Abstract
Arabinoxylans (AXs) are hemicellulosic polysaccharides consisting of a linear backbone of β-1,4-linked xylose residues branched by high content of α-L-arabinofuranosyl (Araf) residues along with other side-chain substituents, and are abundantly found in various agricultural crops especially cereals. The efficient bioconversion of AXs into monosaccharides, oligosaccharides and/or other chemicals depends on the synergism of main-chain enzymes and de-branching enzymes. Exo-α-L-arabinofuranosidases (ABFs) catalyze the hydrolysis of terminal non-reducing α-1,2-, α-1,3- or α-1,5- linked α-L-Araf residues from arabinose-substituted polysaccharides or oligosaccharides. ABFs are critically de-branching enzymes in bioconversion of agricultural biomass, and have received special attention due to their application potentials in biotechnological industries. In recent years, the researches on microbial ABFs have developed quickly in the aspects of the gene mining, properties of novel members, catalytic mechanisms, methodologies, and application technologies. In this review, we systematically summarize the latest advances in microbial ABFs, and discuss the future perspectives of the enzyme research.
Graphical abstract
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Data availability
All the data generated or analyzed during this review are available in the references cited within this article.
Abbreviations
- ABF(s):
-
exo-α-L-arabinofuranosidase(s)
- Araf :
-
α-L-arabinofuranosyl
- AX(s):
-
Arabinoxylan(s)
- AXH(s):
-
AX-α-L-arabinofuranohydrolase(s)
- AXOS:
-
Arabinoxylooligosaccharides
- CAZymes:
-
Carbohydrate-active enzymes
- CBM(s):
-
Carbohydrate binding module(s)
- RAX:
-
Rye arabinoxylan
- WAX:
-
Wheat arabinoxylan
- Xylp :
-
β-D-xylopyranosyl
- XOS:
-
Xylooligosaccharides
- NSP:
-
Non-starch polysaccharides
References
Ahmed S, Luis AS, Bras JLA, Ghosh A, Gautam S, Gupta MN, Fontes CMGA, Goyal A (2013) A novel α-L-arabinofuranosidase of family 43 glycoside hydrolase (Ct43Araf ) from Clostridium thermocellum. PLoS ONE 8(9):e73575. https://doi.org/10.1371/journal.pone.0073575
Arab-Jaziri F, Bissaro B, Dion M, Saurel O, Harrison D, Ferreira F, Milon A, Tellier C, Fauré R, O’Donohue MJ (2013) Engineering transglycosidase activity into a GH51 α-L-arabinofuranosidase. New Biotechnol 30(5):536–544. https://doi.org/10.1016/j.nbt.2013.04.002
Arab-Jaziri F, Bissaro B, Tellier C, Dion M, Fauré R, O’Donohue MJ (2015) Enhancing the chemoenzymatic synthesis of arabinosylated xylo-oligosaccharides by GH51 α-L-arabinofuranosidase. Carbohydr Res 401:64–72. https://doi.org/10.1016/j.carres.2014.10.029
Arti D, Park JMJ, Jung TY, Song HN, Jang MU, Han NS, Kim TJ, Woo EJ (2012) Structural analysis of α-L-arabinofuranosidase from Thermotoga maritima reveals characteristics for thermostability and substrate specificity. J Microbiol Biotechnol 22(12):1724–1730. https://doi.org/10.4014/jmb.1208.08043
Baruah J, Nath BK, Sharma R, Kumar S, Deka RC, Baruah DC, Kalita E (2018) Recent trends in the pretreatment of lignocellulosic biomass for value-added products. Front Energy Res 6:141. https://doi.org/10.3389/fenrg.2018.00141
Bastien G, Arnal G, Bozonnet S, Laguerre S, Ferreira F, Fauré R, Henrissat B, Lefèvre F, Robe P, Bouchez O, Noirot C, Dumon C, O’Donohue M (2013) Mining for hemicellulases in the fungus-growing termite Pseudacanthotermes militaris using functional metagenomics. Biotechnol Biofuels 6:78. https://doi.org/10.1186/1754-6834-6-78
Baudrexl M, Fida T, Berk B, Schwarz WH, Zverlov VV, Groll M, Liebl W (2022) Biochemical and structural characterization of thermostable GH159 glycoside hydrolases exhibiting α-L-arabinofuranosidase activity. Front Mol Biosci 9:907439. https://doi.org/10.3389/fmolb.2022.907439
Bezalel L, Shoham Y, Rosenberg E (1993) Characterization and delignification activity of a thermostable α-L-arabinofuranosidase from Bacillus stearothermophilus. Appl Microbiol Biotechnol 40:57–62
Bhattacharya A, Ruthes A, Vilaplana F, Karlsson EN, Adlecreutz P, Stålbrand H (2020) Enzyme synergy for the production of arabinoxylo-oligosaccharides from highly substituted arabinoxylan and evaluation of their prebiotic potential. Lwt-Food Sci Technol 131:109762. https://doi.org/10.1016/j.lwt.2020.109762
Borsenberger V, Dornez E, Desrousseaux M-L, Courtin CM, O’Donohue MJ, Fauré R (2013) A substrate for the detection of broad specificity α-L-arabinofuranosidases with indirect release of a chromogenic group. Tetrahedron Lett 54(24):3063–3066. https://doi.org/10.1016/j.tetlet.2013.03.136
Borsenberger V, Dornez E, Desrousseaux ML, Massou S, Tenkanen M, Courtin CM, Dumon C, O’Donohue MJ, Fauré R (2014) A 1H NMR study of the specificity of α-L-arabinofuranosidases on natural and unnatural substrates. Biochimica Biophys Acta Gen Subj 1840(10):3106–3114. https://doi.org/10.1016/j.bbagen.2014.07.001
Bouraoui H, Desrousseaux ML, Ioannou E, Alvira P, Manaï M, Rémond C, Dumon C, Fernandez-Fuentes N, O’Donohue MJ (2016) The GH51 alpha-L-arabinofuranosidase from Paenibacillus sp.THS1 is multifunctional, hydrolyzing main-chain and side-chain glycosidic bonds in heteroxylans. Biotechnol Biofuels 9:140. https://doi.org/10.1186/s13068-016-0550-x
