - Ralet_1994_Carbohydr.Res_263_257
Author(s) : Ralet MC , Faulds CB , Williamson G , Thibault JF
Ref : Carbohydr Res , 263 :257 , 1994
Abstract : The activity of two forms of ferulic acid esterase (FAE) from Aspergillus niger on a synthetic feruloylated substrate (methyl ferulate) and on 11 different feruloylated oligosaccharides from sugar-beet pulp and wheat bran was determined. The enzymes exhibited different specificities for the various feruloylated substrates and were more active on certain substrates of cell-wall origin than on methyl ferulate. Both enzymes preferred the arabinose residue to which ferulic acid is attached in the furanose form. FAE-I had no clear preference for the type of linkage involved between the ferulic acid units and the oligosaccharide chain. In contrast, FAE-III had a clear requirement for ferulic acid to be attached to O-5 of the Ara f ring while no catalysis was observed when ferulic acid was attached to O-2. Both enzymes showed maximum activity on feruloylated trisaccharides. An increase in the length of the oligosaccharide chain did not preclude catalysis, but feruloylated oligosaccharides of a dp > 3 were hydrolysed at a reduced rate. Our results support the hypothesis that different kinds of ferulic acid esterases exist with different specificities for the oligosaccharide chain of the feruloylated substrates.
ESTHER : Ralet_1994_Carbohydr.Res_263_257
PubMedSearch : Ralet_1994_Carbohydr.Res_263_257
PubMedID: 7805053
Gene_locus related to this paper: aspng-faeb , aspni-FAEA

Title : Structure identification of feruloylated oligosaccharides from sugar-beet pulp by NMR spectroscopy - Colquhoun_1994_Carbohydr.Res_263_243
Author(s) : Colquhoun IJ , Ralet MC , Thibault JF , Faulds CB , Williamson G
Ref : Carbohydr Res , 263 :243 , 1994
Abstract : 1D NMR (1H and 13C) and 2D NMR spectroscopy have been used to determine the structure of feruloylated oligosaccharides obtained by enzymic degradation or mild acid hydrolysis of sugar-beet pulp. Feruloylated oligosaccharides derived from pectic neutral side-chains containing arabinose or galactose residues were identified. In the feruloylated arabinose oligosaccharides, feruloyl groups were linked to O-2 of L-Ara f residues. The structure of the feruloylated arabinose disaccharide was identified as O-[2-O-(transferuloyl)-alpha-L-Ara f]-(1-->5)-L-Ara f and that of the feruloylated arabinose trisaccharide as O-alpha-L-Ara f-(1-->3)-O-[2-O-(trans-feruloyl)-alpha-L-Ara f]-(1-->5)-L- Ara f. The structure of the feruloylated galactose disaccharide was identified as O-[6-O-(trans-feruloyl) -beta-D-Gal p]-(1-->4)-D-Gal p. From our results, we suggest that the feruloyl groups present in sugar-beet pulp are linked to the arabinofuranosyl residues of the main core of alpha-(1-->5)-linked arabinan chains and to the galactopyranosyl residues of the main core of beta-(1-->4)-linked type I galactan chains.
ESTHER : Colquhoun_1994_Carbohydr.Res_263_243
PubMedSearch : Colquhoun_1994_Carbohydr.Res_263_243
PubMedID: 7805052

Title : Ferulic acid esterase from Aspergillus niger: purification and partial characterization of two forms from a commercial source of pectinase - Faulds_1993_Biotechnol.Appl.Biochem_17_349
Author(s) : Faulds CB , Williamson G
Ref : Biotechnol Appl Biochem , 17 :349 , 1993
Abstract : Two forms of ferulic acid esterase from Aspergillus niger have been isolated from a commercial source of pectinase. One, designated I, has a M(r) of 132,000, is probably dimeric, and has a pI of 3.0. The second, designated II, was partially purified and is monomeric (M(r) 29,000), with a pI of 3.6. Both enzymes were free of pectinase and xylanase activity and released ferulic acid from methyl ferulate. In association with a xylanase, they also released ferulic acid from destarched wheat bran. Ferulic acid esterase II released a small amount of ferulic acid (0.09 unit/mg of protein) in the absence of xylanase. The enzymes had different specificities for a range of methyl ester derivatives of cinnamoyl and benzoyl acids, acetylated xylan and p-nitrophenyl acetate.
ESTHER : Faulds_1993_Biotechnol.Appl.Biochem_17_349
PubMedSearch : Faulds_1993_Biotechnol.Appl.Biochem_17_349
PubMedID: 8338641

Title : The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes - Faulds_1991_J.Gen.Microbiol_137_2339
Author(s) : Faulds CB , Williamson G
Ref : J Gen Microbiol , 137 :2339 , 1991
Abstract : A 4-hydroxy-3-methoxycinnamic acid (ferulic acid) esterase has been purified from the extracellular broth of cultures of Streptomyces olivochromogenes after growth on oat splet xylan. The purification procedure utilizes ion exchange on DEAE-BioGel A, anion exchange on Mono Q, gel filtration and hydrophobic interaction chromatography. The purified enzyme appeared as a single band on SDS-PAGE, with an apparent Mr of 29,000. Two bands, at pI7.9 and 8.5, were observed on isoelectric focusing. With methyl ferulate as substrate, the pH and temperature optima were 5.5 and 30 degrees C respectively, with a Km of 1.86 mM and Vmax of 0.3 mumols min-1 mg-1. The purfied enzyme released ferulic acid from de-starched wheat bran only in the presence of xylanase.
ESTHER : Faulds_1991_J.Gen.Microbiol_137_2339
PubMedSearch : Faulds_1991_J.Gen.Microbiol_137_2339
PubMedID: 1663152