Feruloyl Esterases: Biocatalysts to Overcome Biomass Recalcitrance and for the Production of Bioactive Compounds Dyoni M

Feruloyl esterases: Biocatalysts to overcome biomass recalcitrance and for the production of bioactive compounds Dyoni M. Oliveira, Thatiane R. Mota, Bianca Oliva, Fernando Segato, Rogério Marchiosi, Osvaldo Ferrarese-Filho, Craig Faulds, Wanderley D. dos Santos

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Dyoni M. Oliveira, Thatiane R. Mota, Bianca Oliva, Fernando Segato, Rogério Marchiosi, et al.. Feru- loyl esterases: Biocatalysts to overcome biomass recalcitrance and for the production of bioactive compounds. Bioresource Technology, Elsevier, 2019, 278, pp.408-423. 10.1016/j.biortech.2019.01.064. hal-02627378

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Distributed under a Creative Commons Attribution| 4.0 International License Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 rdcin f iatv compounds, bioactive of production Biocatalyst esterases: Feruloyl W.D., Santos, dos C.B., Faulds, Oliva, T.R., Mota, D.M., Oliveira, as: article this cite Please 16January2019 January2019 14 12December2018 Accepted Date: Revised Date: Received Date: To appearin: Reference: DOI: PII: Marchiosi, Osvaldo Ferrarese-Filho, Craig B. Faulds, Wanderley Dyoni M. Oliveira, Thatiane R. Mota, Bianca Oliva, Fernando Seg production ofbioactivecompounds Feruloyl esterases:Biocatalyststoovercomebiomassrecalcitra Review Accepted Manuscript errors maybediscoveredwhichcould affect content,and the l legaldisclaimers al that apply to the journalpertain. production process during the form. Please notethat final review oftheresultingproofbeforeitispublishedinits manu The manuscript. the of version early this providing are we acce been has that manuscript unedited an of file PDF a is This 2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos Bioresource Technology https://doi.org/10.1016/j.biortech.2019.01.064 S0960-8524(19)30077-X BITE 20941 Comment citer cedocument: Bioresource Technology

B., Segato, F., Marchiosi, R., Ferrarese-Filho, O., Ferrarese-Filho, R., Marchiosi, F., Segato, B., nce andforthe pted for publication. As a service to our customers our to service a As publication. for pted s to overcome biomass recalcitrance and for the for and recalcitrance biomass overcome to s D. dos Santos (2019), doi: script will undergo copyediting, typesetting, and typesetting, copyediting, undergo will script ato, Rogério https://doi.org/10.1016/j.biortech. Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos Saccharification. Keywords derivatives of industrial interest. for as as well lignocellulosebiomass treatments aiming of forproduction bioethanol andother a microorganism’senzymatic wall-degrading plant cell arsenal responsible molecularof weight low phenolic compounds biomass. inplant Feruloylare of esterases part hydroxycinnamate acidandits Ferulic derivativesrepresentoneof most the abundant forms Abstract Av. Colombo, 5790, Zona 7, Jardim Universitário, Bloco I *Corresponding author: 1 France c Brazil b a biotechnologic This to furtherbiotechnological reviewcontributes applications. structural, functional, and according andorganized totheir function, biochemical properties, substrate specificity, content encoding for several esterases. systematically about enzymes feruloyl is Information basicknowledgethe and biotechnological recent advancesin genecharacteristics the and valuemolecules. to plant biomass biosynthesisofhigh-added and conversion repurposedimprovement dedicated effortshavebiocatalysts made been identify,createand to requirements,industrial scientificdiscoveries accelerating andcontinuous knowledgetransfer, hydroxycinnamatesStimulated wall-bound by insoluble cytosolic soluble conjugates. and

Aix DepartmentBiochemistry, of State University Maringá, of Maringá, Paraná, Brazil The authorsThe contributedequally DepartmentBiotechnology, of Feruloyl esterases: Biocatalysts to overcome biomass recalcitrance and for for and recalcitrance toovercome biomass Biocatalysts esterases: Feruloyl - Marseille Université, INRA Dyoni M.Oliveira

Marchiosi

: Biorefinery; al R&D both R&Dhydroxycinnamates al forobtaining from by-products agricultural a , Osvaldo Ferrarese-Filho DMO ( the production of bioactive compounds compounds bioactive of production the a1* Comment citer cedocument: Carbohydrate esterases; Carbohydrate esterases; , Thatiane R. Mota Engineering School of Lorena,

[email protected] UMR 1163 Biodiversité et Biotechnologie Fongiques (BBF)

a , Craig B. Faulds , Craig a1 , 1 1

BiancaOliva - Cell wall; Cell wall; 89, ZIP 87020 ); WDS ( ); WDS University of SãoPaulo, Lorena, SãoPaulo, [email protected] Genome c b , WanderleyD.dos Santos , SegatoFernando - 900, Maringá, Paraná, Brazil

mining; Lignocellulose;

)

for cleaving Here we review , 13009 b , Rogério

Marseille,

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos are able toneutralize free protectingare cell radicals, ( membranes andDNA Information about severalenzymesInformationabout systematicallyorganized is according function,to their in advances comprehensive mining biotechnological and about biochemical characteristics. 2015). ( Carpita, cross-linking and McCann hydroxycinnamate-hemicellulose content composition, lignin and occlusionof the bylignin- cell wall the organization ofcellulosemicrofibrils, hemicellulose polymerization and substitutionpattern, energyi additional architecture and oilinreplace the potential materialraw hasthe toproduce and in nature biofuelsonascalelargeenoughto recalcitrance tohydrolysis, wherefore lignocellulosic biomassmost isthe abundantrenewable FAEs forlignocellulosic biomass keyrole deconstruction has a indecreasing biomass the wall thecell polymers. thebiomass Therefore, cross-linking recalcitrance, application of extensively investigated ( microbialthe biotransformation tovanillinmajor ofFA (a aroma) foodindustry hasbeen guaiacol; offlavor aprecursorforsynthesis compounds,andis also suchasvanillin 4-vinyl antidiabetic effects; andasasunprotectiveand neuroprotective factor.F antimicrobial antibacterial, therapeuticagent,includinganti-inflammatory, properties; as a ( hydroxycinnamic acids to tools catalyzebiosynthetic of esterification esters ofand transesterification bioethanol production, improving the of digestion forage forruminants,as plants and delignifica andsubsequent bioconversion biological tohighaddedaromaticwastes value compounds, applications,with many as:obtaining such FAfrom biotechnological by-product agricultural plant walls, cytoplasm FAEs synthetic substrates. arefoundinbacteria,fungiandplants, and capacity ferulicthe to release acid(FA) hydroxycinnamic andother from cell acids plant due architec 1.

to the to the factorsaccessibilityseveral cellulosecrystallinity,and suchas, polymerization, the Introduction This research review des review This research Biomass recalcitrance is mainly wall derivedfromcell composition plant the and acid(FA Ferulic (FAE;Feruloyl esterases EC3.1.1.73)are acidesterasesa subclassofcarboxylic with ture providesof ture lignocellulose convert cellulose abarrier into to fermentable sugars, tion of non-woody plants enzymatic industry, tionfor thepaper plants for of hydrolysis non-woody it mid-term ( is conferred bydifferentis interactions among nputs for their disruption nputsattack fordisruption (M their Comment citer cedocument: ) has applications applications as afooddueantioxidant) has toits preservative and Furuya et al.,Furuya et 2017 Furuya et Furuya et al., 2017 Linh et al.,2017 Linh et cribes fundamental current cribes the knowledge andrecent

; ). FAimportant). isan for factor lignocellulosic ; Gopalan et al., 2 Gopalan etal., Mota 2 2 etal.,2018 cCann and 015 ). its

; Carpita, Thecomplex 2015).

components, requiring Oliveira et al., 2017Oliveira al., et ). A Paiva et et Paiva al., 2013 and its derivatives derivatives and its

). It ).