Cárdenas-Fernández M, Hamley-Bennett C, Leak DJ, Lye GJ (2018) Continuous enzymatic hydrolysis of sugar beet pectin and L-arabinose recovery within an integrated biorefinery. Bioresource Technol 269:195–202. https://doi.org/10.1016/j.biortech.2018.08.069
Cartmell A, McKee LS, Peña MJ, Larsbrink J, Brumer H, Sa K, Ichinose H, Lewis RJ, Viksø-Nielsen A, Gilbert HJ, Marles-Wright J (2011) The structure and function of an arabinan-specific α-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases. J Biol Chem 286(17):15483–15495. https://doi.org/10.1074/jbc.M110.215962
Chettri D, Verma AK, Verma AK (2020) Innovations in CAZyme gene diversity and its modification for biorefinery applications. Biotechnol Rep 28:e00525. https://doi.org/10.1016/j.btre.2020.e00525
Couturier M, Haon M, Coutinho PM, Henrissat B, Lesage-Meessen L, Berrin JG (2011) Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl Environ Microbiol 77(1):237–246. https://doi.org/10.1128/AEM.01761-10
Cozannet P, Kidd MT, Montanhini Neto R, Geraert PA (2017) Next-generation non-starch polysaccharide-degrading, multi-carbohydrase complex rich in xylanase and arabinofuranosidase to enhance broiler feed digestibility. Poult Sci 96(8):2743–2750. https://doi.org/10.3382/ps/pex084
Culleton H, McKie VA, de Vries RP (2014) Overexpression, purification and characterisation of homologous alpha-L-arabinofuranosidase and endo-1,4-beta-D-glucanase in Aspergillus vadensis. J Ind Microbiol Biotechnol 41(11):1697–1708. https://doi.org/10.1007/s10295-014-1512-6
De La Mare M, Guais O, Bonnin E, Weber J, Francois JM (2013) Molecular and biochemical characterization of three GH62 α-L-arabinofuranosidases from the soil deuteromycete Penicillium funiculosum. Enzym Microb Technol 53(5):351–358. https://doi.org/10.1016/j.enzmictec.2013.07.008
de Wet BJM, Matthew MKA, Storbeck KH, van Zyl WH, Prior BA (2008) Characterization of a family 54 α-L-arabinofuranosidase from Aureobasidium pullulans. Appl Microbiol Biotechnol 77(5):975–983. https://doi.org/10.1007/s00253-007-1235-y
Dionisi HM, Lozada M, Campos E (2023) Diversity of GH51 α-L-arabinofuranosidase homolog sequences from subantarctic intertidal sediments. Biologia 78:1899–1918. https://doi.org/10.1007/s11756-023-01382-x
dos Santos CR, de Giuseppe PO, de Souza FHM, Zanphorlin LM, Domingues MN, Pirolla RAS, Honorato RV, Tonoli CCC, de Morais MAB, de Matos Martins VP, Fonseca LM, Büchli F, de Oliveira PSL, Gozzo FC, Murakami MT (2018) The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans. Biotechnol Biofuels 11(1):223. https://doi.org/10.1186/s13068-018-1212-y
Dumorne K, Córdova DC, Astorga-Eló M, Renganathan P (2017) Extremozymes: a potential source for industrial applications. J Microbiol Biotechnol 27(4):649–659. https://doi.org/10.4014/jmb.1611.11006
Escamilla-Alvarado C, Pérez-Pimienta JA, Ponce-Noyola T, Poggi-Varaldo HM (2017) An overview of the enzyme potential in bioenergy-producing biorefineries. J Chem Technol Biotechnol 92(5):906–924. https://doi.org/10.1002/jctb.5088
Fehér C (2018) Novel approaches for biotechnological production and application of L-arabinose. J Carbohyd Chem 37(5):251–284. https://doi.org/10.1080/07328303.2018.1491049
Fortune B, Mhlongo S, van Zyl LJ, Huddy R, Smart M, Trindade M (2019) Characterisation of three novel alpha-L-arabinofuranosidases from a compost metagenome. BMC Biotechnol 19(1):22. https://doi.org/10.1186/s12896-019-0510-1
Fujimoto Z, Ichinose H, Maehara T, Honda M, Kitaoka M, Kaneko S (2010) Crystal structure of an exo-1,5-α-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo-and endo-type enzymes in glycoside hydrolase family 43. J Biol Chem 285(44):34134–34143. https://doi.org/10.1074/jbc.M110.164251
Gao L, Li S, Xu Y, Xia C, Xu J, Liu J, Qin Y, Song X, Liu G, Qu Y (2019) Mutation of a conserved alanine residue in transcription factor araR leads to hyperproduction of alpha-L-arabinofuranosidases in Penicillium oxalicum. Biotechnol J 14(7):1800643. https://doi.org/10.1002/biot.201800643
Geng A, Wu J, Xie R, Wang H, Wu Y, Li X, Chang F, Sun J (2019) Highly thermostable GH51 α-arabinofuranosidase from Hungateiclostridium clariflavum DSM 19732. Appl Microbiol Biotechnol 103(9):3783–3793. https://doi.org/10.1007/s00253-019-09753-8
Giacobbe S, Vincent F, Faraco V (2014) Development of an improved variant of GH51 α-L-arabinofuranosidase from Pleurotus ostreatus by directed evolution. New Biotechnol 31(3):230–236. https://doi.org/10.1016/j.nbt.2014.02.004
Gilbert HJ, Knox JP, Boraston AB (2013) Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules. Curr Opin Struct Biol 23(5):669–677. https://doi.org/10.1016/j.sbi.2013.05.005
Gonçalves TA, Damásio AR, Segato F, Alvarez TM, Bragatto J, Brenelli LB, Citadini AP, Murakami MT, Ruller R, Paes Leme AF, Prade RA, Squina FM (2012) Functional characterization and synergic action of fungal xylanase and arabinofuranosidase for production of xylooligosaccharides. Bioresour Technol 119:293–299. https://doi.org/10.1016/j.biortech.2012.05.062
Hassan N, Kori LD, Gandini R, Patel BK, Divne C, Tan TC (2015) High-resolution crystal structure of a polyextreme GH43 glycosidase from Halothermothrix orenii with α-L-arabinofuranosidase activity. Acta Crystallogr F Struct Biol Commun F71:338–345. https://doi.org/10.1107/S2053230X15003337
