Abstract
The properties of pectinolytic enzymes have drawn a great attention from many research teams as potential biological catalysts in diverse industrial processes for plant transformation. Pectin-related enzymes are ubiquitous, produced by plants, fungi and bacteria. Due to the highly complex structure described in Chap. 2, pectin is the substrate for many modifying and degrading enzymes belonging to three families of Carbohydrate Active enZymes (CAZy): glycoside hydrolases, polysaccharide lyases and carbohydrate esterases. They are distinguished by their different mechanisms (hydrolysis or β-elimination), action patterns (endo/exo) and specificities (homogalacturonan, rhamnogalacturonan, neutral side-chains, oligogalacturonates). In the 90s, literature dealt with their biochemical characterisation while more recently, progress in protein biotechnologies allowed investigating the production of recombinant and mutated enzymes to study the role of key amino acids. This chapter reviews the state of knowledge of pectin-processing enzymes to illustrate their structural and functional diversities. Their physico-chemical and biological properties are presented, as well as the occurrence of inhibiting proteins.
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References
Abbott DW, Boraston AB (2007) The structural basis for exopolygalacturonase activity in a family 28 glycoside hydrolase. J Mol Biol 368:1215–1222
Alalouf O, Balazs Y, Volkinshtein M, Grimpel Y, Shoham G, Shoham Y (2011) A new family of Carbohydrate Esterases is represented by a GDSL hydrolase/acetylxylan esterase from Geobacillus stearothermophilus. J Biol Chem 286:41993–42001
Andres-Robin A, Reymond MC, Dupire A, Battu V et al (2018) Evidence for the regulation of Gynoecium morphogenesis by ETTIN via cell wall dynamics. Plant Physiol 178:1222–1232
Arnal G, Bastien G, Monties N et al (2015) Investigating the function of an arabinan utilization locus isolated from a termite gut community. Appl Environ Microbiol 81:31–39
Atkinson RG, Sutherland PW, Johnston SL et al (2012) Down-regulation of POLYGALACTURONASE 1 alters firmness, tensile strength and water loss in apple (Malus x domestica) fruit. BMC Plant Biol 12:129
Azadi P, O’Neill MA, Bergmann C, Darvill AG, Albersheim P (1995) The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase. Glycobiology 5:783–789
Beldman G, Schols HA, Pitson SM, Searle-van Leeuwen MJF, Voragen AGJ (1997) Arabinans and arabinan degrading enzymes. Adv Macromol Carbohydr Res 1:1–64
Benoit I, Danchin EGJ, Bleichrodt R-J, de Vries RP (2008) Biotechnological applications and potential of fungal feruloyl esterases based on prevalence, classification and biochemical diversity. Biotechnol Lett 30:387–396
Beylot M-H, McKie V, Voragen AGJ, Doeswijk-Voragen CHL, Gilbert HJ (2001) The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity. Biochem J 358:607–614
Böger M, Hekelaar J, van Leeuwen SS, Dijkhuizen L, Lammerts van Bueren A (2019) Structural and functional characterization of a family GH53 β-1,4-galactanase from Bacteroides thetaiotaomicron that facilitates degradation of prebiotic galactooligosaccharides. J Struct Biol 205:1–10
Bonivento D, Pontiggia D, Di Matteo A et al (2008) Crystal structure of the endopolygalacturonase from the phytopathogenic fungus Colletotrichum lupini and its interaction with polygalacturonase-inhibiting proteins. Proteins 70:294–299
Bonnin E, Thibault J-F (1996) Galactooligosaccharide production by transfer reaction of an exogalactanase. Enzym Microb Technol 19:99–106
Bonnin E, Le Goff A, van Alebeek GJWM, Voragen AGJ, Thibault J-F (2003) Mode of action of Fusarium moniliforme endopolygalacturonase towards acetylated pectin. Carbohydr Polym 52:381–388
Bonnin E, Clavurier K, Daniel S, Kauppinen S, Mikkelsen JD, Thibault J-F (2008) Pectin acetylesterases from Aspergillus are able to deacetylate homogalacturonan as well as rhamnogalacturonan. Carbohydr Polym 74:411–418