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos differ the — ester-linkedcell andFAoccursin Caryophyllalesat bromeliads, ‘core’ wall gingers, covalentl pla sunscreen and ( antioxidant inplants and pharmaceutical products conserving the resonating radical among theirchemical thisa linkages. For itworksas reason, chain by afree reactions releasing radicalispositive, phenylpropanoids freeradical stop peroxidases andotherchain, metabolic( activities toelectron)byUV-light, produced molecule stabilize respiratory afree radical (non-paired phenolic and other compounds, structure FApresentsapolyenic(conjugated) that allows the ( biosynthesis andasfinal ofthepathway products intermediaryboth as metabolites towards formation the during lignin monolignols of phenylpropanoidProduced viathe pathway,FA canbeseen andits ester of CoA,FA-CoA, hydroxy)-3 acid Ferulic inplant 2.1. cell wallsand biomass recalcitrance and peroxidases 5-5’ thatactonFAand (e.g. by specific to produce esters dehydrodimers efficiency( hydrolysis can the ofblock attack cross-linkages reducing hydrolases, polymers. Such enzymatic withligninor ether-link dimerize withotherFA-arabinoxylan, cross-linkingcell these wall ( other backbone) than andis xylopyranosyl arabinoxylanmore abundant (β-1,4-linked groups hydroxylof of group FAis thearabinosylincluding intheC-5 residue grasses, the esterified tissue, as summarized in ( 2. saccharification of biomass. lignocellulosic andobtainment improved ofhydroxycinnamic acidsfrom by-products agricultural biochemical andstructural evaluation, asbiotechnological aswell applications ofFAEs tothe functional, substrateFAEs andtheir relationship may instrument for powerful further bea mapping We thatthis biochemical believe kinetics, of properties, andspecificity. substrate Oliveira etOliveira Dupree,2019 & Terrett

nt cell walls, FA plays a key role in inter- and may walls,intra-polymer cross-linkage.nt cell It be FAplays also akeyroleininter- ent and high concentrations mg/g andhighconcentrations (>3.5 ent In commelinid monocots— acidisahydroxy Ferulic acid:Ferulic apolyvale y linked to lignin through the ether or ester bonds and esterified to polysaccharides y linked and topolysaccharides theetheroresterbonds esterified toligninthrough -phenyl-2-propenoic acid ( or3-methoxy-4-hydroxy-cinnamicacid al., 2015 al., ). FA). the ester-linkedto arabinosyl residueof is arabinoxylan able to Oliveira etOliveira al., 2015 Comment citer cedocument: ). Table 1

cinnamic systematic acidwiththe name (3-methoxy-4- nt molecule nt molecule .

In the primaryIn the walls of cell commelinidmonocots, a group a group of palms, angiosperms grasses, including

). ). The production of FA cross-linkages is catalyzed ofThe production is FA cross-linkages

cell wall) according wall) cell 3 3 Bento-Silva et al., 2018 Bento-Silva etal., Oliveira etOliveira 2015 al., to the specie, organto the specie, and dos Santos etal., 2008 ). Like). monolignols ). for AstheΔG Fig. 1

A ). ). In ).

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos Staphylococcus aureus microorganisms as such and intestinal disorders with antibioticscan synergistically inthe treatment act ofpathogenic al.,2006 et organismthe ( side against effects (abdominal discomfort), whichlimit treatment the toenhance natural capacity immune defensesand gastrointestinal movement, tract protecting FA hasbeeninvestigated adjunct administrated asan in cancer chemotherapy duetoits ( antimicrobialand its activities with effects and against yeasts bacteria its FAeffectsactivities of protective hasdemonstrated againsttumor factor (TNF) necrosis ( countries insomeadditive amongothers. food For that reason, FAisapopular cholesterol-lowering, anti-inflammatory,carcinogenic, antioxidant,antimicrobial, antiviral, anti-allergic, and to toxicity the variety organism broad properties: andshowinga ofbiomedical anti- mgfrom low 180to165 in its ofFA,which ispresent conjugated and freeforms, having physiological concentration andpharmacokinetics. Generally, given ina meal, ingest people potential ferulic Pharmaceutical of 2.2. andderivatives acid ( bioethanol polysaccharideswall for biomass hydrolases, byto alimitationglycosyl conversion arabinoxylan isthe ofrecalcitranceincrease with of consequent reduction digestibility ofcell acce toarabinoxylanesterified affects wall manysuch cell properties, asadherence, extensibility, al.,2015 et arabinoxylans linking tobyforminglignin complex ( lignin–ferulate–arabinoxylan a because ferulatemaybut also for as act anucleating formationsite andhencethe lignin, of of isimportantarabinoxylaningrasses, arabinoxylan notonly itleadsbecause cross-linked to conversionwall andnegativelyim 1999 8 - -4’-dehydrodiferulic acid) cross-linking vicinal arabinoxylan ( O-4’-dehydrodiferulic acid) cross-linking ssibility andbiodegradability ).

Lignin polymertoefficient Lignin ofbarrier cell plant tissues imposes andferuloylation a Due to the observed properties,Due tothe anextensivefunctions study of biological andrelated The therap Cross-linking ofgrasswall cell especiallythrough components, FAanddiFA Srinivasan et 2007 al., ). Inaddition, increase the of promotedmotility intestinal byFA some inhibits ; Oliveira etal.,Oliveira 2015 Terr ett ett eutic effect and efficacy onsome ofFAas dependent such are properties & Dupree, 2019

and Comment citer cedocument: Escherichia coli, Lysteria Lysteria monocytogenes ; ). Perez-Boada etPerez-Boada 2014 al., .

pacts digestibility ( digestibility pacts An of consequenceof additional diFAcross-linkages

Helicobacter pylori 4 4 .

Ponnusamy 2019 etal., ) .

, Pseudomonas aeruginosa Fig. 2 Borges et Borges et al., 2013 ) ( Hatfield & Hatfield & R ). ). Feruloylation

Oliveira Oliveira Badary alph, alph, , ). ).

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos thera ( of synergistically interacts FA,which with someusedinthetreatment drugs ofdiabetes dismutase These catalase. resultscorrelated and superoxide are withthe antioxidant capacity and glucose thiobarbituric acid-reactivesubstances, increases andalso the of action bymacrophages.produced Diabetic supplementedrats FA with showedin areduction blood Sompong 2017 etal., DNAthe damage improvement( tothe performance due inantioxidant intubation viaintragastric rats increases protection against lipidperoxidation anddecreases (CE1) within the Carbohydrate-Active Enzymes (CAZy Carbohydrate-Active database (CE1) within the in – www.cazy.org), 3. ( andtransferase superoxidedismutase apoptosis and in components, alteration keyantioxidant suchasglutathione, glutathione S- Asparasites. animportantfunction, microfilaricidal activity inducedbyFAculminates in mixed capacities,FA hasinducing in antioxidantmechanisms apoptosis andpro-oxidant ( drugpackages to produce viscositythe ofpolysaccharides to obtain gels,andcanbe it intomaterialsincorporated used preserving oranges,stabilizingsoybeanoil, theoxidation and inhibiting ofbiscuits, increasing natural as a preserves uses,compound diversified foods,soithasvery that including in maize. that,FA Besides showsthat inhibits thegrowth activity microorganisms of andacts dehydrodimers may graminearum Fusarium against beused together insolubilitywall of with dietary compounds,andcanbeusedfibers. incereal FA ( treatment ofmooddisorders in brain promotesneurotransmitter the and vasodilatation that beneficial forthecan be Additional demonstrated has work thatmonoamine FAincreasesthe levels of intestinepancreas, andliver( byreducing inflammationoxidative and stress positive bacteria by changing cellmorphology andmembrane permeability withstreptomycinapplied in consort and Gram- against bothpathogenicGram-negative Nankar et AnimportantNankar al.,2017). function ofFA asprotective, wasobserved showing

peutic onnephropathyaction andprotective effectsbrain, inorganssuch as the kidney, Currently, classified the knownFAEsare the into EsteraseFamilyCarbohydrate 1 Classification FA exhibits FA exhibits decreasinganti-inflammatory thelevels ofcompounds properties,

The phytochemical-antibiotic combinationeffectwhen assays showed asynergistic In foodscience,FAhasmuchdue intrinsiccharacteristics utilization to its cell in the ). ).

of feruloyl esterases and genomeanalysis of feruloylesterases Comment citer cedocument: Silva Silva & Batista, 2017 Chen et 2015 al.,

Saini et al.,Saini et 2012 5 5 ). ). ).

). Theadministration ofWistar). FAin , a fungus accountable for , afungusaccountable disease Paiva et 2013Paiva et al., ( Ren etal., 2017 Shi et Shi et al., 2016

; ). ). ). ).

L. acidophilus L. acidophilus RaXynB. Nevertheless, members of this sub-class may identifiedbasedonly be RaXynB. members sub-class ontheir Nevertheless, ofthis ent classification systems have been proposed for FAEs. In this article, Inthis wereviewedFAEs. systems classification ent beenproposed for have ined biochemical andfunctional andsequence characteristics similarities ined ( According toCrepin’sAccording classification, FAEssequencesby aminoacid beclassified can The Crepi As a further refinement for FAEs classification, Benoit and coworkers provided an As afurther FAEsclassification, refinementfor andcoworkers Benoit classification, to According Crepin’s phylogenetic the analysisthatsome alsosuggests bstrates, andbstrates, amino homology, sequence whichalso the indicates acid ty forsynthetic substrates containing hydroxycinnamic(methylmethyl esters ), ability t ), ability n’s classification system is based in n’spreviously based thecorrelation classification system between is oup – e.g.PeFaeAfrom– oup d on the phylogenic analysis genomic phylogenicanalysis the of sequences knownfungal d on F46 the is classified into putative E,indicating functionaltype thatthe Comment citer cedocument: o FAdehydrodimers release (especially, 5,5’-diFA, p -coumarate – MpCA, methyl caffeate-coumarate– MpCA,methyl XynZ, Ruminococcus

Kim 2015 &Baik, Crepin 2004 etal., Pleurotus eryngii Pleurotus 6 6 Benoit etal.,Benoit 2008 sp. RspXyn1, ).