Hidalgo-Cantabrana C, Delgado S, Ruiz L, Ruas-Madiedo P, Sánchez B, Margolles A (2017) Bifidobacteria and their health-promoting effects. Microbiol Spectrum. https://doi.org/10.1128/microbiolspec.BAD-0010-2016
Houfani AA, Anders N, Spiess AC, Baldrian P, Benallaoua S (2020) Insights from enzymatic degradation of cellulose and hemicellulose to fermentable sugars–a review. Biomass Bioenergy 134:105481. https://doi.org/10.1016/j.biombioe.2020.105481
Hövel K, Shallom D, Niefind K, Belakhov V, Shoham G, Baasov T, Shoham Y, Schomburg D (2003) Crystal structure and snapshots along the reaction pathway of a family 51 α-L-arabinofuranosidase. Embo J 22(19):4922–4932. https://doi.org/10.1093/emboj/cdg494
Hu Y, Zhao Y, Tian S, Zhang G, Li Y, Li Q, Gao J (2018) Screening of a novel glycoside hydrolase family 51 α-L-arabinofuranosidase from Paenibacillus polymyxa KF-1: cloning, expression, and characterization. Catalysts 8(12):589. https://doi.org/10.3390/catal8120589
Huang D, Liu J, Qi Y, Yang K, Xu Y, Feng L (2017) Synergistic hydrolysis of xylan using novel xylanases, β-xylosidases, and an α-L-arabinofuranosidase from Geobacillus thermodenitrificans NG80-2. Appl Microbiol Biotechnol 101(15):6023–6037. https://doi.org/10.1007/s00253-017-8341-2
Jaafar NR, Ayob SN, Abd Rahman NH, Abu Bakar FD, Murad AMA, Illias RM (2021) Rational protein engineering of α-L-arabinofuranosidase from Aspergillus niger for improved catalytic hydrolysis efficiency on kenaf hemicellulose. Process Biochem 102:349–359. https://doi.org/10.1016/j.procbio.2020.12.012
Ji MG, Lee YR, Nam YH, Castañeda R, Hong BN, Kang TH (2020) Immunostimulatory action of high-content active arabinoxylan in rice bran. ACS Omega 5(41):26374–26381. https://doi.org/10.1021/acsomega.0c02472
Ji M, Li S, Chen A, Liu Y, Xie Y, Duan H, Shi J, Sun J (2021) A wheat bran inducible expression system for the efficient production of α-L-arabinofuranosidase in Bacillus subtilis. Enzyme Microbial Technol 144:109726. https://doi.org/10.1016/j.enzmictec.2020.109726
Jia L, Budinova GALG, Takasugi Y, Noda S, Tanaka T, Ichinose H, Goto M, Kamiya N (2016) Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase. Biochem Eng J 114:268–275. https://doi.org/10.1016/j.bej.2016.07.013
Kaji A, Yoshihara O (1969) Production and properties of α-L-Arabinofuranosidase from Corticium rolfsii. Appl Microbiol 17(6):910–913. https://doi.org/10.1128/am.17.6.910-913.1969
Kaji A, Tagawa K, Ichimi T (1969) Properties of purified α-L-arabinofuranosidae from Aspergillus niger. Biochim Biophys Acta-Enzym 171(1):186–188. https://doi.org/10.1016/0005-2744(69)90118-1
Kaur AP, Nocek BP, Xu X, Lowden MJ, Leyva JF, Stogios PJ, Cui H, Di Leo R, Powlowski J, Tsang A, Savchenko A (2015) Functional and structural diversity in GH62 α-L-arabinofuranosidases from the thermophilic fungus Scytalidium thermophilum. Microb Biotechnol 8(3):419–433. https://doi.org/10.1111/1751-7915.12168
Komeno M, Hayamizu H, Fujita K, Ashida H (2019) Two novel α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum belonging to glycoside hydrolase family 43 cooperatively degrade arabinan. Appl Environ Microbiol 85(6):e02582-e2618. https://doi.org/10.1128/AEM.02582-18
Komeno M, Yoshihara Y, Kawasaki J, Nabeshima W, Maeda K, Sasaki Y (2022) Two α-L-arabinofuranosidases from Bifidobacterium longum subsp. longum are involved in arabinoxylan utilization. Appl Microbiol Biotechnol 106:1957–1965. https://doi.org/10.1007/s00253-022-11845-x
Koseki T, Okuda M, Sudoh S, Kizaki Y, Iwano K, Aramaki I, Matsuzawa H (2003) Role of two α-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori. J Biosci Bioeng 96(3):232–241. https://doi.org/10.1016/S1389-1723(03)80187-1
Kotake T, Tsuchiya K, Aohara T, Konishi T, Kaneko S, Igarashi K, Samejima M, Tsumuraya Y (2006) An α-L-arabinofuranosidase/β-D-xylosidase from immature seeds of radish (Raphanus sativus L.). J Exp Bot 57(10):2353–2362. https://doi.org/10.1093/jxb/erj206
Koutaniemi S, Tenkanen M (2016) Action of three GH51 and one GH54 α-arabinofuranosidases on internally and terminally located arabinofuranosyl branches. J Biotechnol 229:22–30. https://doi.org/10.1016/j.jbiotec.2016.04.050
Kurakake M, Kanbara Y, Murakami Y (2014) Characteristics of α-L-arabinofuranosidase from Streptomyces sp I10–1 for production of L-arabinose from corn hull arabinoxylan. Appl Biochem Biotechnol 172(5):2650–2660. https://doi.org/10.1007/s12010-013-0691-3
Ladha JK, Tirol-Padre A, Reddy CK, Cassman KG, Verma S, Powlson DS, van Kessel C, de B. Richter D, Chakraborty D, Pathak H (2016) Global nitrogen budgets in cereals: a 50-year assessment for maize, rice, and wheat production systems. Sci Rep 6:19355. https://doi.org/10.1038/srep19355
Lee RC, Hrmova M, Burton RA, Lahnstein J, Fincher GB (2003) Bifunctional family 3 glycoside hydrolases from barley with α-L-arabinofuranosidase and β-D-xylosidase activity: Characterization, primary structures, and COOH-terminal processing. J Biol Chem 278(7):5377–5387. https://doi.org/10.1074/jbc.M210627200
Leschonski KP, Kaasgaard SG, Spodsberg N, Krogh KBRM, Kabel MA (2022) Two subgroups within the GH43_36 α-L-arabinofuranosidase subfamily hydrolyze arabinosyl from either mono-or disubstituted xylosyl units in wheat arabinoxylan. Int J Mol Sci 23:13790. https://doi.org/10.3390/ijms232213790