Bordenave M (1996) Analysis of pectin methyl esterases. Plant Cell Wall Anal 17:165–180
Brummell DA, Cin VD, Crisosto C, Labavitch J (2004) Cell wall metabolism during maturation, ripening and senescence of peach fruit. J Exp Bot 55:2029–2039
Cao J (2012) The pectin lyases in Arabidopsis thaliana: evolution, selection and expression profiles. PLoS ONE 7:e46944
Chen M, Citovsky V (2003) Systemic movement of a tobamovirus requires host cell pectin methylesterase. Plant J 35:386–392
Chen C, Chen JL, Lin TY (1997) Purification and characterization of a xylanase from Trichoderma longibrachiatum for xylooligosaccharide production. Enzym Microb Technol 21:91–96
Cheng J, Romantsov T, Engel K, Doxey AC, Rose DR, Neufeld JD, Charles TC (2017) Functional metagenomics reveals novel β-galactosidases not predictable from gene sequences. PLoS ONE 12:e0172545
Chotigeat W, Duangchu S, Wititsuwannakun R, Phongdara A (2009) Cloning and characterization of pectate lyase from Hevea brasiliensis. Plant Physiol Biochem 47:243–247
Chourasia A, Sane VA, Nath P (2006) Differential expression of pectate lyase during ethylene-induced postharvest softening of mango (Mangifera indica var. Dashehari). Physiol Plant 128:546–555
Crepin VF, Faulds CB, Connerton I (2004) Functional classification of the microbial feruloylesterases. Appl Microbiol Biotechnol 63:647–652
Cui Z, Maruyama Y, Mikami B, Hashimoto W, Murata K (2007) Crystal structure of glycoside hydrolase family 78 α-L-rhamnosidase from Bacillus sp GL1. J Mol Biol 374:384–398
De Freitas ST, Handa AK, Wu Q, Park S, Mitcham EJ (2012) Role of pectin methylesterases in cellular calcium distribution and blossom-end rot development in tomato fruit. Plant J 71:824–835
De Souza AJ, Pauly M (2015) Comparative genomics of pectin acetylesterases: insight on function and biology. Plant Signal Behav 10:e1055434
De Vries RP, Parenicova L, Hinz SWA, Kester H, Beldman G, Benen JAE, Visser J (2002) The β-1,4-endogalactanase A gene from Aspergillus niger is specifically induced on arabinose and galacturonic acid and plays an important role in the degradation of pectic hairy regions. Eur J Biochem 269:4985–4993
Denès J-M, Baron A, Renard CMGC, Péan C, Drilleau J-F (2000) Different action patterns for apple pectin methylesterase at pH 7.0 and 4.5. Carbohydr Res 327:385–393
Derbyshire P, McCann MC, Roberts K (2007) Restricted cell elongation in Arabidopsis hypocotyls is associated with a reduced average pectin esterification level. BMC Plant Biol 7:1–12
Despres J, Forano E, Lepercq P et al (2016) Unraveling the pectinolytic function of Bacteroides xylanisolvens using a RNA-seq approach and mutagenesis. BMC Genomics 17:147
Di Matteo A, Giovane A, Raiola A et al (2005) Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein. Plant Cell 17:849–858
Dilokpimol A, Mäkelä MR, Aguilar-Pontes MV et al (2016) Diversity of fungal feruloyl esterases: updated phylogenetic classification, properties, and industrial applications. Biotechnol Biofuels 9:231
Dixit S, Upadhyay S, Singh H, Pandey B, Chandrashekar K, Verma P (2013) Pectin Methylesterase of Datura species, purification, and characterization from Datura stramonium and its application. Plant Signal Behav 8:e25681
Domingo C, Roberts K, Stacey NJ, Connerton I, Ruíz-Teran F, McCann MC (1998) A pectate lyase from Zinnia elegans is auxin inducible. Plant J 13:17–28
Dorokhov YL, Komarova TV, Petrunia I (2012) Airborne signals from a wounded leaf facilitate viral spreading and induce antibacterial resistance in neighboring plants. PLoS Pathol 8:e1002640
Expert D, Patrit O, Shevchik VE, Perino C, Boucher V, Creze C, Wenes E, Fagard M (2018) Dickeya dadantii pectic enzymes necessary for virulence are also responsible for activation of the Arabidopsis thaliana innate immune system. Mol Plant Pathol 19:313–327