Orpinomyces

and AnFaeAfrom This classification hasbeen Lombard al.,2014 et R. flavefaciens MCA, and methyl sinapate – methylMCA, and sinapate ). ). Based onBenoit’s

sp. OspFaeA, Fig. 2

RfXynE and A. niger Crepin al., et ) from

acquired acquired ) . .

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos heterologously expressed andcharacterizedWhile soon. some fungi, as such genes thus farencoding have beenidentified in fungi,whichwill allowmoreFAEs tobe FAE- amultiplicity genes.Multiple predicted organisms ofputativeenzyme-encoding contain bacterial demonstrating groupingboth thelimitationsandfungalFAEs in together. latest proposedtogether classification,In this are withan 13sub-families unclassified group, consideringfungal FAEs bothphylogeny( andsubstrate specificity actual FAEs. corresponding biochemicalwithout confirmingdata that thesesequences do correspondto only and soasequence-based proteases classification lipases,and is difficult to predict identity proteases,FAEs ahighsequence withother serine share asacetylesterases, such a applying combination of with prediction tools experimental data. fromThe 12proposed amino werederived families sequence. therespective validated acid composition, proteinstructure, secondary andphysicochemical composition descriptors and plant 2011 al., valuemolecules throughhigh-added ( esterification andtransesterification reactions ofcapability onabonds acting ester cleaving large range and synthesizing of substrates for the andplant.Theclassification 12whichhave bacteria resultedin families, distinct classificationnovel system,– forfirst time grouping the from FAEskingdoms three subfamily 2,while verydistant 7is from other allthe subfamilies. the includes FAE genefrom from genes The these haddataset FAE same access authors to. for almost is subfamily true contains 1that re is characterization of AtFaeDfrom anovel subfamilies, upgrade this classification inthe last system with able the was identification and five into performedphylogenetic that divided analysis fungal FAEs a membersCE1 family of ( CE1 familyof CAZydatabase according classification, grouped to only this in 5and6are somefrom sub-families FAEs Members genus the of thoseB andC), classified excluding esterases previouslyas type Dandall bacterial FAEs. stricted FAEsfrom genes to With of microbial expansion genome the it has sequencing, beenrevealed that for Recently, andthe ofdeVries haveproposedanotherclassification groups Hildén proposing a Udatha and extendedtheby coworkers further classification ofFAEs ). ). origin collected were andclustered groupsinto distinct basedon amino acid In thisclassificationsystem, FAE-relatedsequences 365 putative offungi, bacteria A. fumigatus, A.niger, oryzae Aspergillus Comment citer cedocument: Talaromyces Udatha al., More et 2011). recently, samethe groups research A. niger

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O k m la cat -β-D-xylopyranosyl-(1→4)-D-xylopyranose) ( -β-D-xylopyranosyl-(1→4)-D-xylopyranose) and -Peña & -Peña

and

p ) k . Asystem -coumaric, sinapicor caffeic from acids esters. their cat k Fig. 3 Fig. cat

is correlated with decreased with is correlated substrate polarity for Contreras-Esquivel, 2016 Contreras-Esquivel, / K m C

( 9 9 Table2 , FAEs are optimally, FAEs atpH6.5, are active

atic evaluationatic ofFAEs from oftheactivity ) are differencesaffected) are bystructural ). Numerous). model n O- -alkyl ferulates was [5 - O -( trans Hunt et al., ( Udatha et Udatha

O -feruloyl)- - Hunt et [5 Udatha - O n - -

, and expressed in active form( P. pastoris s of disulfide bridgess ofdisulfide onthe thermostability offrom AuFaeA Increasing Increasing the repertoireWu ofclonedFAEs, colleagueswith performed and studies Using a Most well well heterologoushosts Most characterized in FAEs beencloned and expressed have ized metalized ionaffinity chromatography, followed by a size exclusion Yin etal.,2015a C. thermocellum C. thermocellum ngle stepngle yieldandspecificwith high activity (for example, an P. pastoris , and ntrated enzyme andthe chromatography, bygel filtration waspurified E. coli ; Zhang A. niger

A. niger A. Comment citer cedocument: Damásio al.,2013 et BL21 (DE3) as a soluble fraction and purified by two steps — BL21 (DE3) first, asoluble fraction as andby purified two steps

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Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos AnFaeA, it was shown that the OH the andAnFaeA, wasshownthat it OCH phenolic ring ofthehydroxycinnamates withthe withintheactiveof residues site FAEs.Fo th improvem re 2012 al., ( phase substrates the siteopen conformationinto active accommodatethe FA-type in to aqueous enzymelipase, the FAE suggesting significant activity, obtained that the mutant adopted an mutationa Phe toIle ona wascorresponding residue in constructed aswell( as been foundforlipases, influencing its optimum pH substratethe naphthyl discriminationchain ashas towards ofesters, esterase long-acyl this especially a Pheormutation,Tyr to Ile the changed hydrophobicity of hence the and region from of Mutationsinthelid/flapofspecificity thisesterase. region AwFaeA with smaller residues suchasvalineor resulted serine broadeningofthe in a substrate as binding, measured by active siteofAnFaeA investigated, itwasshown was these that residuesare involved in ( Tyr80 improvem ofmin °C (39.8inWT), a 198 half-life 50correspondingto the 3.96-fold at °C, Inaddition,the correspond to shown 20°Cand25 higherthan that wild-type. bythe an increase in optimal the temperatures 60°C(mutant to M6), M4) and 65°C(mutant which ( improved bytworoundsofmutagenesis random ( fromefficiently bran wheat low thermostabilitydisplays temperaturesat 50°C higher than to butwasable release FA bond disulphide andageneral increase hydrophobicity of in protein. the mainlysubstitutions, with associated dimer the interface, theleading to formation of anew 50 °Cwas i ofdirectedtwo rounds evolution,AnFaeA. thermostability After the ofthemutated EstF27 at enzyme 2015b sidues in AnFaeA, four being surface exposed and eight being surfaceeight and the being sidues inAnFaeA, exposed in inner partofthefour ermostable at 32minwild-type 50 of than °C with ahalf-life 82min. longer ). The study revealed that revealedproduced Thestudy that best). the variant Ser33E/Asn92-4 Andersen et 2002al., The substrate specificity interactionof thesubstitutions between FAEonthe involves Directed evolution Directed was ( applied to improvethermostability the of AnFaeA The EstF27 isolated fromThe EstF27isolated metagenomics asoil overexpressed and in library Faulds al., et 2005 , were i , were )

and dimeric the ( EstF27from metagenomics asoil library ent compared to the wild-type. Further, was bestSer33Further, the variant Ser33-6 wild-type. compared the to ent ent of FA release from wheat bran was obtained as a result of six ofFAwas bran releasefroment obtained as aresultof wheat mproved over 3000-fold, and a 1.9-fold higher 3000-fold, catalytic anda1.9-fold efficiency anda2-fold mproved over dentified directedafter evolution tobebeneficial to the thermostability of Comment citer cedocument: K ). W ). m , but also the specificity,replacement as the , butalso Trp260 ofTyr80and ). ). Sang etal.,2011 hen the importance ofthepolarandaromatic residues inhen the the

3 ). F ).