Li X, Xie X, Liu J, Wu D, Cai G, Lu J (2020) Characterization of a putative glycoside hydrolase family 43 arabinofuranosidase from Aspergillus niger and its potential use in beer production. Food Chem 305:125382. https://doi.org/10.1016/j.foodchem.2019.125382
Limsakul P, Phitsuwan P, Waeonukul R, Pason P, Tachaapaikoon C, Poomputsa K, Kosugi A, Ratanakhanokchaia K (2021) A novel multifunctional arabinofuranosidase/endoxylanase/ß-xylosidase GH43 enzyme from Paenibacillus curdlanolyticus B-6 and its synergistic action to produce arabinose and xylose from cereal arabinoxylan. Appl Environ Microbiol 87:e01730-e1821. https://doi.org/10.1128/AEM.01730-21
Linares NC, Li X, Dilokpimol A, de Vries RP (2022) Comparative characterization of nine novel GH51, GH54 and GH62 α-L-arabinofuranosidases from Penicillium subrubescens. FEBS Lett 596:360–368. https://doi.org/10.1002/1873-3468.14278
Linares-Pastén JA, Falck P, Albasri K, Kjellstrom S, Adlercreutz P, Logan DT, Karlsson EN (2017) Three-dimensional structures and functional studies of two GH43 arabinofuranosidases from Weissella sp. strain 142 and Lactobacillus brevis. FEBS J 284(13):2019–2036. https://doi.org/10.1111/febs.14101
Long L, Sun L, Lin Q, Ding S, St John FJ (2020) Characterization and functional analysis of two novel thermotolerant α-L-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum. Appl Microbiol Biotechnol 104:8719–8733. https://doi.org/10.1007/s00253-020-10867-7
Long L, Sun L, Liu Z, Lin Q, Wang J, Ding S (2022) Functional characterization of a GH62 family α-L-arabinofuranosidase from Eupenicillium parvum suitable for monosaccharification of corncob arabinoxylan in combination with key enzymes. Enzym Microb Technol 154:109965. https://doi.org/10.1016/j.enzmictec.2021.109965
Long L, Wang W, Liu Z, Lin Y, Wang J, Lin Q, Ding S (2023) Insights into the capability of the lignocellulolytic enzymes of Penicillium parvum 4–14 to saccharify corn bran after alkaline hydrogen peroxide pretreatment. Biotechnol Biofuels Bioprod 16:79. https://doi.org/10.1186/s13068-023-02319-x
Maehara T, Fujimoto Z, Ichinose H, Michikawa M, Harazono K, Kaneko S (2014) Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor. J Biol Chem 289(11):7962–7972. https://doi.org/10.1074/jbc.M113.540542
Malgas S, Mafa MS, Mathibe BN, Pletschke BI (2021) Unraveling synergism between various GH family xylanases and debranching enzymes during hetero-xylan degradation. Molecules 26:6770. https://doi.org/10.3390/molecules26226770
Manisseri C, Gudipati M (2010) Bioactive xylo-oligosaccharides from wheat bran soluble polysaccharides. Lwt-Food Sci Technol 43(3):421–430. https://doi.org/10.1016/j.lwt.2009.09.004
Marcolongo L, Ionata E, La Cara F, Amore A, Giacobbe S, Pepe O, Faraco V (2014) The effect of Pleurotus ostreatus arabinofuranosidase and its evolved variant in lignocellulosic biomasses conversion. Fungal Genet Biol 72:162–167. https://doi.org/10.1016/j.fgb.2014.07.003
Margolles-Clark E, Tenkanen M, Nakari-Setälä T, Penttila M (1996) Cloning of genes encoding α-L-arabinofuranosidase and β-xylosidase from Trichoderma reesei by expression in Saccharomyces cerevisiae. Appl Environ Microbiol 62(10):3840–3846. https://doi.org/10.1128/aem.62.10.3840-3846.1996
Martínez C, Gertosio C, Labbe A, Perez R, Ganga MA (2006) Production of Rhodotorula glutinis: a yeast that secretes α-L-arabinofuranosidase. Electron J Biotechnol 9(4):407–413. https://doi.org/10.2225/vol9-issue4-fulltext-8
Mathew S, Aronsson A, Karlsson EN, Adlercreutz P (2018) Xylo- and arabinoxylooligosaccharides from wheat bran by endoxylanases, utilisation by probiotic bacteria, and structural studies of the enzymes. Appl Microbiol Biotechnol 102(7):3105–3120. https://doi.org/10.1007/s00253-018-8823-x
Maurício da Fonseca MJ, Jurak E, Kataja K, Master ER, Berrin JG, Stals I, Desmet T, Van Landschoot A, Briers Y (2018) Analysis of the substrate specificity of α-L-arabinofuranosidases by DNA sequencer-aided fluorophore-assisted carbohydrate electrophoresis. Appl Microbiol Biotechnol 102(23):10091–10102. https://doi.org/10.1007/s00253-018-9389-3
McCleary BV, McKie VA, Draga A, Rooney E, Mangan D, Larkin J (2015) Hydrolysis of wheat flour arabinoxylan, acid-debranched wheat flour arabinoxylan and arabino-xylo-oligosaccharides by β-xylanase, α-L-arabinofuranosidase and β-xylosidase. Carbohydr Res 407:79–96. https://doi.org/10.1016/j.carres.2015.01.017
McGregor NGS, Artola M, Nin-Hill A, Linzel D, Haon M, Reijngoud J, Ram A, Rosso MN, van der Marel GA, Codée JDC, van Wezel GP, Berrin JG, Rovira C, Overkleeft HS, Davies GJ (2020a) Rational design of mechanism-based inhibitors and activity-based probes for the identification of retaining α-L-arabinofuranosidases. J Am Chem Soc 142(10):4648–4662. https://doi.org/10.1021/jacs.9b11351
McGregor NGS, Turkenburg JP, Mørkeberg Krogh KBR, Nielsen JE, Artola M, Stubbs KA, Overkleeft HS, Davies GJ (2020b) Structure of a GH51 α-L-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi. Acta Crystallogr D Structl Biol 76(11):1124–1133. https://doi.org/10.1107/s205979832001253x