Federici L, Caprari C, Mattei B et al (2001) Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein). Proc Natl Acad Sci U S A 98:13425–13430
Flint HJ, Bayer EA, Rincon MT, Lamed R, White BA (2008) Polysaccharide utilization by gut bacteria: potential for new insights from genomic analysis. Nat Rev Microbiol 6:121–131
Francis KE, Lam SY, Copenhaver GP (2006) Separation of Arabidopsis pollen tetrads is regulated by QUARTET1, a pectin methylesterase gene. Plant Physiol 142:1004–1013
Frenkel C, Peters JS, Tieman DM, Tiznado ME, Handa AK (1998) Pectin methylesterase regulates methanol and ethanol accumulation in ripening tomato (Lycopersicon esculentum) fruit. J Biol Chem 273:4293–4295
Gomez LD, Steele-King CG, Jones L, Foster JM, Vuttipongchaikij S, McQueen-Mason SJ (2009) Arabinan metabolism during seed development and germination in Arabidopsis. Mol Plant 2:966–976
Gou J, Miller LM, Hou G, Yu X, Chen X, Liu C (2012) Acetylesterase-mediated deacetylation of pectin impairs cell elongation, pollen germination, and plant reproduction. Plant Cell 24:50–65
Guénin S, Mareck A, Rayon C et al (2011) Identification of pectin methylesterase 3 as a basic pectin methylesterase isoform involved in adventitious rooting in Arabidopsis thaliana. New Phytol 192:114–126
Herron SR, Benen JA, Scavetta RD, Visser J, Jurnak F (2000) Structure and function of pectic enzymes: virulence factors of plant pathogens. Proc Natl Acad Sci U S A 97:8762–8769
Hewezi T, Howe P, Maier TR, Hussey RS et al (2008) Cellulose binding protein from the parasitic nematode Heterodera schachtii interacts with Arabidopsis pectin methylesterase: cooperative cell wall modification during parasitism. Plant Cell 20:3080–3093
Hocq L, Pelloux J, Lefebvre V (2017a) Connecting homogalacturonan-type pectin remodeling to acid growth. Trends Plant Sci 22:20–29
Hocq L, Sénéchal F, Lefebvre V, Lehner A, Domon JM et al (2017b) Combined experimental and computational approaches reveal distinct pH dependence of pectin methylesterase inhibitors. Plant Physiol 173:1075–1109
Hongo S, Sato K, Yokoyama R, Nishitani K (2012) Demethylesterification of the primary wall by pectin methylesterase 35 provides mechanical support to the Arabidopsis stem. Plant Cell 24:2624–2634
Iwai M, Kawakami T, Ikemoto T et al (2015) Molecular characterization of a Penicillium chrysogenum exo-rhamnogalacturonan lyase that is structurally distinct from other polysaccharide lyase family proteins. Appl Microbiol Biotechnol 99:8515–8525
Jenkins JA, Mayans O, Smith D, Worboys K, Pickersgill R (2001) Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site. J Mol Biol 305:951–960
Jiang S, Yang SL, Xie LF, San Puah CH, Zhang XQ et al (2005) VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth in the Arabidopsis style and transmitting tract. Plant Cell 17:584–596
Johansson K, El-Ahmad M, Friemann R, Jörnvall H, Markovic O, Eklund H (2002) Crystal structure of plant pectin methylesterase. FEBS Lett 514:243–249
Jolie RP, Duvetter T, Van Loey AM, Hendrickx ME (2010) Pectin methylesterase and its proteinaceous inhibitor: a review. Carbohydr Res 345:2583–2595
Kaji A, Shimokawa K (1984) New exo-type arabinase from Erwinia carotovora IAM 1024. Agric Biol Chem 48:67–72
Kalunke RM, Tundo S, Benedetti M, Cervone F, De Lorenzo G, D’Ovidio R (2015) An update on polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein that protects crop plants against pathogens. Front Plant Sci 6:146
Kauppinen S, Christgau S, Kofod LV, Halkier T, Dörreich K, Dalbøge H (1995) Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. J Biol Chem 270:27172–27178
Kent LM, Loo TS, Melton LD, Mercadante D, Williams MA et al (2016) Structure and properties of a non-processive, salt-requiring, and acidophilic pectin methylesterase from Aspergillus niger provide insights into the key determinants of processivity control. J Biol Chem 291:1289–1306