11 of FA interact FA interact hydroxylof groups with the urthermore, EstF27 haditsthermostability Cao etal., 2015 Koseki et Koseki et al., 2005 ). The mutations promoted Themutations ). Thermomyces lanuginosa Cao et 2015 al.,

a amino acid A. awamori T m

value of44.5 value ). When). a

Zhang E. coli E. coli ) . Twelve , et et r

 M. -helices twoadditional and insoluble esters, releasing long-chain fatty esters, insoluble whereasreleasing long-chain acids, esterases onwater-soluble act

Only a few crystal structures ofFAEscrystal Only afew havebeentodate,whichmakes solved our Some andstructures have sequences FAEs related tolipases, showing the same serine Three-dimensional structures ound sequence Itisound identity tolipases crystal sequence where structurewasunavailable. thermophila, ). are Lipases lipolytic carboxyl ester hydrolases ability tohydrolyzewith the ). Ontheotherhand,unlike FAEs,twoconformational states lipasesshow with an in open its conformation linkedwith the catalytic respective substrates inthe cleft y ofM6 remained(100%), whereas constant onlyresidual activity remained ), each fold ), displayingcanonical α/β the eight-strand of lipases/esterases. 

followed with screeningforfollowed with their variants selecting higher the with /  Comment citer cedocument: -hydrolase fold, of-hydrolase consists nine which

XynY  Fig. 4A-C Fig. -strands ofenzymes-strands indicative ofhydrolyzing capable and XynZ were the first to be solved the ( and XynZwere first to besolved

Varriale al.,et Varriale 2018

Romano al.,2015 et ). Many FAE models beenMany FAEhave ). constructed 12 A. ) )

niger Levasseur al.,et 2006 ).

with a lipasewith a from  -sheet -sheet core surrounded by

k cat / K m value ofM6atits value Prates et Prates et al., 2001 Fig. 4 Fig. -throughput

shows the shows the

; T. McAuley

;

otein Dataotein Bank  -hydrolase aninterface fold, andin these between domains andthe lid domain, theactive ; McAuley et et 2004McAuley al., It is desirable that isdesirablethat in It enzymes used industrial processes resist non-physiological The three-dimensional structureofAoFaeB from The classical catalytic The classical catalytic atthetriad coreoftheactive of sites these twoesterases and Identification sites ofglycosylation ) . The domain lid contains acalcium andcoordinated by water fiveamino acids ion Topakas et al.,2012b Topakas et ) and ) and lidthe domain whichcoverstheactivesite ( ).

Fig. 4 Fig. ( Suzuki et al.,2014Suzuki et ) Comment citer cedocument: were identifiedhydrophobic( the binding in pocket ; Uraji et Uraji et 2018 al., se exists motifse dimer, exists asa atthe novelCS-D-HC a contains ). ). While MtFae1 resembles lipases,theWhile of MtFae1 resembles structure

solid circle insolid 5 Fig. ).

). In biochemical). addition, studies displayed the 13 A. oryzae A ). Thecatalytic domain shows Fig. 5 blue5 Fig. region Fig. 4 Fig.

is composed two of ( ). Presenting a unique Faulds etal.,2005Faulds Hermoso et Fig.

) ( Suzuki et Suzuki et A. oryzae 5 A al., al., ). ).

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos glycosylation ( glycosylation temperature (melting point coli of52 °C)recovered byinclusion bodies andrefoldedwithout 1997 carbohydrate additional attached theresidues to AnFaeB has18 ra ( structure glycosylation inits SDS- proteins, showing ap protein band of35TheAnFaeAand kDa. purifiedthe protein endo-β- treated with ( 46 and49potential potential AtFaeA from enzymedeglycosylated 60kDa bySDS-PAGE. presents removed thepurified using PsEst1 from endo-β- sequenceacid of analysis fourpotential PsEst1 reveals mass,molecular which was 59.4kDa,asshownin sapidus ( residue or one(generally groupofaserine threonine tothree mannose totheβ-hydroxyl residues) amide residue, group ofanasparagine while mass molecular the estimatedhigher than 6kDacalculatedmolecular bySDS-PAGE mass of protein linkedglycosylation pattern toAsn79. Themature n glycosylated, non native, refolded, AnFaeA. thermalof — molecular stability The forms four AnFaeA of chaesterase inan thus an regionstabilizes theopenconfiguration, conferring theesterase this 'lid' of genera often covalently Zhang et al.,Zhang et 2015 iger iger ises the question ofthe of actualises the importance in thermal of glycosylation the stability ; PA (melting temperature point of56 more AnFaeA °C)is heat resistant than in produced McAuley et McAuley lly attaches abranchedlly asingle mannose or The cr The of investigation In an theeffect ofglycosylation on protein mass,interestingly, PsEst1 band presents aprotein inSDS-PAGEthanthetheoretical 10kDahigher GE indicates anapparentGE indicates molecularmass ahigh of36dueto amount kDa, of Zhang al.,2015 et N -glycosylation sites and53 potential N racter rather( racter lipaseactivity aninterfacial-active than -glycosylation site -glycosylation withthehighratioin AnFaeAcoupled in ofpolar residues ystallographic structure ofAnFaeAformystallographic native inits afungal revealed Benoit etBenoit 2006a al., N N -glycosylated —was evaluated, -glycosylated demonstrating AnFaeA that produced in -glycosylation sites and the electron-density indicatedno maps sites region -glycosylation electron-density and the this in 2004al., -linked and ). SDS-PAGEbands). of 40 protein AtFaeAaround and37kDa, have O I -glycosylation of sites of 3.3andmolecular mass of28proteins. kDaforboth However,the Comment citer cedocument: ). ). ).

de al., Vries et 1997 O -linked to glycosidessites. -linked to atspecific ). ).

N -acetylglucosaminidase amajor Hresultedin A. tubingensis A. flavus O 14 -glycosylation attaches-glycosylation carbohydrate the O N- N -glycosylation sites,which ismore the -glycosylation than ; -acetylglucosaminidase H,the N acetylglucosamine residue ( acetylglucosamine residue Table3 Faulds Faulds -acetylglucosamine residue -acetylglucosamine residue tothe β- AfFaeA and AnFaeA, respectively AfFaeA respectively andAnFaeA, N

-glycosylation sites-glycosylation that after being AtFaeA

& Williamson, 1994 NcFae-I of

( ). Theamino etal.,2016). Kelle enzymes are veryacidic enzymes are Hermoso al.,2004 et N. crassa N A. terreus -glycosylation de Vries al., et ). Theenzyme).

contains a

has two

N ). This P. - A. E.

. The A studydescribing novelfrom a feruloyl esterase

) an ).

N A. oryzae -linked glycosylation motif (Asn79-Tyr-Thr) was of sequence FAEs-linked glycosylationmotif(Asn79-Tyr-Thr) foundinthe d ApFae(from N N A. flavus -glycosylation is important forthethermostability isimportant -glycosylation and protein foldingof the -glycosylation wasconfirmedspectrometry, ionization-mass byelectrospray

enzymes, apparent an AoFaeBandAoFaeC, relative have molecular Topakas and Topakas and MtFae1 from Comment citer cedocument: ) ) and Benoit etBenoit al.,2006a N P.purpurogenum , similar A. pullulans -glycosylation recognition sites present are in AoFaeBthe and A. awamori ) of esterasesShin and) feruloyl AN1772.2(from Chen(2007 Koseki et2009 al., to resultsforan the reported FAE of coworkers (2012b didnotconfirm) coworkers glycosylation the of

Oleas etOleas al., 2017 ). The AN1772.2 glycosylated containedmore). TheAN1772.2glycosylated than

expressed in

M. thermophila, M. thermophila,

and Dilokpimol 2017 al., et ). Underst ). 15

as anoligosacchari Crepin et et Crepin al., 2003a P. chrysogenum ( Crepin 2003b et al., ) . Previously,Koseki andcolleagues also P. pastoris. Table 3 ; anding role of the Sakamoto etal., 2005 A. niger but compared with theoretical it the -deglycosylation, both proteins both -deglycosylation, ).

, AnFaeC,unlike that found , respectively, The analysis ofremoved de anda acceptor )

). Incontra ). . AnFaeB andTsFaeC ; A. niger A. Garcia

N N -linked -linked -glycosylated. ).

-Conesa et al.,et -Conesa

st, the showed slight Zhang

( Koseki et

and A. N -

ds, such ds, such as FA, ). K

m Monomers and dimers of FA are important structural componentsstructural Monomers ofcomplex plant anddimers FAareimportant of Faulds and coworkers were able andcoworkers were to Faulds release hydroxycinnamic from acids spent brewers' Somemicrobial FAEs dehydrodimers release can and,therefore, potentially break FA plantReleasing cell walls from and FAdehydrodimers

0.28 mM 0.28 and Oliveira al., et 2016 p ). Both mutant Bothrate ). enzymes a decreaseinhydrolysis significant exhibited -coumaric, and caffeic acids from coffee pulp, maize bran, apple caffeic from-coumaric, acids and marc pulp,maize coffee and bran, Humicola insolens udied the ability torelease ofAnFaeAandAnFaeB hydroxycinnamic k Comment citer cedocument: cat / K eases 100% 83% and ofcaffeic from acid pulpand coffee apple m

P. fluorescens P. fluorescens 73 s K m 0.66 mM 0.66 and - 1

mM ). Specificcell ). commercial enzymecontainingFAEactivity, cocktail

-1 p -coumaric acid, respectively,-coumaric while AnFaeA does . These data suggest that the glycanthat the suggest . Thesedata chains affect Pf 16 XylD andAnFaeA, alone concertwith a or in K k cat m of 0.26 mM and mM and of 0.26 p / K -coumaric, 5,5’-diFA and8- -coumaric, wall degrading enzymes as such m

145

s - 1 mM -1, -1, Faulds et al., 2004 Faulds etal., k and mutantGln79values cat / K m of 588 O (

Long et al., et Long s -4’-diFA, -4’-diFA,

- 1 mM ).