McKee LS, Peña MJ, Rogowski A, Jackson A, Lewis RJ, York WS, Krogh KBRM, Viksø-Nielsen A, Skjøt M, Gilbert HJ, Marles-Wright J (2012) Introducing endo-xylanase activity into an exo-acting arabinofuranosidase that targets side chains. Proc Natl Acad Sci USA 109(17):6537–6542. https://doi.org/10.1073/pnas.1117686109
Mechelke M, Koeck DE, Broeker J, Roessler B, Krabichler F, Schwarz WH, Zverlov VV, Liebl W (2017) Characterization of the arabinoxylan-degrading machinery of the thermophilic bacterium Herbinix hemicellulosilytica-six new xylanases, three arabinofuranosidases and one xylosidase. J Biotechnol 257:122–130. https://doi.org/10.1016/j.jbiotec.2017.04.023
Méndez-Líter JA, de Eugenio LI, Nieto-Domínguez M, Prieto A, Martínez MJ (2023) Expression and characterization of two α-L-arabinofuranosidases from Talaromyces amestolkiae: role of these enzymes in biomass valorization. Int J Mol Sci 24:11997. https://doi.org/10.3390/ijms241511997
Mewis K, Lenfant N, Lombard V, Henrissat B (2016) Dividing the large glycoside hydrolase family 43 into subfamilies: a motivation for detailed enzyme characterization. Appl Environ Microbiol 82(6):1686–1692. https://doi.org/10.1128/AEM.03453-15
Miyanaga A, Koseki T, Matsuzawa H, Wakagi T, Shoun H, Fushinobu S (2004) Crystal structure of a family 54 α-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose. J Biol Chem 279(43):44907–44914. https://doi.org/10.1074/jbc.M405390200
Motta MLL, Filho JAF, de Melo RR, Zanphorlin LM, dos Santos CA, de Souza AP (2021) A novel fungal metal-dependent α-L-arabinofuranosidase of family 54 glycoside hydrolase shows expanded substrate specificity. Sci Rep-UK 11:10961. https://doi.org/10.1038/s41598-021-90490-2
Mroueh M, Aruanno M, Borne R, de Philip P, Fierobe H-P, Tardif C, Pagès S (2019) The xyl-doc gene cluster of Ruminiclostridium cellulolyticum encodes GH43- and GH62-α-L-arabinofuranosidases with complementary modes of action. Biotechnol Biofuels 12:144. https://doi.org/10.1186/s13068-019-1483-y
Naidu DS, Hlangothi SP, John MJ (2018) Bio-based products from xylan: a review. Carbohyd Polym 179:28–41. https://doi.org/10.1016/j.carbpol.2017.09.064
Numan MT, Bhosle NB (2006) α-L-arabinofuranosidases: the potential applications in biotechnology. J Ind Microbiol Biotechnol 33(4):247–260. https://doi.org/10.1007/s10295-005-0072-1
Onipe OO, Jideani AIO, Beswa D (2015) Composition and functionality of wheat bran and its application in some cereal food products. Int J Food Sci Tech 50(12):2509–2518. https://doi.org/10.1111/ijfs.12935
Orita T, Sakka M, Kimura T, Sakka K (2017) Characterization of Ruminiclostridium josui arabinoxylan arabinofuranohydrolase, RjAxh43B, and RjAxh43B-containing xylanolytic complex. Enzym Microb Technol 104:37–43. https://doi.org/10.1016/j.enzmictec.2017.05.008
Paës G, Skov LK, O’Donohue MJ, Rémond C, Kastrup JS, Gajhede M, Mirza O (2008) The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit. Biochemistry 47:7441–7451. https://doi.org/10.1021/bi800424e
Pitkänen L, Virkki L, Tenkanen M, Tuomainen P (2009) Comprehensive multidetector HPSEC study on solution properties of cereal arabinoxylans in aqueous and DMSO solutions. Biomacromol 10(7):1962–1969. https://doi.org/10.1021/bm9003767
Poria V, Saini JK, Singh S, Nain L, Kuhad RC (2020) Arabinofuranosidases: characteristics, microbial production, and potential in waste valorization and industrial applications. Bioresource Technol 304:123019. https://doi.org/10.1016/j.biortech.2020.123019
Pouvreau L, Joosten R, Hinz SWA, Gruppen H, Schols HA (2011) Chrysosporium lucknowense C1 arabinofuranosidases are selective in releasing arabinose from either single or double substituted xylose residues in arabinoxylans. Enzyme Microb Technol 48:397–403. https://doi.org/10.1016/j.enzmictec.2011.01.004
Qing Q, Yang B, Wyman CE (2010) Xylooligomers are strong inhibitors of cellulose hydrolysis by enzymes. Bioresource Technol 101(24):9624–9630. https://doi.org/10.1016/j.biortech.2010.06.137
Ravanal MC, Rosa L, Eyzaguirre J (2012) α-L-arabinofuranosidase 3 from Penicillium purpurogenum (ABF3): potential application in the enhancement of wine flavour and heterologous expression of the enzyme. Food Chem 134(2):888–893. https://doi.org/10.1016/j.foodchem.2012.02.200
Ravn JL, Glitsø V, Pettersson D, Ducatelle R, Van Immerseel F, Pedersen NR (2018) Combined endo-β-1,4-xylanase and α-L-arabinofuranosidase increases butyrate concentration during broiler cecal fermentation of maize glucurono-arabinoxylan. Anim Feed Sci Technol 236:159–169. https://doi.org/10.1016/j.anifeedsci.2017.12.012
Rémond C, Plantier-Royon R, Aubry N, Maes E, Bliard C, O’Donohue MJ (2004) Synthesis of pentose-containing disaccharides using a thermostable α-L-arabinofuranosidase. Carbohydr Res 339(11):2019–2025. https://doi.org/10.1016/j.carres.2004.04.017
Rizk M, Antranikian G, Elleuche S (2012) End-to-end gene fusions and their impact on the production of multifunctional biomass degrading enzymes. Biochem Biophys Res Commun 428(1):1–5. https://doi.org/10.1016/j.bbrc.2012.09.142
Rudjito RC, Jiménez-Quero A, Hamzaoui M, Kohnen S, Vilaplana F (2020) Tuning the molar mass and substitution pattern of complex xylans from corn fibre using subcritical water extraction. Green Chem 22(23):8337–8352. https://doi.org/10.1039/d0gc02897e
Rumpagaporn P, Reuhs BL, Kaur A, Patterson JA, Keshavarzian A, Hamaker BR (2015) Structural features of soluble cereal arabinoxylan fibers associated with a slow rate of in vitro fermentation by human fecal microbiota. Carbohyd Polym 130:191–197. https://doi.org/10.1016/j.carbpol.2015.04.041
Saha BC (2000) α-L-arabinofuranosidases: biochemistry, molecular biology and application in biotechnology. Biotechnol Adv 18(5):403–423. https://doi.org/10.1016/S0734-9750(00)00044-6
Saha BC, Bothast RJ (1998) Effect of carbon source on production of α-L-arabinofuranosidase by Aureobasidium pullulans. Current Microbiol 37:337–340. https://doi.org/10.1007/s002849900388
Sakamoto T, Inui M, Yasui K, Hosokawa S, Ihara H (2013) 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(3):1121–1130. https://doi.org/10.1007/s00253-012-3978-3
Saleh MA, Han WJ, Lu M, Wang B, Li H, Kelly RM, Li FL (2017) Two distinct α-arabinofuranosidases in Caldicellulosiruptor species drive degradation of arabinose-based polysaccharides. Appl Environ Microbiol 83(13):e00574-e617. https://doi.org/10.1128/AEM.00574-17
Saleh AA, Kirrella AA, Abdo SE, Mousa MM, Badwi NA, Ebeid TA, Nada AL, Mohamed MA (2019) Effects of dietary xylanase and arabinofuranosidase combination on the growth performance, lipid peroxidation, blood constituents, and immune response of broilers fed low-energy diets. Animals 9(7):467. https://doi.org/10.3390/ani9070467
Saleh MA, Mahmud S, Albogami S, El-Shehawi AM, Paul GK, Islam S, Dutta AK, Uddin MS, Zaman S (2022) Biochemical and molecular dynamics study of a novel GH43 α-L-arabinofuranosidase/β-xylosidase from Caldicellulosiruptor saccharolyticus DSM8903. Front Bioeng Biotechnol 10:810542. https://doi.org/10.3389/fbioe.2022.810542
Sarch C, Suzuki H, Master ER, Wang W (2019) Kinetics and regioselectivity of three GH62 α-L-arabinofuranosidases from plant pathogenic fungi. Biochim Biophys Acta Gen Subj 6:1070–1078. https://doi.org/10.1016/j.bbagen.2019.03.020
Schendel RR, Puchbauer A-K, Bunzel M (2016) Glycoside hydrolase family 51 α-L-arabinofuranosidases from Clostridium thermocellum and Cellvibrio japonicus release O-5-feruloylated arabinose. Cereal Chem 93(6):650–653. https://doi.org/10.1094/CCHEM-01-16-0011-N
Sharma P, Kaila P, Guptasarma P (2016) Creation of active TIM barrel enzymes through genetic fusion of half-barrel domain constructs derived from two distantly related glycosyl hydrolases. FEBS J 283(23):4340–4356. https://doi.org/10.1111/febs.13927
Shi P, Li N, Yang P, Wang Y, Luo H, Bai Y, Yao B (2010) Gene cloning, expression, and characterization of a family 51 α-L-arabinofuranosidase from Streptomyces sp. S9. Appl Biochem Biotechnol 162(3):707–718. https://doi.org/10.1007/s12010-009-8816-4
Shi H, Li X, Gu H, Zhang Y, Huang Y, Wang L, Wang F (2013a) Biochemical properties of a novel thermostable and highly xylose-tolerant β-xylosidase/α-arabinosidase from Thermotoga thermarum. Biotechnol Biofuels 6:27. https://doi.org/10.1186/1754-6834-6-27
Shi P, Chen X, Meng K, Huang H, Bai Y, Luo H, Yang P, Yao B (2013b) Distinct actions by Paenibacillus sp. Strain E18 α-L-arabinofuranosidases and xylanase in xylan degradation. Appl Environ Microbiol 79:1990–1995. https://doi.org/10.1128/aem.03276-12
Shi H, Zhang Y, Xu B, Tu M, Wang F (2014) Characterization of a novel GH2 family α-L-arabinofuranosidase from hyperthermophilic bacterium Thermotoga thermarum. Biotechnol Lett 36(6):1321–1328. https://doi.org/10.1007/s10529-014-1493-6
Shi H, Gao F, Yan X, Li Q, Nie X (2022) Cloning, expression and characterization of a glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermoanaerobacterium thermosaccharolyticum DSM 571. 3 Biotech 12:176. https://doi.org/10.1007/s13205-022-03254-8
Shin HY, Park SY, Sung JH, Kim DH (2003) Purification and characterization of α-L-arabinopyranosidase and α-L-arabinofuranosidase from Bifidobacterium breve K-110, a human intestinal anaerobic bacterium metabolizing ginsenoside Rb2 and Rc. Appl Environ Microbiol 69(12):7116–7123. https://doi.org/10.1128/aem.69.12.7116-7123.2003
Shin KC, Choi HY, Seo MJ, Oh DK (2015) Compound K production from red ginseng extract by β-glycosidase from sulfolobus solfataricus supplemented with α-L-arabinofuranosidase from Caldicellulosiruptor saccharolyticus. PLoS ONE 10(12):e0145876. https://doi.org/10.1371/journal.pone.0145876
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. https://doi.org/10.1016/j.enzmictec.2015.04.003
Si Z, Cai Y, Zhao L, Han L, Wang F, Yang X, Gao X, Lu M, Liu W (2023) Structure and function characterization of the α-L-arabinofuranosidase from the white-rot fungus Trametes hirsuta. Appl Microbiol Biotechnol 107:3967–3981. https://doi.org/10.1007/s00253-023-12561-w
Siguier B, Haon M, Nahoum V, Marcellin M, Burlet-Schiltz O, Coutinho PM, Henrissat B, Mourey L, O’Donohue MJ, Berrin JG, Tranier S, Dumon C (2014) First structural insights into α-L-arabinofuranosidases from the two GH62 glycoside hydrolase subfamilies. J Biol Chem 289:5261–5273. https://doi.org/10.1074/jbc.M113.528133
Sørensen HR, Jørgensen CT, Hansen CH, Jørgensen CI, Pedersen S, Meyer AS (2006) A novel GH43 α-L-arabinofuranosidase from Humicola insolens: mode of action and synergy with GH51 α-L-arabinofuranosidases on wheat arabinoxylan. Appl Microbiol Biotechnol 73(4):850–861. https://doi.org/10.1007/s00253-006-0543-y
Souza TACB, Santos CR, Souza AR, Oldiges DP, Ruller R, Prade RA, Squina FM, Murakami MT (2011) Structure of a novel thermostable GH51 α-L-arabinofuranosidase from Thermotoga petrophila RKU-1. Protein Sci 20(9):1632–1637. https://doi.org/10.1002/pro.693
Sun J, Xu F, Lu J (2020) A glycoside hydrolase family 62 α-L-arabinofuranosidase from Trichoderma reesei and its applicable potential during mashing. Foods 9(3):356. https://doi.org/10.3390/foods9030356
Sürmeli Y, Şanlı-Mohamed G (2022) Structural and functional analyses of GH51 alpha-L-arabinofuranosidase of Geobacillus vulcani GS90 reveal crucial residues for catalytic activity and thermostability. Biotechnol Appl Bioc 70(3):1100–1108. https://doi.org/10.1002/bab.2423
Taylor EJ, Smith NL, Turkenburg JP, D’Souza S, Gilbert HJ, Davies GJ (2006) Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum. Biochem J 395(1):31–37. https://doi.org/10.1042/BJ20051780
Thakur A, Sharma K, Goyal A (2019) α-L-arabinofuranosidase: a potential enzyme for the food industry. In: Parameswaran B, Varjani S, Raveendran S (eds) Green bio-processes energy, environment, and sustainability. Springer, Singapore, pp 229–244
Thakur A, Sharma K, Jamaldheen SB, Goyal A (2020) Molecular characterization, regioselective and synergistic action of first recombinant type III α-L-arabinofuranosidase of family 43 glycoside hydrolase (PsGH43_12) from Pseudopedobacter saltans. Mol Biotechnol 62(9):443–455. https://doi.org/10.1007/s12033-020-00263-x
Tonozuka T, Tanaka Y, Okuyama S, Miyazaki T, Nishikawa A, Yoshida M (2017) Structure of the catalytic domain of α-L-arabinofuranosidase from Coprinopsis cinerea, CcAbf62A, provides insights into structure-function relationships in glycoside hydrolase family 62. Appl Biochem Biotechnol 181(2):511–525. https://doi.org/10.1007/s12010-016-2227-0
Tsukida R, Yoshida M, Kaneko S (2023) Characterization of an α-L-arabinofuranosidase GH51 from the brown-rot fungus Gloeophyllum trabeum. J Appl Glycosci 70:9–14. https://doi.org/10.5458/jag.jag.JAG-2022_0009
Valls A, Diaz P, Pastor FIJ, Valenzuela SV (2016) A newly discovered arabinoxylan-specific arabinofuranohydrolase. Synergistic action with xylanases from different glycosyl hydrolase families. Appl Microbiol Biotechnol 100(4):1743–1751. https://doi.org/10.1007/s00253-015-7061-8
van den Broek LAM, Lloyd RM, Beldman G, Verdoes JC, McCleary BV, Voragen AG (2005) Cloning and characterization of arabinoxylan arabinofuranohydrolase-D3 (AXHd3) from Bifidobacterium adolescentis DSM20083. Appl Microbiol Biotechnol 67(5):641–647. https://doi.org/10.1007/s00253-004-1850-9
Vandermarliere E, Bourgois TM, Winn MD, Van Campenhout S, Volckaert G, Delcour JA, Strelkov SV, Rabijns A, Courtin CM (2009) Structural analysis of a glycoside hydrolase family 43 arabinoxylan arabinofuranohydrolase in complex with xylotetraose reveals a different binding mechanism compared to other members of the same family. Biocheml J 418(1):39–47. https://doi.org/10.1042/BJ20081256
Vangsøe CT, Nørskov NP, Devaux MF, Bonnin E, Bach Knudsen KE (2020) Carbohydrase complexes rich in xylanases and arabinofuranosidases affect the autofluorescence signal and liberate phenolic acids from the cell wall matrix in wheat, maize, and rice bran: an in vitro digestion study. J Agric Food Chem 68(37):9878–9887. https://doi.org/10.1021/acs.jafc.0c00703
Wang W, Mai-Gisondi G, Stogios PJ, Kaur A, Xu X, Cui H, Turunen O, Savchenko A, Master ER (2014) Elucidation of the molecular basis for arabinoxylan-debranching activity of a thermostable family GH62 α-L-arabinofuranosidase from Streptomyces thermoviolaceus. Appl Environ Microbiol 80(17):5317–5329. https://doi.org/10.1128/AEM.00685-14
Wang W, Andric N, Sarch C, Silva BT, Tenkanen M, Master ER (2018) Constructing arabinofuranosidases for dual arabinoxylan debranching activity. Biotechnol Bioeng 115(1):41–49. https://doi.org/10.1002/bit.26445
Wilkens C, Andersen S, Petersen BO, Li A, Busse-Wicher M, Birch J, Cockburn D, Nakai H, Christensen HEM, Kragelund BB, Dupree P, McCleary B, Hindsgaul O, Hachem MA, Svensson B (2016) An efficient arabinoxylan-debranching α-L-arabinofuranosidase of family GH62 from Aspergillus nidulans contains a secondary carbohydrate binding site. Appl Microbiol Biotechnol 100(14):6265–6277. https://doi.org/10.1007/s00253-016-7417-8
Wilkens C, Andersen S, Dumon C, Berrin JG, Svensson B (2017) GH62 arabinofuranosidases: structure, function and applications. Biotechnol Adv 35(6):792–804. https://doi.org/10.1016/j.biotechadv.2017.06.005
Wu X, Zhang S, Zhao S, Dai L, Huang S, Liu X, Yu J, Wang L (2022) Functional specificity of three α-arabinofuranosidases from different glycoside hydrolase families in Aspergillus niger An76. J Agric Food Chem 70:5039–5048. https://doi.org/10.1021/acs.jafc.1c08388
Xie J, Zhao D, Zhao L, Pei J, Xiao W, Ding G, Wang Z, Xu J (2016) Characterization of a novel arabinose-tolerant α-L-arabinofuranosidase with high ginsenoside Rc to ginsenoside Rd bioconversion productivity. J Appl Microbiol 120(3):647–660. https://doi.org/10.1111/jam.13040
Xin D, Chen X, Wen P, Zhang J (2019) Insight into the role of α-arabinofuranosidase in biomass hydrolysis: cellulose digestibility and inhibition by xylooligomers. Biotechnol Biofuels 12:64. https://doi.org/10.1186/s13068-019-1412-0
Xiong JS, Balland-Vanney M, Xie ZP, Schultze M, Kondorosi A, Kondorosi E, Staehelin C (2007) Molecular cloning of a bifunctional β-xylosidase/α-L-arabinosidase from alfalfa roots: heterologous expression in Medicago truncatula and substrate specificity of the purified enzyme. J Exp Bot 58(11):2799–2810. https://doi.org/10.1093/jxb/erm133
Xu B, Dai L, Zhang W, Yang Y, Wu Q, Li J, Tang X, Zhou J, Ding J, Han N, Huang Z (2019) Characterization of a novel salt-, xylose- and alkali-tolerant GH43 bifunctional β-xylosidase/α-L-arabinofuranosidase from the gut bacterial genome. J Biosci Bioeng 128(4):429–437. https://doi.org/10.1016/j.jbiosc.2019.03.018
Xue Y, Cui X, Zhang Z, Zhou T, Gao R, Li Y, Ding X (2020) Effect of β-endoxylanase and α-arabinofuranosidase enzymatic hydrolysis on nutritional and technological properties of wheat brans. Food Chem 302:125332. https://doi.org/10.1016/j.foodchem.2019.125332
Yang X, Shi P, Huang H, Luo H, Wang Y, Zhang W, Yao B (2014) Two xylose-tolerant GH43 bifunctional β-xylosidase/α-arabinosidases and one GH11 xylanase from Humicola insolens and their synergy in the degradation of xylan. Food Chem 148:381–387. https://doi.org/10.1016/j.foodchem.2013.10.062
Yang J, Summanen PH, Henning SM, Hsu M, Lam H, Huang J, Tseng CH, Dowd SE, Finegold SM, Heber D (2015a) Xylooligosaccharide supplementation alters gut bacteria in both healthy and prediabetic adults: a pilot study. Front Physiol 6:216. https://doi.org/10.3389/fphys.2015.00216
Yang W, Bai Y, Yang P, Luo H, Huang H, Meng K, Shi P, Wang Y, Yao B (2015b) A novel bifunctional GH51 exo-α-L-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity. Biotechnol Biofuels 8:197. https://doi.org/10.1186/s13068-015-0366-0
Yang Y, Zhu N, Yang J, Lin Y, Liu J, Wang R, Wang F, Yuan H (2017) A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose. Microb Cell Factories 16(1):166. https://doi.org/10.1186/s12934-017-0777-7
Yegin S, Altinel B, Tuluk K (2018) A novel extremophilic xylanase produced on wheat bran from Aureobasidium pullulans NRRL Y-2311-1: effects on dough rheology and bread quality. Food Hydrocolloid 81:389–397. https://doi.org/10.1016/j.foodhyd.2018.03.012
Zhang R, Tan SQ, Zhang BL, Guo ZY, Tian LY, Weng P, Luo ZY (2021) Two key amino acids variant of α-L-arabinofuranosidase from Bacillus subtilis Str. 168 with altered activity for selective conversion ginsenoside Rc to Rd. Molecules 26:1733. https://doi.org/10.3390/molecules26061733
Zhao J, Esque J, AndréI OMJ, Fauré R (2021a) Synthesis of α-L-Araf and β-D-Galf series furanobiosides using mutants of a GH51 α-L-arabinofuranosidase. Bioorg Chem 116:105245. https://doi.org/10.1016/j.bioorg.2021.105245
Zhao J, Tandrup T, Bissaro B, Barbe S, Poulsen J-CN, André I, Dumon C, Lo Leggio L, O’Donohue MJ, Fauré R (2021b) Probing the determinants of the transglycosylation/hydrolysis partition in a retaining α-L-arabinofuranosidase. New Biotechnol 62:68–78. https://doi.org/10.1016/j.nbt.2021.01.008
Zhou X, Li W, Mabon R, Broadbelt LJ (2017) A critical review on hemicellulose pyrolysis. Energy Technol-Ger 5(1):52–79. https://doi.org/10.1002/ente.201600667
Zhou T, Xue Y, Zhang Z, Dong Y, Gao R, Li Y (2019) Improvement of the characteristics of steamed bread by supplementation of recombinant α-L-arabinofuranosidase containing xylan-binding domain. Food Biotechnol 33(1):34–53. https://doi.org/10.1080/08905436.2018.1553048
Zoghlami A, Paës G (2019) Lignocellulosic biomass: understanding recalcitrance and predicting hydrolysis. Front Chem 7:874. https://doi.org/10.3389/fchem.2019.00874
Zuo SS, Wang YC, Zhu L, Zhao JY, Li MG, Han XL, Wen ML (2020) Cloning and characterization of a ginsenoside-hydrolyzing α-L-arabinofuranosidase, CaAraf51, from Cellulosimicrobium aquatile Lyp51. Curr Microbiol 77(10):2783–2791. https://doi.org/10.1007/s00284-020-02078-0
Acknowledgements
We are grateful to Franz J. St John from the Forest Products Laboratory, USDA Forest Service, for his help in preparing the manuscript.
Funding
The author(s) received no financial support for the research, authorship, and/or publication of this article.
Author information
Authors and Affiliations
Contributions
LL: Conceptualization, Literature research, Data analysis, Writing-original draft, Writing-review & editing. QL: Data analysis, Visualization. JW: Literature research. SD: Supervision, Writing-review & editing. All authors read and approved the final manuscript.
Corresponding author
Ethics declarations
Conflict of interest
The authors declare that they have no conflict of interest.
Additional information
Publisher's Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Supplementary Information
Below is the link to the electronic supplementary material.
Rights and permissions
Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.
About this article
Cite this article
Long, L., Lin, Q., Wang, J. et al. Microbial α-L-arabinofuranosidases: diversity, properties, and biotechnological applications. World J Microbiol Biotechnol 40, 84 (2024). https://doi.org/10.1007/s11274-023-03882-z
Received:
Accepted:
Published:
DOI: https://doi.org/10.1007/s11274-023-03882-z