Kirsh R, Heckel DG, Pauchet Y (2016) How the rice we evil breaks down the pectin network: enzymatic synergism and sub-functionalization. Insect Biochem Mol Biol 71:72–82
Kofod LV, Kauppinen S, Christgau S, Andersen LN, Heldt-Hansen H-P, Dörreich K, Dalbøge H (1994) Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus. J Biol Chem 269:29182–29189
Kotake T, Hirata N, Degi Y et al (2011) Endo-β-1,3-galactanase from winter mushroom Flammulina velutipes. J Biol Chem 286:27848–27854
Kunishige Y, Iwai M, Nakazawa M, Ueda M, Tada T, Nishimura S, Sakamoto T (2018) Crystal structure of exo-rhamnogalacturonan lyase from Penicillium chrysogenum as a member of polysaccharide lyase family 26. FEBS Lett 592:1378–1388
L’Enfant M, Domon JM, Rayon C, Desnos T, Ralet MC, Bonnin E, Pelloux J, Pau-Roblot C (2015) Substrate specificity of plant and fungi pectin methylesterases: identification of novel inhibitors of PMEs. Int J Biol Macromol 81:681–691
L’Enfant M, Kutudila P, Rayon C, Domon JM, Shin WH, Kihara D, Wadouachi A, Pelloux J, Pourceau G, Pau-Roblot C (2019) Lactose derivatives as potential inhibitors of pectin methylesterases. Int J Biol Macromol 132:1140–1146
Leroux C, Bouton S, Kiefer-Meyer MC, Fabrice TN et al (2015) Pectin methylesterase48 is involved in Arabidopsis pollen grain germination. Plant Physiol 167:367–380
Lewis KC, Selzer T, Shahar C, Udi Y, Tworowski D, Sagi I (2008) Inhibition of pectin methyl esterase activity by green tea catechins. Phytochemistry 69:2586–2592
Lionetti V, Raiola A, Camardella L, Giovane A, Obel N, Pauly M et al (2007) Overexpression of pectin methylesterase inhibitors in Arabidopsis restricts fungal infection by Botrytis cinerea. Plant Physiol 143:1871–1880
Luis AS, Briggs J, Zhang X et al (2018) Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides. Nat Microbiol 3:210–219
Mardones W, Callegari E, Eyzaguirre J (2015) Heterologous expression of a Penicillium purpurogenum exo-arabinanase in Pichia pastoris and its biochemical characterization. Fungal Biol 119:1267–1278
Martens-Uzunova ES, Zandleven JS, Benen JAE et al (2006) A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation. Biochem J 400:43–52
Matsumoto S, Yamada H, Kunishige Y, Takenaka S, Nakazawa M, Ueda M, Sakamoto T (2017) Identification of a novel Penicillium chrysogenum rhamnogalacturonan rhamnohydrolase and the first report of a rhamnogalacturonan rhamnohydrolase gene. Enzym Microb Technol 98:76–85
Mayans O, Scott M, Connerton I, Gravesen T, Benen J et al (1997) Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases. Structure 5:677–689
McCarthy TW, Der JP, Honaas LA, de Pamphilis CW, Anderson CT (2014) Phylogenetic analysis of pectin-related gene families in Physcomitrella patens and nine other plant species yields evolutionary insights into cell walls. BMC Plant Biol 14:79
Mølgaard A, Kauppinen S, Larsen S (2000) Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure 8:373–383
Müller K, Levesque-Tremblay G, Bartels S, Weitbrecht K et al (2013) Demethylesterification of cell wall pectins in Arabidopsis plays a role in seed germination. Plant Physiol 161:305–316
Mutter M, Beldman G, Schols HA, Voragen AGJ (1994) Rhamnogalacturonan a-L-rhamnopyranohydrolase: a novel enzyme specific for the terminal non reducing rhamnosyl unit in rhamnogalacturonan region of pectins. Plant Physiol 106:241–250
Mutter M, Colquhoun IJ, Schols HA, Beldman G, Voragen AGJ (1996) Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan α -L-rhamnosyl-(1,4)-α-D-galactopyranosyluronide lyase. Plant Physiol 110:73–77
Mutter M, Renard CMGC, Beldman G, Schols HA, Voragen AGJ (1998a) Mode of action of RG-hydrolase and RG-lyase toward rhamnogalacturonan oligomers. Characterization of degradation products using RG-rhamnohydrolase and RG-galacturonohydrolase. Carbohydr Res 311:155–164
Mutter M, Beldman G, Pitson SM, Schols HA, Voragen AGJ (1998b) Rhamnogalacturonan α-D-galactopyranosyluronohydrolase, an enzyme that specifically removes the terminal nonreducing galacturonosyl residue in rhamnogalacturonan regions of pectin. Plant Physiol 117:153–163
Nafisi M, Stranne M, Zhang L, van Kan JAL, Sakuragi Y (2014) The endo-arabinanase BcAra1 is a novel host-specific virulence factor of the necrotic fungal phytopathogen Botrytis cinerea. Mol Plant Microbe Interact 27:781–792
Nakano H, Kitahata H, Watanabe Y, Fujimoto H, Ajisaka K, Takenishi S (1991) Transfer reaction catalysed by exo-β-1,4-galactanase from Bacillus subtilis. Agric Biol Chem 55:2075–2082
Naran R, Pierce ML, Mort AJ (2007) Detection and identification of rhamnogalacturonan lyase activity in intercellular spaces of expanding cotton cotyledons. Plant J 50:95–107
Ndeh D, Rogowski A, Cartmell A, Luis AS, Baslé A, Gray J, Venditto I, Briggs J, Zhang X, Labourel A, Terrapon N, Buffetto F, Nepogodiev S, Xiao Y, Field RA, Zhu Y, O’Neill MA, Urbanowicz B, York WS, Davies GJ, Abbott DW, Ralet M-C, Martens EC, Henrissat B, Gilbert HJ (2017) Complex pectin metabolism by gut bacteria reveals novel catalytic functions. Nature 544:65–73
Normand J, Ralet M-C, Thibault J-F, Rogniaux H, Delavault P, Bonnin E (2010) Purification, characterization and mode of action of a rhamnogalacturonan-hydrolase from Irpex lacteus, tolerant to an acetylated substrate. Appl Microbiol Biotechnol 86:577–588
Ochoa-Jiménez V-A, Berumen-Valera G, Fernandez-Valle R, Tiznado M-E (2018) Rhamnogalacturonan lyase: a pectin modification enzyme of higher plants. Emirate J Food Agric 30:910–917
Ogawa M, Kay P, Wilson S, Swain SM (2009) Arabidopsis dehiscence zone polygalacturonase1 (ADPG1), ADPG2, and QUARTET2 are polygalacturonases required for cell separation during reproductive development in Arabidopsis. Plant Cell 21:216–233
Oh C, Ryu BH, An DR, Nguyen DD, Yoo W, Kim T et al (2016) Structural and biochemical characterization of an octameric carbohydrate acetylesterase from Sinorhizobium meliloti. FEBS Lett 2016(590):1242–1252
Oliveira DM, Mota TR, Oliva B, Segato F, Marchiosi R, Ferrarese-Filho O, Faulds CB, dos Santos WD (2019) Feruloyl esterases: biocatalysts to overcome biomass recalcitrance and for the production of bioactive compounds. Bioresour Technol 278:408–423
Orfila C, Degan FD, Jørgensen B, Scheller HV, Ray PM, Ulvskov P (2012) Expression of mung bean pectin acetyl esterase in potato tubers: effect on acetylation of cell wall polymers and tuber mechanical properties. Planta 236:185–196
Pages S, Valette O, Abdou L, Belaich A, Belaich J-P (2003) A rhamnogalacturonan lyase on the Clostridium cellulolyticum cellulosome. J Bacteriol 185:4727–4733
Peaucelle A, Louvet R, Johansen JN, Höfte H, Laufs P, Pelloux J, Mouille G (2008) Arabidopsis phyllotaxis is controlled by the methyl-esterification status of cell-wall pectins. Curr Biol 18:1943–1948
Peaucelle A, Braybrook SA, Le Guillou L, Bron E et al (2011) Pectin-induced changes in cell wall mechanics underlie organ initiation in Arabidopsis. Curr Biol 21:1720–1726
Pelletier S, Van Orden J, Wolf S et al (2010) A role for pectin de-methylesterification in a developmentally regulated growth acceleration in dark-grown Arabidopsis hypocotyls. New Phytol 188:726–739
Pelloux J, Rusterucci C, Mellerowicz EJ (2007) New insights into pectin methylesterase structure and function. Tr Plant Sci 12:267–277
Petersen TN, Christgau S, Kofod LV, Kauppinen MS, Dalbøge H, Johnson AH (1997) Crystallization and preliminary X-ray studies of rhamnogalacturonase A from Aspergillus aculeatus. Acta Crystallogr D 53:105–107
Philippe F, Pelloux J, Rayon C (2017) Plant pectin acetylesterase structure and function: new insights from bioinformatic analysis. BMC Genomics 18:456
Pickersgill R, Jenkins J, Harris G, Nasser W, Robert-Baudouy J (1994) The structure of Bacillus subtilis pectate lyase in complex with calcium. Nat Struct Biol 1:717–723
Posé S, Kirby AR, Paniagua C, Waldron KW, Morris VJ, Quesada MA, Mercado JA (2013) The nanostructural characterization of strawberry pectins in pectate lyase or polygalacturonase silenced fruits elucidates their role in softening. Carbohydr Polym 132:134–145
Raiola A, Lionetti V, Elmaghraby I, Immerzeel P, Mellerowicz E et al (2011) Pectin methylesterase is induced in Arabidopsis upon infection and is necessary for a successful colonization by necrotrophic pathogens. Mol Plant Microbe Interact 24:432–440
Ralet M-C, Cabrera J-C, Bonnin E, Quemener B, Hellin P, Thibault J-F (2005) Mapping sugar beet pectin acetylation pattern. Phytochemistry 66:1832–1843
Ravanal MC, Eyzaguirre J (2015) Heterologous expression and characterization of α-L-arabinofuranosidase 4 from Penicillium purpurogenum and comparison with the other isoenzymes produced by the fungus. Fungal Biol 119:641–647
Rhee SY, Osborne E, Poindexter P, Somerville C (2003) Microspore separation in the quartet 3 mutants of Arabidopsis is impaired by a defect in a developmentally regulated polygalacturonase required for pollen mother cell wall degradation. Plant Physiol 133:1170–1180
Ross HA, Wright KM, McDougall GJ, Roberts AG et al (2011) Potato tuber pectin structure is influenced by pectin methyl esterase activity and impacts on cooked potato texture. J Exp Bot 62:371–381
Rui Y, Xiao C, Yi H, Kandemir B, Wang JZ, Puri VM, Anderson CT (2017) Polygalacturonase involved in expansion3 functions in seedling development, rosette growth, and stomatal dynamics in Arabidopsis thaliana. Plant Cell 29:2413–2432
Sakamoto T, Ishimaru M (2013) Peculiarities and applications of galactanolytic enzymes that act on type I and II arabinogalactans. Appl Microbiol Biotechnol 97:5201–5213
Sakamoto T, Thibault J-F (2001) Exo-arabinanase of Penicillium chrysogenum able to release arabinobiose from α-1,5-L-arabinan. Appl Environ Microbiol 67:3319–3321
Sakamoto M, Shirane Y, Naribayashi I, Kimura K, Morishita N, Sakamoto T, Sakai T (1994) Purification and characterization of a rhamnogalacturonase with protopectinase activity from Trametes sanguinea. Eur J Biochem 226:285–291
Sakamoto T, Bonnin E, Thibault J-F (2002) Purification and characterisation of two exo-polygalacturonases from Aspergillus niger able to degrade xylogalacturonan and acetylated homogalacturonan. Biochim Biophys Acta 1572:10–18
Sakamoto T, Ogura A, Inui M, Tokuda S, Hosokawa S, Ihara H, Kasai N (2011a) Identification of a GH62 α-L-arabinofuranosidase specific for arabinoxylan produced by Penicillium chrysogenum. Appl Microbiol Biotechnol 90:137–146
Sakamoto T, Tanaka H, Nishimura Y, Ishimaru M, Kasai N (2011b) Characterization of an exo-β-1,3-D-galactanase from Sphingomonas sp. 24T and its application to structural analysis of larch wood arabinogalactan. Appl Microbiol Biotechnol 90:1701–1710
Sakamoto T, Inui M, Yasui K, Hosokawa S, Idhara H (2013a) Substrate specificity and gene expression of two Penicillium chrysogenum α-L-arabinofuranosidases (AFQ1 and AFS1) belonging to glycoside hydrolase families 51 and 54. Appl Microbiol Biotechnol 97:1121–1130
Sakamoto T, Nishimura Y, Makino Y, Sunagawa Y, Harada N (2013b) Biochemical characterization of a GH53 endo-β-1,4-galactanase and a GH35 exo-β-1,4-galactanase from Penicillium chrysogenum. Appl Microbiol Biotechnol 97:2895–2906
Santiago-Doménech N, Jiménez-Bemúdez S, Matas AJ, Rose JK, Muñoz-Blanco J, Mercado JA, Quesada MA (2008) Antisense inhibition of a pectate lyase gene supports a role for pectin depolymerization in strawberry fruit softening. J Exp Bot 59:2769–2779
Schols HA, Geraeds CCJM, Searle-van Leeuwen MJF, Kormelink FJM, Voragen AGJ (1990) Rhamnogalacturonase : a novel enzyme that degrades the hairy regions of pectins. Carbohydr Res 206:105–115
Searle-van Leeuwen MJF, van der Broek LAM, Schols HA, Beldman G, Voragen AGJ (1992) Rhamnogalacturonan acetylesterase: a novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy regions of pectins. Appl Microbiol Biotechnol 38:347–349
Searle-van Leeuwen MJF, Vincken J-P, Schipper D, Voragen AGJ, Beldman G (1996) Acetyl esterases of Aspergillus niger: purification and mode of action on pectins. In: Visser J, Voragen AGJ (eds) Pectins and pectinases. Elsevier, Amsterdam, pp 793–798
Sénéchal F, Wattier C, Rustérucci C, Pelloux J (2014) Homogalacturonan-modifying enzymes: structure, expression, and roles in plants. J Exp Bot 65:5125–5560
Sénéchal F, L’Enfant M, Domon JM, Rosiau E, Crépeau MJ et al (2015) Tuning of pectin methylesterification: Pectin methylesterase inhibitor 7 modulates the processive activity of co-expressed pectin methylesterase 3 in a pH-dependent manner. J Biol Chem 290:23320–22335
Sénéchal F, Habrylo O, Hocq L, Domon JM, Marcelo P, Lefebvre V, Pelloux J, Mercadante D (2017) Structural and dynamical characterization of the pH-dependence of the pectin methylesterase-pectin methylesterase inhibitor complex. J Biol Chem 292:21538–21547
Shevchik VE, Hugouvieux-Cotte-Pattat N (2003) PaeX, a second pectin acetylesterase of Erwinia chrysanthemi 3937. J Bacteriol 185:3091–3100
Shimizu T, Nakatsu T, Miyairi K, Okuno T, Kato H (2002) Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution. Biochemist 41:6651–6659
Shinozaki A, Hosokawa S, Nakazawa M, Ueda M, Sakamoto T (2015) Identification and characterization of three Penicillium chrysogenum α-L-arabinofuranosidases (PcABF43B, PcABF51C, and AFQ1) with different specificities toward arabino-oligosaccharides. Enzym Microb Technol 73-74:65–71
Siedlecka A, Wiklund S, Péronne MA, Micheli F, Lesniewska J et al (2008) Pectin methyl esterase inhibits intrusive and symplastic cell growth in developing wood cells of Populus. Plant Physiol 146:554–565
Stranne M, Sakuragi Y (2016) Arabinan: biosynthesis and a role in host-pathogen interactions. In: Collinge DB (ed) Plant pathogen resistance biotechnology. Wiley, Hoboken, pp 91–103
Stratilova E, Markovic O, Dzurova M, Malovikava A, Capek P, Omelkova J (1998) The pectolytic enzymes of carrots. Biologia 53:731–738
Sun L, Van Nocker S (2010) Analysis of promoter activity of members of the pectate lyase-like (PLL) gene family in cell separation in Arabidopsis. BMC Plant Biol 10:1–13
Suykerbuyk MEG, Kester HCM, Schaap PJ, Stam H, Musters W, Visser J (1997) Cloning and characterization of two rhamnogalacturonan hydrolase genes from Aspergillus niger. Appl Environ Microbiol 63:2507–2515
Tabachnikov O, Shoham Y (2013) Functional characterization of the galactan utilization system of Geobacillus stearothermophilus. FEBS J 280:950–964
The International Brachypodium Initiative (2010) Genome sequencing and analysis of the model grass Brachypodium distachyon. Nature 463(7282):763–768
Turbant A, Fournet F, Lequart M, Zabijak L, Pageau K, Bouton S, Van Wuytswinkel O (2016) PME58 plays a role in pectin distribution during seed coat mucilage extrusion through homogalacturonan modification. J Exp Bot 67:2177–2190
Udatha DBRKG, Kouskoumvekaki I, Olsson L, Panagiotou G (2011) The interplay of descriptor-based computational analysis with pharmacophore modeling builds the basis for a novel classification scheme for feruloyl esterases. Biotechnol Adv 29:94–110
Van Dijk C, Boeriu C, Stolle-Smits T, Tijskens LMM (2006) The firmness of stored tomatoes (cv. Tradiro). 2. Kinetic and near infrared models to describe pectin degrading enzymes and firmness loss. J Food Eng 77:585–593
Vilches F, Ravanal MC, Bravo-Moraga F, Gonzalez-Nilo D, Eyzaguirre J (2018) Penicillium purpurogenum produces a novel endo-1,5-arabinanase, active on debranched arabinan, short arabinooligosaccharides and on the artificial substrate p-nitrophenyl arabinofuranoside. Carbohydr Res 455:106–113
Vogel J, Raab T, Schiff C, Somerville S (2002) PMR6, a pectate lyase–like gene required for powdery mildew susceptibility in Arabidopsis. Plant Cell 14:2095–2106
Voxeur A, Habrylo O, Guénin S, Miart F, Soulié M-C, Rihouey C, Pau-Roblot C, Domon J-M, Gutierrez L, Pelloux J, Mouille G, Fagard M, Höfte H, Vernhettes S (2019) Oligogalacturonide production upon Arabidopsis thaliana–Botrytis cinerea interaction. Proc Natl Acad Sci U S A 116(39):19743–19752
Wakasa Y, Kudo H, Ishikawa R, Akada S, Senda M, Niizeki M, Harada T (2006) Low expression of an ENDOPOLYGALACTURONASE gene in apple fruit with long-term storage potential. Postharvest Biol Technol 39:193–198
Wang D, Yeats TH, Uluisik S, Rose JKC, Seymour GB (2018) Fruit softening: revisiting the role of pectin. Trends Plant Sci 23:302–310
Wefers D, Dong J, Abdel-Hamid A, Paul HM, Pereira GV, Han Y, Dodd D, Baskaran R, Mayer B, Mackie RI, Cann IKO (2017) Enzymatic mechanism for arabinan degradation and transport in the thermophilic bacterium Caldanaerobius polysaccharolyticus. Appl Environ Microbiol 83:e00794–e00717
Wen B, Ström A, Tasker A, West G, Tucker GA (2013) Effect of silencing the two major tomato fruit pectin methylesterase isoforms on cell wall pectin metabolism. Plant Biol 15:1025–1032
Williamson G (1991) Purification and characterization of pectin acetylesterase from orange peel. Phytochemistry 30:445–449
Wolf S, Rausch T, Greiner S (2009) The N-terminal pro region mediates retention of unprocessed type-I PME in the Golgi apparatus. Plant J 58:361–375
Wolf S, Mravec J, Greiner S, Mouille G, Höfte H (2012) Plant cell wall homeostasis is mediated by brassinosteroid feedback signaling. Curr Biol 22:1732–1737
Xiao C, Somerville C, Anderson CT (2014) Polygalacturonase involved in expansion1 functions in cell elongation and flower development in Arabidopsis. Plant Cell 26:1018–1035
Xiao C, Barnes WJ, Zamil MS, Yi H, Puri VM, Anderson CT (2017) Activation tagging of Arabidopsis polygalacturonase involved in expansion2 promotes hypocotyl elongation, leaf expansion, stem lignification, mechanical stiffening, and lodging. Plant J 89:1159–1173
Yang Y, Zhang L, Guo M, Sun J, Matsukawa S, Xie J, Wei D (2015) Novel α-L-Arabinofuranosidase from Cellulomonas fimi ATCC 484 and its substrate-specificity analysis with the aid of computer. J Agric Food Chem 63:3725–3733
Yang L, Huang W, Xiong F, Xian Z, Su D, Ren M, Li Z (2017) Silencing of SlPL, which encodes a pectate lyase in tomato, confers enhanced fruit firmness, prolonged shelf-life and reduced susceptibility to grey mould. Plant Biotechnol J 12:1544–1555
Yang Y, Yu Y, Liang Y, Anderson CT, Cao J (2018) A profusion of molecular scissors for pectins: classification, expression, and functions of plant polygalacturonases. Front Plant Sci 9:1208
Yoshimi Y, Yaguchi K, Kaneko S, Tsumuraya Y, Kotake T (2017) Properties of two fungal endo-β-1,3-galactanases and their synergistic action with an exo-β-1,3-galactanase in degrading arabinogalactan-proteins. Carbohydr Res 453-454:26–35
Zandleven JS, Beldman G, Bosveld M, Benen JAE, Voragen AGJ (2005) Mode of action of xylogalacturonan hydrolase towards xylogalacturonan and xylogalacturonan oligosaccharides. Biochem J 387:719–725
Zandleven JS, Beldman G, Bosveld M, Schols HA, Voragen AGJ (2006) Enzymatic degradation studies of xylogalacturonans from apple and potato, using xylogalacturonan hydrolase. Carbohydr Polym 65:495–503
Zhang L, Wang P, Chen F, Lai S, Yu H, Yang H (2019) Effects of calcium and pectin methylesterase on quality attributes and pectin morphology of jujube fruit under vacuum impregnation during storage. Food Chem 289:40–48
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Bonnin, E., Pelloux, J. (2020). Pectin Degrading Enzymes. In: Kontogiorgos, V. (eds) Pectin: Technological and Physiological Properties. Springer, Cham. https://doi.org/10.1007/978-3-030-53421-9_3
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