-1 ,

). ) . The type of xylanases used . Thetype used ofxylanases inwithFAEs thesynergy affects level and form ofFA

The maximum bioconversionoflignocellulosic material the requires action ofefficient FaeLac from The degree The degree of orsynergism oftwomeasuresmore synergy ability the or enzymes to betweenSynergism andhemicellulases FAEs

is able to is ableto release FAand y using EstF27 from the soil metagenomics EstF27soil thermostable y using and EstF27 from library the 5′ Lactobacillus acidophilusLactobacillus Damásio al., 2013 et -diFA and8- Comment citer cedocument: ; etMandalari al.,2008 p -4’-diFA from andwheat cell barley ( O-4’-diFA walls Braga 2014 et; al., -coumaric acid from biomass acid insoluble-coumaric and sugarcane

). Theenzymatic). of hydrolysis wheatarabinoxylan p 17 Segato et al., 2014 -coumaric acid and 2-fold more-coumaric acid FAthanTRA, and2-fold K1 Dyk &Pletschke, 2012

hydrolyzes brewers'spentgrainand Szwajgier et 2010al., Li et Li et al., 2014

Jia etal.,2015 ; Xue et al., 2017 Xue etal., ).

). Thesynergism is ). ). AcFaef ). Faulds etFaulds al., p

FAEs exhibit FAEs exhibit -coumaric acid Faulds etal., See Fig. 2

). ). FAEs rom A. ).

AnFaeB increased Topakas and coworkers observed the maximal release ofTopakas and theFA(33%ofTRA) from coworkers maximalobserved release by AnFaeA xylanase. released plus FA isefficiently preparation bran from awheat The addition ofRuFae2 mixturesofendoxylanase GH10 reaction in from gosaccharides. and β- gosaccharides. The incubation ofwith arabinofuranosidase AnFaeB T. reesei leased 1% FA from sugar-beet pulp,while additionofarabinanasethe and leased 1%FAfrom sugar-beet FaeIII. and from to H1, FaeI,FaeII Theadditionof FaeII xylanase FaeI ut they haveut they preferencesfor polysaccharides opposite ( these osidase (Kroonand osidase in themixture reaction improved release of the FAto12% al.,2010 Topakas et al., 2004 Topakas etal.,

reased 37% 27%, and respectively, amount the released ofreducing sugars is mo ying 0.4U/g of 6.7 and -fold release from the ofFA and2.7-fold wheat- fromwheat bran st A.

) Comment citer cedocument: active towards sugar-beet pectin, whereas sugar-beet AnFaeApectin, active towards ismo . Wong et

A. awamori awamori T. viride T. viride Debeire etal.,2012 reported production ofthree the FAEs from M. thermophila Wu al.,2012 et al., 2013 A. niger A.

). ). efficiently hydrolyzed steam-pretreatedhydrolyzed sugarcanebagasse efficiently

xylanase demonstratedxylanase that 3hofresulted hydrolysis in a E. coli

produced FAE,synergisticallyproduced with whichacts ). ). ) - increases the hydrolysis of sugar-beet pectin, increases hydrolysis of the sugar-beet expressed Zhang et al. al. (2015Zhang et 18

). Theexperim ). Mt ).

Fae with 500 U/g xylanase within Fae with 1hof500 U/gxylanase S. cellulosum de Vries et de et Vries al., 2002 ) ) ents with0.45U/mlents ofScFae2 conducted a thorough study conducted athorough study

ScFae1 and ScFae2 were ScFae1 andScFae2were de Vries etal.,de Vries Cellulosilyticum Cellulosilyticum ).

st Cellvibrio

active in active in T.

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos 10. mixtures ofcocktails, that accurately complexity reflect the of plantcell walls. investigationsFuture shouldtherefore uponmore center complexenzymatic cocktails, or efficient biomass. degradationof manner,contributingtothe complementary plant diverse phenomenon indicates that FAEmay different substrates isoenzymes target ina debranching differently enzymesrespond towards feruloylated polysaccharides. the This AtFaeD from treatmentfrom wheatarabinoxylan wassuccessfullyimprovedwith 30%with the by27%to together( incubated xylanase followed pre-treatedwith was sequentially the withAtFaeDthan enzymes co- moresubstrateThe releasing ofFAefficient from was whenthe wheatarabinoxylan 11-fold co 2017 ( enzyme addition yieldfrom300 U,andxylooligosaccharide almost 0to optimum inthe doubled levelof was FA released from greatly of enhanced theactivity 70%as 16.8%to AnXyn11A increased applicoworkers wheatbranforco-production Wuin hydrolyzing of the FAandxylooligosaccharides, and TRA, theenzymes ahighdegreeofsynergy, 5.1. show concentration treatment ofFA.Although the xylanase releasedonly withAcFaeplus 7.7%of ahighcontaining releasedfrombagasse,anagricultural sugarcane residue (1.97-fold) al.,2016 et commercial preparationxylanase on at30 sugarcane bagasse hydrolysis °C for 24h theour researchgroupevaluated synergistic effect ofAcFae from Recently, ofproduction them along particle ofcorncobwith the size and increased stalk. corn higherfrom than sugars producedstalk, about fromcorn andthe is reducing 2-fold corncob (20,40,mesh)sizes The content of 80,100 ofcornstalk and corncob for 50°C. 1hat hydrolase rhamnogalacturonan and rhamnogalacturonan acetyl esterase notshowwheat bran, but did effect cooperative withendopolygalacturonase, xylanase ( AtFaeAusing from -incubation treatment with FAE and xylanase to release FA from lignocellulosic substrates. -incubation treatment withFAEandxylanase to FAfrom release substrates. lignocellulosic

The groupsSeveral arecurrentlyworking tounderstand why precisely and FAEs Evaluating thesimult Immobilization and influence of organic co-solvents onthe and Immobilization influence oforganicco-solvents FAE activity T.

). The treatment resulted in asignificant increase in amount the ofreducing sugars proof-of-principle was proof-of-principle able todemonstrate the differential effect ofsequential or lanuginosus A. terreus ed AnFaeA and (0to1000U)simultaneously, (100U)andAnXyn11A the Wu al.,2017 et Mäkelä etal.,2018 A. terreus Comment citer cedocument:

and and ) releases FAand commercial xylanase. aneous cooperation andxylanaseGH11(AnXyn11A) ofAnFaeA

with xylanasefrom ) . On otherhand, the AnFaeCfrom

Besides, p -coumaric acid from -coumaric acid wheatarabinoxylan and 19

the productionthe ofxylooligosaccharides A. niger

to hydrolyze different particle A. clavatus A. niger ( Dilokpimol et al., Dilokpimol al., et

in synergy with and a

( Oliveira Oliveira

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos coated magnetic Fe coated therapeutic onsilica- biosensor as as well applications. Soybean immobilized peroxidase ( increase inactivitycompared FAE, to putative a2-fold free enzyme PhEst,with the 52.4% ofits initial activity fortherelease ofFA 5cycles fromwheatbran after insoluble increase inan optimal from temperature 45 ability to to poreability adjust the ofthe size material to the dimensions oftheenzyme ofinterest. su large ( oxidation hydroxycinnamates, with compounds application inhibitorsas antioxidants and ofLDL- (CLEAs)immobilized enzymeaggregates the ascross-linked usedin of and synthesis alkyl antioxidants. new generate used to bioactive compounds, potential with higher monomeric than FAas andproduction could be byperoxidases also pulpand mills,paper phenolic acids cross-linked forproposed remediation environmental from ofeffluents wine distilleries,oil olive ( obtained withonly 57% thefree peroxidase al.,2015 et ( can esterase differentadopt orientations within the pores, silica which byinfluenced surface distribution the charge around activepocket, the site indicating that the ( with the shown tobecorrelated pH,withaoneunit shift in theoptimal transesterification pH Mes 2018). maxim be immobilizationhave to enzyme, carefullyindividually foreach designedsince the thermophila immobilizedMonocomponent FAEshavebeen onmagnetic Fe biomedical applications. for Theimmobilization ofFAE studied hasbeen suchapplications. compoundsandplatformbioactive development the chemicals, andin ofnanomaterials for Immobilized reducingcosts. reuse, enzymes forthe beused can ). et2011). wasproposedthatsuchParracino It al., immobilized biocatalystscouldbe used for Thörn et Thörn et al., 2013 Thörn et al., 2011 um activity and enzyme stability can vary in different FAE preparations can vary al.,(Zerva et in different andenzymeFAE activity preparations um stability AnFaeA esterase-containinghave cocktails andferuloyl successfully enzyme been Immobilization ofImmobilization FoFaeCfrom In industry, In industry, immobilization isoftenemployed to stabilize enzymes facilitatetheir and

rface area Vafiadi etal., 2008a ). Fe Supermagnetic oporous asenzyme used due materials supports to their havebeen immobilization

and T. wortmanni , allowing enzyme high theirhigh loading, mechanical stability,andthe ) ; 3

