Abstract
Heteropolymers of mannan are polysaccharide components of the plant cell wall of gymnosperms and some angiosperms, including palm trees (Arecales and Monocot). Degradation of the complex structure of these polysaccharides requires the synergistic action of enzymes that disrupt the internal carbon skeleton of mannan and accessory enzymes that remove side chain substituents. However, complete degradation of these polysaccharides is carried out by an exo-hydrolase termed β-mannosidase. Microbial β-mannosidases belong to families 1, 2, and 5 of glycosyl hydrolases, and catalyze the hydrolysis of non-reducing ends of mannose oligomers. Besides, these enzymes are also involved in transglycosylation reactions. Because of their activity at different temperatures and pH values, these enzymes are used in a variety of industrial applications and the pharmaceutical, food, and biofuel industries.
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References
Ademark P, Lundqvist J, Hägglund P, Tenkanen M, Torto N, Tjerneld F, Stålbrand H (1999) Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J Biotechnol 75:281–289. https://doi.org/10.1016/S0168-1656(99)00172-8
Ademark P, De Vries RP, Hägglund P, Stålbrand H, Visser J (2001) Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation. Eur J Biochem 268:2982–2990. https://doi.org/10.1046/j.1432-1327.2001.02188.x
Aditiya HB, Mahlia TMI, Chong WT, Nur H, Sebayang AH (2016) Second generation bioethanol production: a critical review. Renew Sust Energ Rev 66:631–653. https://doi.org/10.1016/j.rser.2016.07.015
Aehle W (2004) Enzymes in industry. Wiley-VCH, Weinheim
Akino T, Nakamura N, Horikoshi K (1988) Characterization of β-mannosidase of an alkalophilic Bacillus sp. Agric Biol Chem 52:1459–1464. https://doi.org/10.1080/00021369.1988.10868864
Amore A, Giacobbe S, Faraco V (2013) Regulation of cellulase and hemicellulase gene expression in fungi. Curr Genomics 14:230–249. https://doi.org/10.2174/1389202911314040002
Amore A, Giacobbe S, Liguori R, Faraco V (2014) The second generation ethanol production. Rend Accad Naz Sci XL Mem Sci Fis Naur 37:113–136. https://doi.org/10.4399/97888548717176
Arai M, Fujimoto H, Ooi T, Ogura S, Murao S (1995) Purification and properties of a β-mannosidases from Aspergillus aculeatus. J Appl Glycosci 42:49–51. https://doi.org/10.11541/jag1994.42.49
Araraki M, Kitamikado T (1988) Exo-1,4-beta-mannanase from Aeromonas hydrophila. Methods Enzymol 160:583–589. https://doi.org/10.1016/0076-6879(88)60172-8
Asano I, Hamaguchi K, Fujii S, Iino K (2003) In vitro digestibility and fermentation of mannooligosaccharides from coffee mannan. Food Sci Technol Res 9:62–66. https://doi.org/10.3136/fstr.9.62
Aspinall GO (1959) Structural chemistry of the hemicelluloses. In: Wolfrom ML (ed) Advances in carbohydrate chemistry, 1st edn. Academic Press, New York, pp 429–526
Aspinall GO, Hirst EL, Percival EGV, Williamson IR (1953) The mannans of ivory nut ( Phytelephas macrocarpa). Part I. The methylation of mannan A and mannan B. J Chem Soc 0:3184–3188. https://doi.org/10.1039/JR9530003184
Aspinall GO, Rashbrook RB, Kessler G (1958) The Mannans of ivory nut (Phytelephas macrocarpa). Part II. The partial acid hydrolysis of mannas A and B. J Chem Soc. https://doi.org/10.1039/JR9580000215