Thörn al.,2013 et . Other factors. Other caninfluence theinteraction theirproposed ofFAEswith O 4

nanoparticles removes ofFAmix areaction from 99% to compared Comment citer cedocument: using CLEAmethodology demonstrated that conditionsfor ; 3 O Vafi 4 @Au core-shell nanoparticles used were @Au core-shell toimmobilize

adi etal.,2008badi ) . Accessibility to . Accessibility active the site oftheFAE was F. oxysporum o C to55 Silva al., et 2016 20 o ) C andtemperature stability, retaining .

on a mesoporous silica supportwas silica on amesoporous Immobilization FAEs ofeight from ). W ). 3 O de novo 4 hile this systemhile was

nanoparticles, leading to are pH-dependent synthesis of

( He a

M. M.

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos FAEs against v/v)concentrations of enhancedand DMSO(<20% hydrolytic broadenedof the capacity the hydrolysisthe byphysicalsilica adsorptionresults mesoporousin transesterification lower efficiency, since 2017 preparations( development inthe for ofbiocatalysts esterification reactions activity.their demonstratessuitability Thisstudy of immobilized the crude enzyme 24 h.Rinsing toremovefrom withsolvent water immobilizedthe enzymes improved further initial activity reusability wasobservedina experiment reaction nine each after cycles, lasting ratio washigherhydrolysis whenusingimmobilized addition,over90% enzymes.In of the Although thebutyl highest yields ferulate areobtainedwith the freeenzyme, synthesis- the offerulatesynthesis butyl through oftransesterification methyl with ferulate 1-butanol. diameteron pore size.The andprotein immobilized enzymes successfully were Using cr particlessilica porediameters ( with varying from6.6 nm to10.9nm M. thermophila, dependent,FAEsstructure with morebeingstable. the lipase-like ( in rearrangement.side canbeused liquids (IL) and Ionic reactions forbothhydrolytic synthetic controlandutilizationofthe FAE. animmobilized chargedpositively surface at low surface charge density and canhigh ionicstrength maximize lignocellulose components. Astudy by deconstruction orchanging byalteringsolubility ofsubstrates the solubility the of caninteraction beweakenedorstrengthened withbuffer strength ionic byregulated electrostatic ina such forceswaythat betweenprotein the andthe surface, of itself. Theadsorption AnFaeA was charged surface ontoa simulated and showntobe isinteracting it with,whether it is an immobilization support biomassor the lignocellulosic can materialesterase hydrophobicity,be affectedcrystallinity bythe and charge surface ofthe orcanalterthesubstrate, specificity adsorption of FAE.Thephysical the stability ofthe Zeuner etZeuner al.,2011 volving FAEs,volving butsomebeenshownFAEs tobemore unstable have in others ILsthan ). ).

The immobilizationof and four MtFaeA2,MtFaeB1, from FAEs,MtFaeA1, MtFaeB2 The immobilizationof a commercially feruloyl available on esterase,E-FAERU, The addition co-solvents oforganic canexpandtheFAEs use inlignocellulose ude enzyme enrichment preparations, ofimmobilized infunction FAEs wasobserved model includingacetylated compounds, compounds, possibly through an active

reaction reaction by is preferred regardless E-FAERU, of itisfreeor whether

was studied andoptimized adsorption onto physical via mesoporousvarious ). Stabilityin ). ILs was linked to bothaniondependentandenzyme being Comment citer cedocument:

Faulds et al. etal. Faulds 21

(2011 ) ) demonstrated that low Hüttner et 2017 et al., Hüttner

(

Liu al.,2015 et Hüttner etal.,Hüttner used for the

) . A ). ). to -

Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos and diferuloyl glycerol and diferuloyl glycerol ( (DFG) lower 0.1% are than materials FGsfromseparate raw since natural themonoferuloyl contents of glycerol (MFG) ( drug industries functionsbiological asnatural UV and lightfilters antioxidantsthe chemical, in and food, higherpresent solubility than derivativesin water ofFA, freeFA.Natural FG present many (FGs) consistofFAwhich toglycerol,naturally esterified foundinplants, a compound ( byproducts lipophilic in results and sugars. In turn,thealteration ofFA esterification via with aliphatic alcohols solubilityimprove ofFA water the bylinking it to hydrophilic glycerol compounds, suchas ( withtriacylglycerolstransesterification been reportedmodification of that FAthroughesterification with aliphatic alcohols or lowsolubility andstability inhydrophobicmedia, overcomeis its to limitation, this it has food and processing corresponding for other industries obstacle application of FAinoil-based FAcannotsince directly used be as donor the in transesterification majorreactions. A transesterification morecomplicatedreactions than reactions, are esterification expensive and industrialwidespread potential dueto antioxidant applications, their Forindustrial properties. modify propertiesused to thephysical hydroxycinnamic ofFAvarious with and acids, ofvariety food( andpharmaceutical applications es the or solvents to low-aqueous produce may andtransesterification esterification innon- catalyze ( antitumor, antiviral agents antimicrobial, andanti-inflammatory 2012 conditions, reaction low consumption( energy and highenantioselectivity efficiencychemicalcatalytic methods, enzymaticin mild ofFGs synthesis high involves 6 biotechnological approaches for the biosynthesis of ferulate isderivatives summarized in 11. cannotberegarded and enzyme-specific asreflecting thegeneral behavior ofFAEs. ( immobilized .

). ). terified compounds with novel physicochemical characteristics, expanding theira use in terified compounds novelphysicochemical with characteristics,

Feruloyl andphenolicesterFeruloyl esters sugars have functions,important biological as There has been remarkable progress in synthesizing many hasbeenremarkable progressinsynthesizingThere compounds feruloylated to

Synthesis of Synthesis Bonzom al.,2018 et Compton 2012 al., et esters-products by esterification activity esters-products byesterificationactivity Kikugawa al.,2012 et Comment citer cedocument: ). ). demonstratesThis result enzymethat immobilization is

). How ). Vafiadi al.,2008b et ever, it hasbeen it reportedthat isdifficultever, it to ; 22 Kikugawa et al.,2016 Kikugawa et Nieter al.,Nieter et 2016 Sun &Chen, 2015 ).

Current knowledgeCurrent of Paiva et2013 al., ). ). ). Feruloylglycerols). Esterification can be ). I ). n comparison to Compton et al.,

). ). FAEs Fig.

-MS asthecorresponding-MS feruloylated Fivesaccharides. FAEs, MtFaeA2, MtFaeA1, ) Commercial). enzyme are able preparations toperform transesterifications ofFA to . AnFaeA is able . AnFaeAferulate isable to synthesize in 1-glycerol a mixture FA,85%glycerol of1% l hydroxyl group of glycerol (2-FG) or at one of the terminal hydroxyl groups (1-FG) orat l hydroxylgroup oneoftheterminal of groups (1-FG) (2-FG) glycerol hydroxyl Kelle 2016 etal., Zeng andcoworkers conducted astudy AoFaeA using Future perspectives An important proof

either feruloylto produce two the glycerol esterisomers, at the with bondoccurring Antonopoulou et al., Antonopoulou etal., inyl caffeate, fatty alcohols and carbohydrates as acyl donors (Varriale al.,et inyl alcohols 2018). caffeate,fatty andcarbohydrates (Varriale as acyl donors ). The major product wasdetermined by reaction γ-feruloyl-α,α′-diglycerol tobe

were able were able to prenylferulate,caffeate, catalyze glyceryl prenyl caffeate, glyceryl fied froma commercial enzyme produced by preparation ). Themaximum). esterification 60.3%at contentyield reached water of 20%, Comment citer cedocument: ). Fort -of-principle milestone wasachievedwith synthesisthe of Tsuchiyama al.,2006 et D- 2017 unately, there newunately,During there is a development front. onthis sucrose, )

. The wild-type and evolved variants of andevolvedThe wild-type variants MtFae1afrom D -lactose, M. thermophila Tsuchiyama al.,2006 et

23 C1 andMtFae1a from D -maltose) methyl using as ferulate aFA ; Vaf Kelle 2016 etal.,

iadi et al.,2007 et iadi ( Topakas etal., 2005 D

-glucose, -glucose, from A. oryzae A. oryzae ). Ki ). M. thermophila M. thermophila D A. niger -fructose, -fructose, ; kugawa ; Tsuchiyama etal., Tsuchiyama Vafiadi et al., P. sapidus expressed in ), which), isthe

( and

Kikugawa D - ATCC

was P. M.

This work was supported by grants fromThis workwassupportedgrants ConselhoNacionaldeDesenvolvimento by the Conclusion Conclusion mostEven though produced characterized have and studies FAEs, recent This review This review plant wall,In the FApolysaccharides cell to component isanessential cross-linking

esterification ofand transesterification ofhydroxycinnamic esters FAand acids. , Tecnológico (CNPq), Coordenação de deNível(CNPq), Aperfeiçoamento Coordenação Tecnológico dePessoal highlighting presents presents Comment citer cedocument:

the recent advances biochemicalproperties,the in the and biodiversity a critical assessment various strategies comparing forFAE

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Brassica ), Poaceae ), Baloskion tetraphylBaloskion ), Poaceae ), oleraceae ), Alliaceae ), Lollium

),Fabaceae ), Amaranthaceae ),

), Amaranthaceae ), Phoenix oleraceae ),Poaceae

), Bromeliaceae ), perenne ), Cyperaceae ), ),Amaranthaceae

), Brassicaceae

), ), ), Poaceae ), ), ),

), Poaceae ), lum ), ), ),

Stem Stem Grain Stem bagasse Culm Shoot bladeLeaf Stem Bran Grain tissue or Organ – – – – – Root Root Bulb Leaf Stem Stem coreFruit

3.43 3.18 to 0.143 0.091 3.51 to 17.0 8.0 6.03 3.86 6.27 to 33.0 26.1 20.66 FAof (mg Concentration 0.0029 0.041 0.0027 0.12 0.074 4.59 6.93 0.007 0.17 1.07 2.27 6.84

( ( ( 1984 ( ( 1984 ( 1984 ( 1984 ( ( 1984 ( Reference ( ( ( ( ( ( ( ( ( ( ( ( Karlen etal.,Karlen 2018 etal.,Karlen 2018 Moghadasian, and 2008 Zhao andHaverkamp,Hartley et Masarin al.,2011 andHaverkamp,Hartley andHaverkamp,Hartley andHaverkamp,Hartley Zhao andHaverkamp,Hartley Mattila and Hellström, Mattila and 2007 Hellström, Mattila and 2007 Hellström, Mattila and 2007 Hellström, Mattila and 2007 Hellström, Mattila and 2007 Waldron etal., 1999 Waldron etal., 1999 Moghadasian, and 2008 Zhao etal.,Karlen 2018 etal.,Karlen 201 etal.,Karlen 2018 etal.,Karlen 2018 ) ) ) ) )

and Moghadasian,and 2008

8 ) ) ) ) ) )

)

) )

) ) ) ) )

) ) )

sp.

judae

H1 Comment citer cedocument:

AtFaeA AtFAE AtFAE AtFAE AtFaeD AtFaeA AoFaeC AoFaeB AoFaeA AnFaeC AnFaeB AnFaeA Fae Fae AN1772.2 AfFaeA AcFae AwFaeA ActOFaeI Enzyme FaeII FaeI CjFae1B Est1E EstBC ApFae AuFaeA - - II I

- - -

3 2 1

37 30 75 36 29 63 130 40 28.4 35 32 (kDa) MW 31.5 58 61 31.6 36 210 36 36 36 23 76 43 35 75 61 37 -

4.9 4.8 4.9 3.3 3.6 3.0 4.6 – – 4.2 – p 6.02 5.59 – – 3.2 6.5 4.3 3.3 – – – 4.34 – – – I

5.0 7.0 6.0 5.0 7.0 6.0 7.0 5.5 6.5 pH opt 8.0 6.0 6.5 6.5 6.7 5.0 5.0 5.0 5.0 5.0 7.0 5.0 6.0 6.0 – – –

- 7.0

50 50 50 55 45 58 30 55 30 (°C) T 35 40 35 61 60 45 60 40 40 50 50 50 55 55 – – – opt

- - - 60 40 66

50 45 50 45 – – 50 40 (°C) T 45 50 40 – 60 45 55 55 55 37 – 60 55 – – – – –

sta

0.81 – – 1.44 2.08 0.47 1.11 0.15 1.21 0.659 0.248 – 0.26 0.31 0.44 – 1.38 2.79 (mM) K 0.16 0.36 13.76 2.50 4.78 – 0.24 0.19 0.04 0.098 0.137 0.010 0.050 4.64 – 0.07 0.07 0.08 – ND 0.29 0.38 0.61 0.091 0.058 0.10 0.104 0.022 0.14

– – – 84.95 70.74 – – – 0.90 0.27 2.21 – – 278.18 (s k 232.7 645.9 7.78 2.34 – 24.0 23.0 1.4 30.0 23.7 31.1 15.3 – – 1.32 1.27 1.32 – ND 4.68 0.31 2.59 – – – – – – – – 8.46 cat

)

– – – 3.53 91.0 – – – – – 3.47 0.88 5.02 – – 99.61 (s k 1,454.4 1,794.2 0.57 0.94 1.77 – 100.0 121.05 38 306.12 172.99 2,933.96 – – 18.89 18.14 16.58 – ND 16.14 0.81 4.25 – – – – – – 304.78 cat

−1

)

MCA MFA MpCA MCA MFA – pNB MFA MCA MSA MpCA MFA MFA – MpCA MpCA MpCA – MCA MSA MpCA MFA MCA MpCA MFA MCA MpCA MFA MFA – – MSA MFA MpCA MFA MpCA MFA MpCA MFA MCA MSA MpCA MFA – MFA MCA Substrate pNA

( ( ( ( ( ( ( ( ( ( ( ( ( ( ( ( 2004 ( 2017 ( ( ( ( ( ( ( ( Reference Li Li et al.,2011 et al.,2011 McClendon et2010 al., Goldstone Haase Rumboldal., et 2003 al.,2013Gong et Vriesde etal., 1997 Vriesde etal., 1997 Vriesde etal., 1997 Vriesde etal., 1997 Vriesde etal., 1997 et al.,Zhang 2015 et al.,2009Koseki et al.,2009Koseki et al.,Zeng 2014 etDilokpimol al.,2017 Vriesde etal., 2002 Williamson,& Faulds 1994 Williamson,& Faulds 1993 Williamson,& Faulds 1993 Chen, Shin & 2007 et al.,Zhang 2013 et al.,Damásio 2013 et al.,Fazary 2010 et al.,2016Hunt ) )

- Aschoff etal.,2013

)

) ) )

) ) ) ) )

)

) ) ) ) ) ) ) ; )

) (

Levasseuret al., ) )

)

) ) ; ; Wong,2006 ( Wuet al., )

Schizophyllumcommune sapidus Pleurotus Pleurotus eryngii piceumPenicillium expansumPenicillium giganteus Panus Neurosporacrassa Myceliophthora thermophila plantarum Lactobacillus Lactobacillus farciminis Lactobacillus amylovorus Lactobacillus acidophilus Lactobacillus Lactarius hatsudake Fusarium proliferatum Fusarium oxysporum Erwinia chrysanthemi thermocellum Clostridium Chrysosporium lucknowense sp. Chaetomium Sorangium cellulosum fermentum

CQ31

Comment citer cedocument: PeFae PgFae NcFae MtFaeC MtFaeB Lp_0796 FaeLfe FaeLfa FaeLam FaeLac LhFae FpFae FoFaeC FoFaeB/FaeI FoFaeA/FaeII FaeT FaeD XynZ FaeB2 Fae2 Fae1 Fae FaeIII ScFae2 ScFae1 ScFaeD2 ScFaeD1 PsEst1 PeFaeA PpFae

31 62 31 27 35 35 45 33 36 29 29.6 42 34 35 54 63 55 67 56 65 61 35 23 33 28 29 29 29 29 55 38

- 36

– 9.5 9.9 – – 5.8 6.0 5.2 5.5 – 4.98 4.67 5.07 – – 5.7 5.2 – – – 8.26 3.5 3.1 – – – – 5.6 – –

6.5−7.5 6.0 7.0 7.0 7.5 7.5 6.0 8.0 7.5 6.5 7.5 9.0 6.0 7.0 7.5 7.5 6.0 5.0 3.0 5.6 4.0 6.0 6.0 6.0 7.0 6.5 7.0 8.0 6.5 4.0