Bai X, Hu H, Chen H, Wei Q, Yang Z, Huang Q (2014) Expression of a β-mannosidase from Paenibacillus polymyxa A-8 in Escherichia coli and characterization of the recombinant enzyme. PLoS One 9:e111622. https://doi.org/10.1371/journal.pone.0111622
Bajpai P (2004) Biological bleaching of chemical pulps. Crit Rev Biotechnol 24:1–58. https://doi.org/10.1080/07388550490465817
Bauer MW, Bylina EJ, Swanson RV, Kelly RM (1996) Comparison of a β-glucosidase and a β-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. J Biol Chem 271:23749–23755. https://doi.org/10.1074/jbc.271.39.23749
Béki E, Nagy I, Vanderleyden J, Jäger S, Kiss L, Fülöp L, Hornok L, Kukolya J (2003) Cloning and heterologous expression of a β-d-mannosidase (EC 3.2.1.25)-encoding gene from Thermobifida fusca TM51. Appl Environ Microbiol 69:1944–1952. https://doi.org/10.1128/AEM.69.4.1944-1952.2003
Bettiol JLP, Cooremans SPG, Johnstone KR, Sreekrishna K, Saunders CW, Herbots IVAJ, Baeck AC (2002) Laundry detergent compositions comprising a saccharide gum degrading enzyme. Procter & Gamble. N° US 6.486.112 B1. Cincinnate
Bissaro B, Monsan P, Fauré R, O’Donohue MJ (2015) Glycosynthesis in a waterworld: new insight into the molecular basis of transglycosylation in retaining glycoside hydrolases. Biochem J 467:17–35. https://doi.org/10.1042/BJ20141412
Bouquelet S, Spik G, Montreuil J (1978) Properties of a β-D-mannosidase from Aspergillus niger. Biochim Biophys Acta 522:521–530. https://doi.org/10.1016/0005-2744(78)90084-0
Brás NF, Fernandes PA, Ramos MJ (2009) Docking and molecular dynamics studies on the stereoselectivity in the enzymatic synthesis of carbohydrates. Theor Chem Accounts 122:283–296. https://doi.org/10.1007/s00214-009-0507-2
Bremner I, Wilkie KCB (1971) The hemicelluloses of bracken: Part II. A galactoglucomannan. Carbohydr Res 20:193–203. https://doi.org/10.1016/S0008-6215(00)81372-5
Buckeridge MS (2010) Seed cell wall storage polysaccharides: models to understand cell wall biosynthesis and degradation. Plant Physiol 154:1017–1023. https://doi.org/10.1104/pp.110.158642
Buckeridge MS, Pessoa dos Santos H, Tiné MAS (2000a) Mobilisation of storage cell wall polysaccharides in seeds. Plant Physiol Biochem 38:141–156. https://doi.org/10.1016/S0981-9428(00)00162-5
Buckeridge MS, Tiné MAS, dos Santos HP, Lima DU (2000b) Cell wall storage polysaccharides in seeds. Structure, metabolism, function and ecological aspects. Rev Bras Fisiol Veg 12:137–162
Chang PK, Ehrlich KC (2013) Genome-wide analysis of the Zn(II)2Cys6 zinc cluster-encoding gene family in Aspergillus flavus. Appl Microbiol Biotechnol 97:4289–4300. https://doi.org/10.1007/s00253-013-4865-2
Chudzikowski RJ (1971) Guar gum and its applications. J Soc Cosmet Chem 22:43–60
Davies G, Henrissat B (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3:853–859. https://doi.org/10.1016/S0969-2126(01)00220-9
De Pourcq K, De Schutter K, Callewaert N (2010) Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl Microbiol Biotechnol 87:1617–1631. https://doi.org/10.1007/s00253-010-2721-1
Demain AL, Vaishnav P (2009) Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 27:297–306. https://doi.org/10.1016/j.biotechadv.2009.01.008
Dengler EC, Alberti LA, Bowman BN, Kerwin AA, Wilkerson JL, Moezzi DR, Limanovich E, Wallace JA, Milligan ED (2014) Improvement of spinal non-viral IL-10 gene delivery by d-mannose as a transgene adjuvant to control chronic neuropathic pain. J Neuro-Oncol 11:92. https://doi.org/10.1186/1742-2094-11-92
Dey PM (1978) Biochemistry of plant galactomannans. Adv Carbohydr Chem Biochem 35:341–376. https://doi.org/10.1016/S0065-2318(08)60221-8
Dhugga KS, Barreiro R, Whitten B, Stecca K, Hazebroek J, Randhawa GS, Dolan M, Kinney AJ, Tomes D, Nichols S, Anderson P (2004) Guar seed beta-mannan synthase is a member of the cellulose synthase super gene family. Science 303:363–366. https://doi.org/10.1126/science.1090908
Dias FM, Vincent F, Pell G, Prates JA, Centeno MS, Tailford LE, Ferreira LM, Fontes CM, Davies GJ, Gilbert HJ (2004) Insights into the molecular determinants of substrate specificity in glycoside hydrolase family 5 revealed by the crystal structure and kinetics of Cellvibrio mixtus mannosidase 5A. J Biol Chem 279:25517–25526. https://doi.org/10.1074/jbc.M401647200
Do BC, Dang TT, Berrin JG, Haltrich D, To KA, Sigoillot JC, Yamabhai M (2009) Cloning, expression in Pichia pastoris, and characterization of a thermostable GH5 mannan endo-1,4-beta-mannosidase from Aspergillus niger BK01. Microb Cell Factories 8:59. https://doi.org/10.1186/1475-2859-8-59
Dotsenko GS, Semenova MV, Sinitsyna OA, Hinz SW, Wery J, Zorov IN, Kondratieva EG, Sinitsyn AP (2012) Cloning, purification, and characterization of galactomannan-degrading enzymes from Myceliophthora thermophila. Biochemistry (Mosc) 77:1303–1311. https://doi.org/10.1134/S0006297912110090
Duan X, Zou C, Wu J (2015) Triton X-100 enhances the solubility and secretion ratio of aggregation-prone pullulanase produced in Escherichia coli. Bioresour Technol 194:137–143. https://doi.org/10.1016/j.biortech.2015.07.024
Duffaud GU, McCutchen CM, Leduc P, Parker KN, Kelly RM (1997) Purification and characterization of extremely thermostable beta-mannanase, beta-mannosidase, and alpha-galactosidase from the hyperthermophilic eubacterium Thermotoga neapolitana 5068. Appl Environ Microbiol 63:169–177
Elbein AD, Adya S, Lee YC (1977) Purification and properties of a beta-mannosidase from Aspergillus niger. J Biol Chem 252:2026–2031
Flemming JS, Freitas JRS, Fontoura P, Montanhini Neto R, Arruda JS (2004) Use of mannanoligosaccharides in broiler feeding. Rev Bras Cienc Avic 6:159–161. https://doi.org/10.1590/S1516-635X2004000300005
Fliedrová B, Gerstorferová D, Křen K, Weignerová L (2012) Production of Aspergillus niger β-mannosidase in Pichia pastoris. Protein Expr Purif 85:159–164. https://doi.org/10.1016/j.pep.2012.07.012
Fogh J, Irani M, Andersson C, Weigelt C (2003) Production of recombinant human lysosomal alpha-mannosidase. HemeBiotech. N° US2003/0199073. Hillerod
Franková L, Fry SC (2013) Biochemistry and physiological roles of enzymes that “cut and paste” plant cell-wall polysaccharides. J Exp Bot 64:3519–3550. https://doi.org/10.1093/jxb/ert201
Gille S, Cheng K, Skinner ME, Liepman AH, Wilkerson CG, Pauly M (2011) Deep sequencing of voodoo lily (Amorphophallus konjac): an approach to identify relevant genes involved in the synthesis of the hemicellulose glucomannan. Planta 234:515–526. https://doi.org/10.1007/s00425-011-1422-z
Goettig P (2016) Effects of glycosylation on the enzymatic activity and mechanisms of proteases. Int J Mol Sci 17:1969. https://doi.org/10.3390/ijms17121969
Gomes J, Terler K, Kratzer R, Kainz E, Steiner W (2007) Production of thermostable β-mannosidase by a strain of Thermoascus aurantiacus: isolation, partial purification and characterization of the enzyme. Enzym Microb Technol 40:969–975. https://doi.org/10.1016/j.enzmictec.2006.08.011
Gomes AR, Byregowda SM, Veeregowda BM, Balamurugan V (2016) An overview of heterologous expression host systems for the production of recombinant proteins. Adv Anim Vet Sci 4:346–356. https://doi.org/10.14737/journal.aavs/2016/4.7.346.356
Gübitz GM, Hayn M, Sommerauer M, Steiner W (1996) Mannan-degrading enzymes from Sclerotium rolfsii: characterisation and synergism of two endo β-mannanases and a β-mannosidase. Bioresour Technol 58:127–135. https://doi.org/10.1016/S0960-8524(96)00093-4
Gustafsson C, Govindarajan S, Minshull J (2004) Codon bias and heterologous protein expression. Trends Biotechnol 22:346–353. https://doi.org/10.1016/j.tibtech.2004.04.006
Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316:695–696. https://doi.org/10.1042/bj3160695
Henrissat B, Davies G (1997) Structural and sequence-based classification of glycoside hydrolases. Curr Opin Struct Biol 7:637–644. https://doi.org/10.1016/S0959-440X(97)80072-3
Herve C, Rogowski A, Blake AW, Marcus SE, Gilbert HJ, Knox JP (2010) Carbohydrate-binding modules promote the enzymatic deconstruction of intact plant cell walls by targeting and proximity effects. Proc Natl Acad Sci U S A 107:15293–15298. https://doi.org/10.1073/pnas.1005732107
Hu X, Shi Y, Zhang P, Miao M, Zhang T, Jiang B (2016) d-mannose: properties, production, and applications: an overview. Compr Rev Food Sci Food Saf 15:773–785. https://doi.org/10.1111/1541-4337.12211
Johnson WG (2014) Disorders of glycoprotein degradation: sialidosis, fucosidosis, α-mannosidosis, β-mannosidosis, and aspartylglycosaminuria. In: Rosenberg RN, Pascual JM (eds) Rosenberg’s molecular and genetic basis of neurological and psychiatric disease, 5th edn. Academic Press, Amsterdam, pp 369–383
Jones MZ, Rathke EJS, Cavanagh K, Hancock LW (1984) Beta-mannosidosis: prenatal biochemical and morphological characteristics. J Inherit Metab Dis 7:80–85. https://doi.org/10.1007/BF01805811
Kamm B, Kamm M (2004) Principles of biorefineries. Appl Microbiol Biotechnol 64:137–145. https://doi.org/10.1007/s00253-003-1537-7
Kanamasa S, Takada G, Kawaguchi T, Sumitani J, Arai M (2001) Overexpression and purification of Aspergillus aculeatus beta-mannosidase and analysis of the integrated gene in Aspergillus oryzae. J Biosci Bioeng 92:131–137. https://doi.org/10.1016/S1389-1723(01)80213-9
Kanamasa S, Kawaguchi T, Takada G, Kajiwara S, Sumitani J, Arai M (2007) Development of an efficient production method for β-mannosidase by the creation of an overexpression system in Aspergillus aculeatus. Lett Appl Microbiol 45:142–147. https://doi.org/10.1111/j.1472-765X.2007.02160.x
Kaper T, van Heusden HH, van Loo B, Vasella A, van der Oost J, de Vos WM (2002) Substrate specificity engineering of beta-mannosidase and beta-glucosidase from Pyrococcus by exchange of unique active site residues. Biochemistry 41:4147–4155. https://doi.org/10.1021/bi011935a
Kulminskaya AA, Eneiskaya EV, Isaeva-Ivanova LS, Savel’ev AN, Sidorenko IA, Shabalin KA, Golubev AM, Neustroev KN (1999) Enzymatic activity and β-galactomannan binding property of β-mannosidase from Trichoderm reesei. Enzym Microb Technol 25:372–377
Kurakake M, Komaki T (2001) Production of beta-mannanase and beta-mannosidase from Aspergillus awamori K4 and their properties. Curr Microbiol 42:377–380. https://doi.org/10.1007/s002840010233
Li YX, Liu Y, Yan QJ, Yang SQ, Jiang ZQ (2015) Characterization of a novel glycoside hydrolase family 5 β-mannosidase from Absidia corymbifera with high transglycosylation activity. J Mol Catal B Enzym 122:265–274. https://doi.org/10.1016/j.molcatb.2015.09.018
Liu L, Yang H, Shin HD, Chen RR, Li J, Du G, Chen J (2013) How to achieve high-level expression of microbial enzymes: strategies and perspectives. Bioengineered 4:212–223. https://doi.org/10.4161/bioe.24761
Mackie W, Sellen DB (1969) The degree of polymerization and polydispersity of mannan from the cell wall of the green seaweed codium fragile. Polymer 10:621–632. https://doi.org/10.1016/0032-3861(69)90082-2
Madurwar MV, Ralegaonkar RV, Mandavgane SA (2013) Application of agro-waste for sustainable construction materials: a review. Constr Build Mater 38:872–878. https://doi.org/10.1016/j.conbuildmat.2012.09.011
McCleary BV (1983) Enzymic interactions in the hydrolysis of galactomannan in germinating guar: the role of exo-β-mannanase. Phytochemistry 22:649–658. https://doi.org/10.1016/S0031-9422(00)86956-3
Meier H, Reid JSG (2015) Reserve polyssacharides other than starch in higher plants. In: Pirson A, Zimmermann MH (eds) Encyclopedia of plant physiology, 1st edn. Springer, Berlin, pp 418–461
Menzella HG (2011) Comparison of two codon optimization strategies to enhance recombinant protein production in Escherichia coli. Microb Cell Factories 10:15. https://doi.org/10.1186/1475-2859-10-15
Moreira LRS, Filho EXF (2008) An overview of mannan structure and mannan-degrading enzyme systems. Appl Microbiol Biotechnol 79:165–178. https://doi.org/10.1007/s00253-008-1423-4
Mudgil D, Barak S, Khatkar BS (2014) Guar gum: processing, properties, and food applications - a review. J Food Sci Technol 51:409–418. https://doi.org/10.1007/s13197-011-0522-x
Mussatto SI, Ballesteros LF, Martins S, Teixeira JA (2012) Use of agro-industrial wastes in solid-state fermentation processes. In: Show KY (ed) Industrial Waste, 1st edn. InTech, Rijeka, pp 121–140
Nascimento AS, Muniz JRC, Aparício R, Golubev AM, Polikarpov I (2014) Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme. FEBS J 281:4165–4178
Nishinari K, Takemasa M, Zhang H, Takahashi R (2007) Storage plant polysaccharides: xyloglucans, galactomannans, glucomannans. In: Kamerling JP (ed) Comprehensive glycoscience, 1st edn. Elsevier, New York, pp 613–646
Oda Y, Tonomura K (1996) Characterization of β-mannanase and β-mannosidase secreted from the yeast Trichosporon cutaneum JCM 2947. Lett Appl Microbiol 22:173–178. https://doi.org/10.1111/j.1472-765X.1996.tb01136.x
Odetallah NH, Ferket PR, Grimes JL, McNaughton JL (2002) Effect of mannan-endo-1,4-beta-mannosidase on the growth performance of turkeys fed diets containing 44 and 48% crude protein soybean meal. Poult Sci 81:1322–1331. https://doi.org/10.1093/ps/81.9.1322
Ogawa M, Kobayashi T, Koyama Y (2012) ManR, a novel Zn(II)2Cys6 transcriptional activator, controls the β-mannan utilization system in Aspergillus oryzae. Fungal Genet Biol 49:987–995. https://doi.org/10.1016/j.fgb.2012.09.006
Pan T, Coleman JE (1990) GAL4 transcription factor is not a “zinc finger” but forms a Zn(II)2Cys6 binuclear cluster. Proc Natl Acad Sci 87:2077–2081
Park SH, Park KH, Oh BC, Alli I, Lee BH (2011) Expression and characterization of an extremely thermostable β-glycosidase (mannosidase) from the hyperthermophilic archaeon Pyrococcus furiosus DSM3638. New Biotechnol 28:639–648. https://doi.org/10.1016/j.nbt.2011.05.002
Pauly M, Keegstra K (2008) Cell-wall carbohydrates and their modification as a resource for biofuels. Plant J 54:559–568. https://doi.org/10.1111/j.1365-313X.2008.03463.x
Pauly M, Gille S, Liu L, Mansoori N, de Souza A, Schultink A, Xiong G (2013) Hemicellulose biosynthesis. Planta 238:627–642. https://doi.org/10.1007/s00425-013-1921-1
Peberdy JF (1994) Protein secretion in filamentous fungi - trying to understand a highly productive black box. Trends Biotechnol 12:50–57. https://doi.org/10.1016/0167-7799(94)90100-7
Prendecka M, Buczyńska A, Rogalski J (2007) Purification and characterization of β-mannosidases from white rot fungus Phlebia radiata. Pol J Microbiol 56:139–147
Puupponen-Pimia R, Aura A-M, Oksman-Caldentey K-M, Mylläriner P, Saarela M, Mattila-Sandholm T, Poutanen K (2002) Development of functional ingredients for gut health. Trends Food Sci Technol 13:3–11. https://doi.org/10.1016/S0924-2244(02)00020-1
Qing Z (2012) The application of enzyme and yeast. Thesis, Saimaa University of Applied Sciences
Rahmani N, Kashiwagi N, Lee J, Niimi-Nakamura S, Matsumoto H, Kahar P, Lisdiyanti P, Yopi PB, Ogino C, Kondo A (2017) Mannan endo-1,4-β-mannosidase from Kitasatospora sp. isolated in Indonesia and its potential for production of mannooligosaccharides from mannan polymers. AMB Express 7:100. https://doi.org/10.1186/s13568-017-0401-6
Reddy SK, Rosengren A, Klaubauf S, Kulkarni T, Karlsson EN, de Vries RP, Stålbrand H (2013) Phylogenetic analysis and substrate specificity of GH2 β-mannosidases from Aspergillus species. FEBS Lett 587:3444–3449. https://doi.org/10.1016/j.febslet.2013.08.029
Rinaldi R, Schüth F (2009) Design of solid catalysts for the conversion of biomass. Energy Environ Sci 2:610–626. https://doi.org/10.1039/B902668A
Rosano GL, Ceccarelli EA (2014) Recombinant protein expression in Escherichia coli: advances and challenges. Front Microbiol 5:172. https://doi.org/10.3389/fmicb.2014.00172
Rye CS, Withers SG (2000) Glycosidase mechanisms. Curr Opin Chem Biol 4:573–580. https://doi.org/10.1016/S1367-5931(00)00135-6
Sadh PK, Duhan S, Duhan JS (2018) Agro-industrial wastes and their utilization using solid state fermentation: a review. Bioresour Bioprocess 5:1. https://doi.org/10.1186/s40643-017-0187-z
Saini JK, Saini R, Tewari L (2015) Lignocellulosic agriculture wastes as biomass feedstocks for second-generation bioethanol production: concepts and recent developments. 3 Biotech 5:337–353. https://doi.org/10.1007/s13205-014-0246-5
Shallom D, Shoham Y (2003) Microbial hemicellulases. Curr Opin Microbiol 6:219–228. https://doi.org/10.1016/S1369-5274(03)00056-0
Shi P, Yao G, Cao Y, Yang P, Yuan T, Huang H, Bai Y, Yao B (2011) Cloning and characterization of a new β-mannosidase from Streptomyces sp. S27. Enzym Microb Technol 49:277–283. https://doi.org/10.1016/j.enzmictec.2011.06.003
Shi H, Huang Y, Zhang Y, Li W, Li X, Wang F (2013) High-level expression of a novel thermostable and mannose-tolerant β-mannosidase from Thermotoga thermarum DSM 5069 in Escherichia coli. BMC Biotechnol 13:83. https://doi.org/10.1186/1472-6750-13-83
Silva COG, Vaz RP, Filho EXF (2017) Bringing plant cell wall-degrading enzymes into the lignocellulosic biorefinery concept. Biofuels Bioprod Biorefin 12:277–289. https://doi.org/10.1002/bbb.1832
Sjöström E (1993) Wood polysaccharides. In: Sjöström E (ed) Wood chemistry, fundamentals, and applications, 2nd edn. Academic Press, San Diego, pp 51–70
Sone Y, Misaki A (1978) Purification and characterization of beta-d-mannosidase and beta-N-acetyl-d-hexosaminidase of Tremella fuciformis. J Biochem 83:1135–1144. https://doi.org/10.1093/oxfordjournals.jbchem.a132003
Srivastava PK, Kapoor M (2017) Production, properties, and applications of endo-β-mannanases. Biotechnol Adv 35:1–19. https://doi.org/10.1016/j.biotechadv.2016.11.001
Stephen AM (1983) Other plant polysaccharides. In: Aspinall GO (ed) The polysaccharides, 1st edn. Academic Press, New York, pp 97–180
Su X, Schmitz G, Zhang M, Mackie RI, Cann IKO (2012) Heterologous gene expression in filamentous fungi. In: Sariaslani S, Gadd GM (eds) Advances in applied microbiology, 1st edn. Elsevier, Amsterdam, pp 2–44
Sun Y, Cheng J (2002) Hydrolysis of lignpcellulosic materials for ethanol production: a review. Bioresour Technol 83:11. https://doi.org/10.1016/S0960-8524(01)00212-7
Sutton RL, Wilcox J (1998) Recrystallization in ice cream as affected by stabilizers. J Food Sci 63:104–107. https://doi.org/10.1111/j.1365-2621.1998.tb15686.x
Suurnäkki A, Tenkanen M, Buchert J, Viikari L (1997) Hemicellulases in the bleaching of chemical pulps. In: Scheper T (ed) Biotechnology in the pulp and paper industry, 1st edn. Springer, Berlin, pp 261–287
Tailford LE, Money VA, Smith NL, Dumon C, Davies GJ, Gilbert HJ (2007) Mannose foraging by Bacteroides thetaiotaomicron: structure and specificity of the β-mannosidase, BtMan2A. J Biol Chem 282:11291–11299. https://doi.org/10.1074/jbc.M610964200
Tailford LE, Offen WA, Smith NL, Dumon C, Morland C, Gratien J, Heck MP, Stick RV, Blériot Y, Vasella A, Gilbert HJ, Davies GJ (2008) Structural and biochemical evidence for a boat-like transition state in β-mannosidases. Nat Chem Biol 4:306–312. https://doi.org/10.1038/nchembio.81
Takada G, Kawaguchi T, Kaga T, Sumitani J, Arai M (1999) Cloning and sequencing of β-mannosidase gene from Aspergillus aculeatus no. F-50. Biosci Biotechnol Biochem 63:206–209. https://doi.org/10.1271/bbb.63.206
Taylor JL, Jaquess PA, Lund H, Pedersen H, Xu H, Clemmoons J (2005) Use of hemicellulase composition in mechanical pulp production. Novozymes N° US 2005/0000666 A1. Buckman Laboratories International, New York
Timell TE (1965) Wood hemicelluloses: part II. Adv Carbohydr Chem Biochem 20:409–483. https://doi.org/10.1016/S0096-5332(08)60304-5
Timell TE (1967) Recent progress in the chemistry of wood hemicelluloses. Wood Sci Technol 1:45–70. https://doi.org/10.1007/BF00592255
Todd RB, Andrianopoulos A (1997) Evolution of a fungal regulatory gene family: the Zn(II)2Cys6 binuclear cluster DNA binding motif. Fungal Genet Biol 21:388–405. https://doi.org/10.1006/fgbi.1997.0993
Tramice A, Andreotti G, Giordano A, Trincone A (2009) Enzymatic transglycosylation. In: Flickinger MC (ed) Encyclopedia of industrial biotechnololgy, 1st edn. Wiley, Hoboken, pp 1–15
Van Immerseel F, Cauwerts K, Devriese LA, Haesebrouck F, Ducatelle R (2002) Feed additives to control Salmonella in poultry. Worlds Poult Sci J 58:501–513. https://doi.org/10.1079/WPS20020036
Visser H, Joosten V, Punt PJ, Gusakov AV, Olson PT, Joosten R, Bartels J, Visser J, Sinitsyn AP, Emalfarb MA, Verdoes JC, Wery J (2011) Development of a mature fungal technology and production platform for industrial enzymes based on a Myceliophthora thermophila isolate, previously known as Chrysosporium lucknowense C1. Ind Biotechnol 7:214–224. https://doi.org/10.1089/ind.2011.7.214
Wan CC, Muldrey JE, Li SC, Li TH (1976) β-Mannosidase from the mushroom Polyporus sulfureus. J Biol Chem 251:4384–4388
Wang L, Ridgway D, Gu T, Moo-Young M (2005) Bioprocessing strategies to improve heterologous protein production in filamentous fungal fermentations. Biotechnol Adv 23:115–129. https://doi.org/10.1016/j.biotechadv.2004.11.001
Wang Y, Alonso AP, Wilkerson CG, Keegstra K (2012) Deep EST profiling of developing fenugreek endosperm to investigate galactomannan biosyaspinallnthesis and its regulation. Plant Mol Biol 79:243–258. https://doi.org/10.1007/s11103-012-9909-y
Whistler RL (1993) Hemicelluloses. In: Whistler RL, BeMiller JN (eds) Industrial gums: polysaccharides and their derivatives, 3rd edn. Academic Press, San Diego, pp 295–308
Wolfrom M, Laver ML, Patin DL (1961) Carbohydrates of the coffee bean. II. Isolation and characterization of a mannan. J Org Chem 26:4533–4535. https://doi.org/10.1021/jo01069a080
Yamabhai M, Sak-Ubol S, Srila W, Haltrich D (2016) Mannan biotechnology: from biofuels to health. Crit Rev Biotechnol 36:32–42. https://doi.org/10.3109/07388551.2014.923372
Yin L, Verhertbruggen Y, Oikawa A, Manisseri C, Knierim B, Prak L, Jensen JK, Knox JP, Auer M, Willats WG, Scheller HV (2011) The cooperative activities of CSLD2, CSLD3, and CSLD5 are required for normal arabidopsis development. Mol Plant 4:1024–1037. https://doi.org/10.1093/mp/ssr026
York WS, Darvill AG, McNeil M, Stevenson TT, Albersheim P (1986) Isolation and characterization of plant cell walls and cell wall components. Methods Enzymol 118:3–40. https://doi.org/10.1016/0076-6879(86)18062-1
Zhang M, Jiang Z, Li L, Katrolia P (2009) Biochemical characterization of a recombinant thermostable β-mannosidase from Thermotoga maritima with transglycosidase activity. J Mol Catal B Enzym 60:119–124. https://doi.org/10.1016/j.molcatb.2009.04.005
Zhao Q (2012) The application of enzyme and yeast. Thesis, Saimaa University of Applied Sciences
Zhao W, Zheng J, Zhou HB (2011) A thermotolerant and cold-active mannan endo-1,4-β-mannosidase from Aspergillus niger CBS 513.88: constitutive overexpression and high-density fermentation in Pichia pastoris. Bioresour Technol 102:7538–7547. https://doi.org/10.1016/j.biortech.2011.04.070
Zhou P, Liu Y, Yan Q, Chen Z, Qin Z, Jiang Z (2014) Structural insights into the substrate specificity and transglycosylation activity of a fungal glycoside hydrolase family 5 β-mannosidase. Acta Crystallogr D Biol Crystallogr 70:2970–2982. https://doi.org/10.1107/S1399004714019762
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The authors acknowledge the receipt of financial support from the Brazilian National Council for Scientific and Technological Development (CNPq), the Coordination for the Improvement of Higher Education Personnel (CAPES), and the Foundation for Research Support of the Federal District (FAPDF).
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Costa, D.A.L., Filho, E.X.F. Microbial β-mannosidases and their industrial applications. Appl Microbiol Biotechnol 103, 535–547 (2019). https://doi.org/10.1007/s00253-018-9500-9
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DOI: https://doi.org/10.1007/s00253-018-9500-9