- - - 8.0 7.0 7.5

50 65 55 45 – – 60 65 40 45 60 40 – – 45 45 50 50 70 37 40 55 55 55 – 37 45 45 30 –

- - - - 60 50 50 50

50 45 30 45 – – 70 – 50 50 55 45 45 45 – 40 60 – 40 – 60 50 30 50 50 50 – – – –

0.196 0.263 0.146 0.16 0.50 0.21 0.12 0.26 1.12 0.20 0.60 0.81 0.29 0.68 0.58 – – 5.0 – – – 0.98 1.26 1.06 0.03 0.51 0.18 0.22 0.43 0.74 0.123 0.137 0.146 0.123 0.151 0.159 1.95 0.44 0.145 – 2.6 0.36 0.02 0.021 0.25 0.14 0.57 0.59 1.64 0.21 0.09 0.71 – – – – – 0.54

– – 140.6 8.2 222.9 120.4 5.91 0.46 19.88 6.85 0.13 1.94 0.21 0.65 – – – – – – – 6 538. 330.9 2,130.9 310.5 6.5 8.2 9.6 8.3 34.1 91.4 54.7 38.4 105.1 51.0 – 3.41 0.85 – – – 4.8 12.19 5.24 0.13 0.40 0.53 2.60 4.56 5.47 3.30 – – – – – – –

– – 879.06 16.4 1,061.43 1,003.47 22.75 0.416 99.44 11.41 0.16 6.70 0.31 1.13 – – – – – – – 427.4 312.1 71.029 608.8 36.11 37.27 22.32 11.21 275.1 666.2 372.6 310.6 696.3 319.2 11.2 7.75 5.85 – – – 100 580 21 0.95 0.70 0.90 1.58 21.74 60.77 4.64 – – – – – – –

MSA MFA MSA MFA MCA MpCA MFA MCA MpCA MFA MFA FAX MFA – MFA – MCA MpCA MFA MCA MSA MpCA MFA MCA MpCA MFA – – – – – MFA MCA MpCA MFA MCA MSA MpCA MFA MCA MSA MpCA MFA MCA MSA MpCA MFA – – – – – MFA MpCA MCA MFA MpCA FAXXX

( ( ( ( ( ( ( ( ( ( ( ( ( ( ( ( ( ( ( ( 2011 ( ( ( ( Wu et al., 2012 Wual., et etal.,2016Nieter et al.,2013Linke etal.,2014Nieter et al.,2016 Gao &Donaghy McKay, 2003 et al.,Wang2014 et al.,Crepin 2003a etal., Topakas 2005 etal., Topakas 2004 Esteban al.,2017 Xu et al.,2017 Xu et al.,2017 Xu et al.,2017 Xu et et al.,Wang2016 Chen, Shin & 2006 etMoukouli al.,2008 etal., Topakas 2003 etal., Topakas 2003 Hugouvieux& Hassan Blumal., 2000et et al.,Kühnel et al.,2013 Yang )

- Torres et Torres al., et 2012 ) ) ) ) )

)

) ) ) ) ) ) )

) ) )

) ) ) )

) 2013

- Cotte )

)

- Pattat, Version postprint of bioactive compounds. Bioresource Technology, 278, 408-423. ,DOI :10.1016/j.biortech.2019.01.064 (2019). Feruloyl esterases: Biocatalysts toovercome biomassrecalcitrance andfor theproduction Oliveira, D.M.,Mota,Oliva, B.,Segato, Marchiosi,Ferrarese-Filho, Faulds,C.,dos Santos pNB: ferulate; MpCA: methyl p arabinofuranosyl-(1→3)]- xylopyranosyl-(1→4)-D-xylopyranose; FAXXX: 1

2 burchelliEquus 2 2 wortmanniTalaromyces stipitatusTalaromyces werraensisStreptomyces olivochromogenes Streptomyces sp. Streptomyces Dimeric protein. Microﬂora ofa cow’srumen Microﬂora samples Fecal of soil metagenomicsCotton p -Nitrophenyl butyrate; pNF:

Rusa unicolorRusa 2 Metagenomic analysis.FAXX: O

-coumarate;methyl MSA: sinapate; ND, not detected; pNA: O

-β-D-xylopyranosyl-(1→4)-D-xylopyranose; MCA: methyl caffeate; MFA: methyl Comment citer cedocument:

and

p -Nitrophenyl ferulate; not–, detected ornot mentioned. RuFae2 Tvmz2a Tvms10 Tan410 Fae68 Fae7262 Fae125 TsFaeC TsFaeB TsFaeA SwFaeD SoFae R43 R18

O -β-D-xylopyranosyl-(1→4)- - [5 29 31.2 18.6 55 58.8 43 40 65 35 35 48 29 52 38 39 - O

-(transferuloyl)-α-L-arabinofuranosyl]-(1→3)-

8.5 – – 4.7 4.9 5.2 5.6 4.6 5.3 3.5 – 7.9 – –

7.0 8.0 7.0 7.0 – – – 6.0 – – 7.5 5.5 7.0 7.5

- 7.0

50 38 35 35 – – – 60 – – 40 30 40 50

O - [5 50 40 40 40 – – – – – 45 40 45 - - O

p -(trans-feruloyl)-α-L- -Nitrophenyl acetate; – – – – – – – 0.37 0.01 0.04 – – 0.12 0.23 1.86 0.54 2.61 3.00 4.41 9.39 3.31 4.31 4.99

– – – – – – – 9.26 9.55 9.65 – – 0.89 1.98 – – – – – – – – –

-β-D- – – – – – – – 25.0 746.0 323.0 – – 7.67 8.73 – – – – – – – – –

– – – – – – – MSA MpCA MFA – – MSA MFA MFA MSA MCA MpCA MFA MSA MCA MpCA MFA

( ( ( ( ( 2003b ( ( ( ( Wong et Wongal., 2013et Chandrasekharaiah et al.,2012 et al.,2013 Yao etal.,2019 Antonopoulou et al.,Crepin 2003b Garcia et al.,Schulz 2018 Williamson,& Faulds 1991 etal Uraji )

- Conesa al., 2004 et ., 2014., )

)

) )

)

) )

; )

( Crepin et al., )

, Glycosylated. Glycosylated.

not detected ornotmentioned.

Comparison in Comparison in protein effects glycosylation ofheterologous expressedFAEs. dus

Non-glycosylated. Protein Fae7262 Fae125 Fae68 TsFaeC PsEst1 Pp NcFae MtFae1 AtFaeA AoFaeC AoFaeB AnFaeD AnFaeC AnFaeB AnFaeA AfFaeA AN1772.2 ApFae FaeA

Comment citer cedocument: -

host Expressed C1 thermophila M. pastoris P. pastoris P. pastoris P. pastoris P. pastoris P. pastoris P. pastoris P. pastoris P. pastoris P. pastoris P. 298302 A. coli niger A. pastoris P. cerevisiae S. -

niger CMICC

and E. #

Predicted molecularPredicted mass. *Tm temperature). (melting

Glycosylated 40 40 and 37 and 40 30.246 35.04 58.8 130 210 39 75 61 43 30 74 40 43 40 66 70 35

MW(kDa)

Non - 29.286 32.303 28.164 55.340 glycosylated 28.552

110 35 55 55 30 60 56 60 32 – – – –

# # # #

Glycosylation 53 23 22 11 O – – – – 2 – – – – – – – 1 –

site

10 13 18 10 N 4 3 2 7 – 1 2 6 – 2 0 – 3 –

Glycosylated Optimum(°C) temperature 55 50 50 50 55 58 45 60 60 50 48 – – – – – - -

Non - glycosylated

50 – – – – – – – – – – – – – – – – –

2018a) etal., (Antonopoulou etal., 2004)(Crepin ( et al.,(Oleas 2017) etal., 2003a)(Crepin etal., (Topakas 2012) et al.,(Zhang 2015) et al.,2009)(Koseki et al.,2009)(Koseki 2018) etal., (Mäkelä et(Dilokpimol al.,2017) ( et al.,2006)(Benoit et al.,(Zhang 2013) Chen,and (Shin 2007) (Rumboldal., et 2003) Reference Kelle et al.,2016Kelle Vriesde etal., 2002

)

Biosynthetic tools for Biosynthetic tools The potentialof areversatiletheFeruloyl esterases biocatalystsproduction of forhydroxycinnamates assessmentCritical various strategies comparing forvalorization feruloyl esterase feruloyl esterases foris highlighted biotechnological feruloyl esterases applications Comment citer cedocument: esterification andtransesterificationcompoundsbioactive of

Comment citer cedocument: