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Volumn 78, Issue , 2015, Pages 63-73

Novel thermophilic hemicellulases for the conversion of lignocellulose for second generation biorefineries

Author keywords

Biocatalysis; Bioconversion; Biofuel; Biotransformation; Thermophilic enzymes; White chemistry

Indexed keywords

AGRICULTURE; BACILLI; BACTERIA; BIOCONVERSION; BIOFUELS; CATALYSIS; CELLULOSE; CROPS; ENZYMATIC HYDROLYSIS; GENES; GLUCOSE; HYDROLASES; HYDROLYSIS; LIGNIN; PLANTS (BOTANY); REFINING; SUGARS;

EID: 84935443496     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2015.06.014     Document Type: Article
Times cited : (26)

References (75)
  • 1
    • 0347294705 scopus 로고    scopus 로고
    • Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens
    • Poon D.K.Y., Webster P., Withers S.G., McIntosh L.P. Characterizing the pH-dependent stability and catalytic mechanism of the family 11 xylanase from the alkalophilic Bacillus agaradhaerens. Carbohyd. Res. 2003, 338:415-421.
    • (2003) Carbohyd. Res. , vol.338 , pp. 415-421
    • Poon, D.K.Y.1    Webster, P.2    Withers, S.G.3    McIntosh, L.P.4
  • 2
    • 9444240973 scopus 로고    scopus 로고
    • Two-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sultolobus soltataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events
    • Ausili A., Di Lauro B., Cobucci-Ponzano B., Bertoli E., Scire A., Rossi M., et al. Two-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sultolobus soltataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events. Biochem. J. 2004, 384:69-78.
    • (2004) Biochem. J. , vol.384 , pp. 69-78
    • Ausili, A.1    Di Lauro, B.2    Cobucci-Ponzano, B.3    Bertoli, E.4    Scire, A.5    Rossi, M.6
  • 3
    • 4944265460 scopus 로고    scopus 로고
    • Effect of dimer dissociation on activity and thermostability of the alpha-glucuronidase from Geobacillus stearothermophilus: dissecting the different oligomeric forms of family 67 glycoside hydrolases
    • Shallom D., Golan G., Shoham G., Shoham Y. Effect of dimer dissociation on activity and thermostability of the alpha-glucuronidase from Geobacillus stearothermophilus: dissecting the different oligomeric forms of family 67 glycoside hydrolases. J. Bacteriol. 2004, 186:6928-6937.
    • (2004) J. Bacteriol. , vol.186 , pp. 6928-6937
    • Shallom, D.1    Golan, G.2    Shoham, G.3    Shoham, Y.4
  • 4
    • 34248596489 scopus 로고    scopus 로고
    • A comparative infrared spectroscopic study of glycoside hydrolases from extremophilic archaea revealed different molecular mechanisms of adaptation to high temperatures
    • Ausili A., Cobucci-Ponzano B., Di Lauro B., D'Avino R., Perugino G., Bertoli E., et al. A comparative infrared spectroscopic study of glycoside hydrolases from extremophilic archaea revealed different molecular mechanisms of adaptation to high temperatures. Proteins 2007, 67:991-1001.
    • (2007) Proteins , vol.67 , pp. 991-1001
    • Ausili, A.1    Cobucci-Ponzano, B.2    Di Lauro, B.3    D'Avino, R.4    Perugino, G.5    Bertoli, E.6
  • 5
    • 34547747311 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes; stability, activity and implementation strategies for high temperature applications
    • Unsworth L.D., Oost J.V.D., Koutsopoulos S. Hyperthermophilic enzymes; stability, activity and implementation strategies for high temperature applications. FEBS J. 2007, 274:4044-4056.
    • (2007) FEBS J. , vol.274 , pp. 4044-4056
    • Unsworth, L.D.1    Oost, J.V.D.2    Koutsopoulos, S.3
  • 6
    • 38049001166 scopus 로고    scopus 로고
    • Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels
    • Atsumi S., Hanai T., Liao J.C. Non-fermentative pathways for synthesis of branched-chain higher alcohols as biofuels. Nature 2008, 451:86-89.
    • (2008) Nature , vol.451 , pp. 86-89
    • Atsumi, S.1    Hanai, T.2    Liao, J.C.3
  • 7
    • 67650215053 scopus 로고    scopus 로고
    • Lignocellulose conversion to biofuels: current challenges, global perspectives
    • Himmel M.E., Bayer E.A. Lignocellulose conversion to biofuels: current challenges, global perspectives. Curr. Opin. Biotechnol. 2009, 20:316-317.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 316-317
    • Himmel, M.E.1    Bayer, E.A.2
  • 8
    • 84866024722 scopus 로고    scopus 로고
    • Biocatalytic conversion of lignocellulose to platform chemicals
    • Jager G., Buchs J. Biocatalytic conversion of lignocellulose to platform chemicals. Biotechnol. J. 2012, 7:1122-1136.
    • (2012) Biotechnol. J. , vol.7 , pp. 1122-1136
    • Jager, G.1    Buchs, J.2
  • 9
    • 84873119880 scopus 로고    scopus 로고
    • Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes
    • Bhalla A., Bansal N., Kumar S., Bischoff K.M., Sani R.K. Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes. Bioresour. Technol. 2013, 128:751-759.
    • (2013) Bioresour. Technol. , vol.128 , pp. 751-759
    • Bhalla, A.1    Bansal, N.2    Kumar, S.3    Bischoff, K.M.4    Sani, R.K.5
  • 10
    • 84880638080 scopus 로고    scopus 로고
    • Hydrolysates of lignocellulosic materials for biohydrogen production
    • Chen R., Wang Y.Z., Liao Q., Zhu X., Xu T.F. Hydrolysates of lignocellulosic materials for biohydrogen production. BMB Rep. 2013, 46:244-251.
    • (2013) BMB Rep. , vol.46 , pp. 244-251
    • Chen, R.1    Wang, Y.Z.2    Liao, Q.3    Zhu, X.4    Xu, T.F.5
  • 13
    • 77954222256 scopus 로고    scopus 로고
    • A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2
    • Cobucci-Ponzano B., Aurilia V., Riccio G., Henrissat B., Coutinho P.M., Strazzulli A. A new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2. J. Biol. Chem. 2010, 285:20691-20703.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20691-20703
    • Cobucci-Ponzano, B.1    Aurilia, V.2    Riccio, G.3    Henrissat, B.4    Coutinho, P.M.5    Strazzulli, A.6
  • 14
    • 82455210960 scopus 로고    scopus 로고
    • Thermophilic, lignocellulolytic bacteria for ethanol production: current state and perspectives
    • Chang T., Yao S. Thermophilic, lignocellulolytic bacteria for ethanol production: current state and perspectives. Appl. Microbiol. Biotechnol. 2011, 92:13-27.
    • (2011) Appl. Microbiol. Biotechnol. , vol.92 , pp. 13-27
    • Chang, T.1    Yao, S.2
  • 16
    • 33846951759 scopus 로고    scopus 로고
    • Biomass recalcitrance: engineering plants and enzymes for biofuels production
    • Himmel M.E., Ding S.Y., Johnson D.K., Adney W.S., Nimlos M.R., Brady J.W., et al. Biomass recalcitrance: engineering plants and enzymes for biofuels production. Science 2007, 315:804-807.
    • (2007) Science , vol.315 , pp. 804-807
    • Himmel, M.E.1    Ding, S.Y.2    Johnson, D.K.3    Adney, W.S.4    Nimlos, M.R.5    Brady, J.W.6
  • 18
    • 0031079791 scopus 로고    scopus 로고
    • Variations in chemical composition and structure of macromolecular components in different morphological regions and maturity stages of Arundo donax
    • Neto C.P., Seca A., Nunes A.M., Coimbra M.A., Domingues F., Evtuguin D., et al. Variations in chemical composition and structure of macromolecular components in different morphological regions and maturity stages of Arundo donax. Ind. Crop Prod. 1997, 6:51-58.
    • (1997) Ind. Crop Prod. , vol.6 , pp. 51-58
    • Neto, C.P.1    Seca, A.2    Nunes, A.M.3    Coimbra, M.A.4    Domingues, F.5    Evtuguin, D.6
  • 19
    • 84933070353 scopus 로고    scopus 로고
    • Perennial grass (Arundo donax L.) as a feedstock for thermo-chemical conversion to energy and materials
    • Saikia R., Chutia R.S., Kataki R., Pant K.K. Perennial grass (Arundo donax L.) as a feedstock for thermo-chemical conversion to energy and materials. Bioresour. Technol. 2015, 188:265-272.
    • (2015) Bioresour. Technol. , vol.188 , pp. 265-272
    • Saikia, R.1    Chutia, R.S.2    Kataki, R.3    Pant, K.K.4
  • 20
    • 0030046744 scopus 로고    scopus 로고
    • Identification of the acidic degradation products of hexenuronic acid and characterisation of hexenuronic acid-substituted xylooligosaccharides by NMR spectroscopy
    • Teleman A., Hausalo T., Tenkanen M., Vuorinen T. Identification of the acidic degradation products of hexenuronic acid and characterisation of hexenuronic acid-substituted xylooligosaccharides by NMR spectroscopy. Carbohydr. Res. 1996, 280:197-208.
    • (1996) Carbohydr. Res. , vol.280 , pp. 197-208
    • Teleman, A.1    Hausalo, T.2    Tenkanen, M.3    Vuorinen, T.4
  • 22
  • 23
    • 0035433271 scopus 로고    scopus 로고
    • Enzymatic synthesis and hydrolysis of xylogluco-oligosaccharides using the first archaeal alpha-xylosidase from Sulfolobus solfataricus
    • Trincone A., Cobucci-Ponzano B., Di Lauro B., Rossi M., Mitsuishi Y., Moracci M. Enzymatic synthesis and hydrolysis of xylogluco-oligosaccharides using the first archaeal alpha-xylosidase from Sulfolobus solfataricus. Extremophiles 2001, 5:277-282.
    • (2001) Extremophiles , vol.5 , pp. 277-282
    • Trincone, A.1    Cobucci-Ponzano, B.2    Di Lauro, B.3    Rossi, M.4    Mitsuishi, Y.5    Moracci, M.6
  • 25
    • 84875480751 scopus 로고    scopus 로고
    • Pyrosequencing reveals high-temperature cellulolytic microbial consortia in great boiling spring after In Situ lignocellulose enrichment
    • Peacock J.P., Cole J.K., Murugapiran S.K., Dodsworth J.A., Fisher J.C., Moser D.P., et al. Pyrosequencing reveals high-temperature cellulolytic microbial consortia in great boiling spring after In Situ lignocellulose enrichment. PloS One 2013, 8.
    • (2013) PloS One , vol.8
    • Peacock, J.P.1    Cole, J.K.2    Murugapiran, S.K.3    Dodsworth, J.A.4    Fisher, J.C.5    Moser, D.P.6
  • 28
    • 3042846865 scopus 로고    scopus 로고
    • A thermostable non-xylanolytic alpha-glucuronidase of Thermotoga maritima MSB8
    • Suresh C., Kitaoka M., Hayashi K. A thermostable non-xylanolytic alpha-glucuronidase of Thermotoga maritima MSB8. Biosci. Biotechnol. Biochem. 2003, 67:2359-2364.
    • (2003) Biosci. Biotechnol. Biochem. , vol.67 , pp. 2359-2364
    • Suresh, C.1    Kitaoka, M.2    Hayashi, K.3
  • 29
    • 0036223466 scopus 로고    scopus 로고
    • The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A
    • Nurizzo D., Nagy T., Gilbert H.J., Davies G.J. The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A. Structure 2002, 10:547-556.
    • (2002) Structure , vol.10 , pp. 547-556
    • Nurizzo, D.1    Nagy, T.2    Gilbert, H.J.3    Davies, G.J.4
  • 30
    • 9144241621 scopus 로고    scopus 로고
    • Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products - Mechanistic implications
    • Golan G., Shallom D., Teplitsky A., Zaide G., Shulami S., Baasov T., et al. Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products - Mechanistic implications. J. Biol. Chem. 2004, 279:3014-3024.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3014-3024
    • Golan, G.1    Shallom, D.2    Teplitsky, A.3    Zaide, G.4    Shulami, S.5    Baasov, T.6
  • 31
    • 0024763430 scopus 로고
    • Purification and characterization of an alpha-d-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus
    • Khandke K.M., Vithayathil P.J., Murthy S.K. Purification and characterization of an alpha-d-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus. Arch. Biochem. Biophys. 1989, 274:511-517.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 511-517
    • Khandke, K.M.1    Vithayathil, P.J.2    Murthy, S.K.3
  • 32
    • 0034629241 scopus 로고    scopus 로고
    • An alpha-glucuronidase of Schizophyllum commune acting on polymeric xylan
    • Tenkanen M., Siika-aho M. An alpha-glucuronidase of Schizophyllum commune acting on polymeric xylan. J. Biotechnol. 2000, 78:149-161.
    • (2000) J. Biotechnol. , vol.78 , pp. 149-161
    • Tenkanen, M.1    Siika-aho, M.2
  • 34
    • 12144282020 scopus 로고    scopus 로고
    • Xylanases, xylanase families and extremophilic xylanases
    • Collins T., Gerday C., Feller G. Xylanases, xylanase families and extremophilic xylanases. FEMS Microbiol. Rev. 2005, 29:3-23.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 3-23
    • Collins, T.1    Gerday, C.2    Feller, G.3
  • 35
    • 30944437053 scopus 로고    scopus 로고
    • Mode of action of endo-beta-1,4-xylanases of families 10 and 11 on acidic xylooligosaccharides
    • Kolenova K., Vrsanska M., Biely P. Mode of action of endo-beta-1,4-xylanases of families 10 and 11 on acidic xylooligosaccharides. J. Biotechnol. 2006, 121:338-345.
    • (2006) J. Biotechnol. , vol.121 , pp. 338-345
    • Kolenova, K.1    Vrsanska, M.2    Biely, P.3
  • 36
    • 70350156419 scopus 로고    scopus 로고
    • Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with cello-oligosaccharides: strong -1 and -2 subsites mimic cellobiohydrolase activity
    • Eckert K., Vigouroux A., Lo Leggio L., Morera S. Crystal structures of A. acidocaldarius endoglucanase Cel9A in complex with cello-oligosaccharides: strong -1 and -2 subsites mimic cellobiohydrolase activity. J. Mol. Biol. 2009, 394:61-70.
    • (2009) J. Mol. Biol. , vol.394 , pp. 61-70
    • Eckert, K.1    Vigouroux, A.2    Lo Leggio, L.3    Morera, S.4
  • 37
    • 33748291593 scopus 로고    scopus 로고
    • Characterization of a beta-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius
    • Di Lauro B., Rossi M., Moracci M. Characterization of a beta-glycosidase from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius. Extremophiles 2006, 10:301-310.
    • (2006) Extremophiles , vol.10 , pp. 301-310
    • Di Lauro, B.1    Rossi, M.2    Moracci, M.3
  • 38
    • 41349111304 scopus 로고    scopus 로고
    • Polysaccharide degradation and synthesis by extremely thermophilic anaerobes
    • Vanfossen A.L., Lewis D.L., Nichols J.D., Kelly R.M. Polysaccharide degradation and synthesis by extremely thermophilic anaerobes. Ann. N. Y. Acad. Sci. 2008, 1125:322-337.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1125 , pp. 322-337
    • Vanfossen, A.L.1    Lewis, D.L.2    Nichols, J.D.3    Kelly, R.M.4
  • 39
    • 84856188460 scopus 로고    scopus 로고
    • S-layer homology domain proteins Csac_0678 and Csac_2722 are implicated in plant polysaccharide deconstruction by the extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus
    • Ozdemir I., Blumer-Schuette S.E., Kelly R.M. S-layer homology domain proteins Csac_0678 and Csac_2722 are implicated in plant polysaccharide deconstruction by the extremely thermophilic bacterium Caldicellulosiruptor saccharolyticus. Appl. Environ. Microbiol. 2012, 78:768-777.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 768-777
    • Ozdemir, I.1    Blumer-Schuette, S.E.2    Kelly, R.M.3
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 42
    • 84873946502 scopus 로고    scopus 로고
    • Biochemical properties of a novel thermostable and highly xylose-tolerant beta-xylosidase/alpha-arabinosidase from Thermotoga thermarum
    • Shi H., Li X., Gu H.X., Zhang Y., Huang Y.J., Wang L.L., et al. Biochemical properties of a novel thermostable and highly xylose-tolerant beta-xylosidase/alpha-arabinosidase from Thermotoga thermarum. Biotechnol. Biofuels 2013, 6.
    • (2013) Biotechnol. Biofuels , vol.6
    • Shi, H.1    Li, X.2    Gu, H.X.3    Zhang, Y.4    Huang, Y.J.5    Wang, L.L.6
  • 43
    • 0000674033 scopus 로고
    • A photometric adaptation of the somogyi method for the determination of glucose
    • Nelson N. A photometric adaptation of the somogyi method for the determination of glucose. J. Biol. Chem. 1944, 153:375-380.
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.1
  • 44
    • 33750423631 scopus 로고
    • Notes on sugar determination
    • Somogyi M. Notes on sugar determination. J. Biol. Chem. 1952, 195:19-23.
    • (1952) J. Biol. Chem. , vol.195 , pp. 19-23
    • Somogyi, M.1
  • 45
    • 17644427704 scopus 로고    scopus 로고
    • Probing the catalytically essential residues of the alpha-L-fucosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus
    • Cobucci-Ponzano B., Mazzone M., Rossi M., Moracci M. Probing the catalytically essential residues of the alpha-L-fucosidase from the hyperthermophilic Archaeon Sulfolobus solfataricus. Biochemistry-US 2005, 44:6331-6342.
    • (2005) Biochemistry-US , vol.44 , pp. 6331-6342
    • Cobucci-Ponzano, B.1    Mazzone, M.2    Rossi, M.3    Moracci, M.4
  • 46
    • 76449108319 scopus 로고    scopus 로고
    • A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability
    • Bai Y., Wang J., Zhang Z., Yang P., Shi P., Luo H., et al. A new xylanase from thermoacidophilic Alicyclobacillus sp. A4 with broad-range pH activity and pH stability. J. Indus. Microbiol. Biotechnol. 2010, 37:187-194.
    • (2010) J. Indus. Microbiol. Biotechnol. , vol.37 , pp. 187-194
    • Bai, Y.1    Wang, J.2    Zhang, Z.3    Yang, P.4    Shi, P.5    Luo, H.6
  • 47
    • 84874702796 scopus 로고    scopus 로고
    • Reconstitution of a thermostable Xylan-degrading enzyme mixture from the bacterium Caldicellulosiruptor bescii
    • Su X.Y., Han Y.J., Dodd D., Moon Y.H., Yoshida S., Mackie R.I., et al. Reconstitution of a thermostable Xylan-degrading enzyme mixture from the bacterium Caldicellulosiruptor bescii. Appl. Environ. Microb. 2013, 79:1481-1490.
    • (2013) Appl. Environ. Microb. , vol.79 , pp. 1481-1490
    • Su, X.Y.1    Han, Y.J.2    Dodd, D.3    Moon, Y.H.4    Yoshida, S.5    Mackie, R.I.6
  • 49
    • 0031014417 scopus 로고    scopus 로고
    • Isolation and analysis of a gene encoding alpha-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan
    • Ruile P., Winterhalter C., Liebl W. Isolation and analysis of a gene encoding alpha-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan. Mol. Microbiol. 1997, 23:267-279.
    • (1997) Mol. Microbiol. , vol.23 , pp. 267-279
    • Ruile, P.1    Winterhalter, C.2    Liebl, W.3
  • 50
    • 0038353117 scopus 로고    scopus 로고
    • Identification of an archaeal alpha-l-fucosidase encoded by an interrupted gene. Production of a functional enzyme by mutations mimicking programmed -1 frameshifting (vol 278, pg 14,622, 2003)
    • Cobucci-Ponzano B., Trincone A., Giordano A., Rossi M., Moracci M. Identification of an archaeal alpha-l-fucosidase encoded by an interrupted gene. Production of a functional enzyme by mutations mimicking programmed -1 frameshifting (vol 278, pg 14,622, 2003). J. Biol. Chem 2003, 278:47350.
    • (2003) J. Biol. Chem , vol.278 , pp. 47350
    • Cobucci-Ponzano, B.1    Trincone, A.2    Giordano, A.3    Rossi, M.4    Moracci, M.5
  • 51
    • 0033677793 scopus 로고    scopus 로고
    • A novel thermostable multidomain 1,4-beta-xylanase from 'Caldibacillus cellulovorans' and effect of its xylan-binding domain on enzyme activity
    • Sunna A., Gibbs M.D., Bergquist P.L. A novel thermostable multidomain 1,4-beta-xylanase from 'Caldibacillus cellulovorans' and effect of its xylan-binding domain on enzyme activity. Microbiology 2000, 146(Pt (11)):2947-2955.
    • (2000) Microbiology , vol.146 , pp. 2947-2955
    • Sunna, A.1    Gibbs, M.D.2    Bergquist, P.L.3
  • 52
    • 0027246551 scopus 로고
    • Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6
    • Khasin A., Alchanati I., Shoham Y. Purification and characterization of a thermostable xylanase from Bacillus stearothermophilus T-6. Appl. Environ. Microbiol. 1993, 59:1725-1730.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1725-1730
    • Khasin, A.1    Alchanati, I.2    Shoham, Y.3
  • 53
    • 0025870894 scopus 로고
    • An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga
    • Simpson H.D., Haufler U.R., Daniel R.M. An extremely thermostable xylanase from the thermophilic eubacterium Thermotoga. Biochem J. 1991, 277(Pt (2)):413-417.
    • (1991) Biochem J. , vol.277 , pp. 413-417
    • Simpson, H.D.1    Haufler, U.R.2    Daniel, R.M.3
  • 54
    • 17844396234 scopus 로고    scopus 로고
    • Characterization of a novel, ultra-large xylanolytic complex (xylanosome) from Streptomyces olivaceoviridis E-86
    • Jiang Z.Q., Deng W., Li X.T., Ai Z.L., Li L.T., Kusakabe I. Characterization of a novel, ultra-large xylanolytic complex (xylanosome) from Streptomyces olivaceoviridis E-86. Enzyme Microb. Tech. 2005, 36:923-929.
    • (2005) Enzyme Microb. Tech. , vol.36 , pp. 923-929
    • Jiang, Z.Q.1    Deng, W.2    Li, X.T.3    Ai, Z.L.4    Li, L.T.5    Kusakabe, I.6
  • 55
    • 84884352075 scopus 로고    scopus 로고
    • A novel neutral xylanase with high SDS resistance from Volvariella volvacea: characterization and its synergistic hydrolysis of wheat bran with acetyl xylan esterase
    • Zheng F., Huang J.X., Yin Y.H., Ding S.J. A novel neutral xylanase with high SDS resistance from Volvariella volvacea: characterization and its synergistic hydrolysis of wheat bran with acetyl xylan esterase. J. Indus. Microbiol. Biotechnol. 2013, 40:1083-1093.
    • (2013) J. Indus. Microbiol. Biotechnol. , vol.40 , pp. 1083-1093
    • Zheng, F.1    Huang, J.X.2    Yin, Y.H.3    Ding, S.J.4
  • 56
    • 84880985423 scopus 로고    scopus 로고
    • Characterization and constitutive expression of a novel endo-1,4-beta-d-xylanohydrolase from Aspergillus niger in Pichia pastoris
    • Zheng J., Guo N., Wu L.S., Tian J., Zhou H.B. Characterization and constitutive expression of a novel endo-1,4-beta-d-xylanohydrolase from Aspergillus niger in Pichia pastoris. Biotechnol. Lett. 2013, 35:1433-1440.
    • (2013) Biotechnol. Lett. , vol.35 , pp. 1433-1440
    • Zheng, J.1    Guo, N.2    Wu, L.S.3    Tian, J.4    Zhou, H.B.5
  • 57
    • 77952879995 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the novel acidic xylanase XYLD from Bispora sp MEY-1 that is homologous to family 30 glycosyl hydrolases
    • Luo H.Y., Yang J., Li J., Shi P.J., Huang H.Q., Bai Y.G., et al. Molecular cloning and characterization of the novel acidic xylanase XYLD from Bispora sp MEY-1 that is homologous to family 30 glycosyl hydrolases. Appl. Microbiol. Biotechnol. 2010, 86:1829-1839.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1829-1839
    • Luo, H.Y.1    Yang, J.2    Li, J.3    Shi, P.J.4    Huang, H.Q.5    Bai, Y.G.6
  • 58
    • 79955631894 scopus 로고    scopus 로고
    • Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1
    • Hung K.S., Liu S.M., Tzou W.S., Lin F.P., Pan C.L., Fang T.Y., et al. Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1. Process Biochem. 2011, 46:1257-1263.
    • (2011) Process Biochem. , vol.46 , pp. 1257-1263
    • Hung, K.S.1    Liu, S.M.2    Tzou, W.S.3    Lin, F.P.4    Pan, C.L.5    Fang, T.Y.6
  • 59
    • 84906968543 scopus 로고    scopus 로고
    • Insight into glycoside hydrolases for debranched xylan degradation from extremely thermophilic bacterium Caldicellulosiruptor lactoaceticus
    • Jia X.J., Mi S.F., Wang J.Z., Qiao W.B., Peng X.W., Han Y.J. Insight into glycoside hydrolases for debranched xylan degradation from extremely thermophilic bacterium Caldicellulosiruptor lactoaceticus. PLoS One 2014, 9.
    • (2014) PLoS One , vol.9
    • Jia, X.J.1    Mi, S.F.2    Wang, J.Z.3    Qiao, W.B.4    Peng, X.W.5    Han, Y.J.6
  • 60
    • 32944473847 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable-cellulase free xylanase from Syncephalastrum racemosum Cohn
    • Sapre M.P., Jha H., Patil M.B. Purification and characterization of a thermostable-cellulase free xylanase from Syncephalastrum racemosum Cohn. J. Gen. Appl. Microbiol. 2005, 51:327-334.
    • (2005) J. Gen. Appl. Microbiol. , vol.51 , pp. 327-334
    • Sapre, M.P.1    Jha, H.2    Patil, M.B.3
  • 61
    • 84858707775 scopus 로고    scopus 로고
    • Purification and biochemical characterization of a highly thermostable xylanase from Actinomadura sp strain Cpt20 isolated from poultry compost
    • Taibi Z., Saoudi B., Boudelaa M., Trigui H., Belghith H., Gargouri A., et al. Purification and biochemical characterization of a highly thermostable xylanase from Actinomadura sp strain Cpt20 isolated from poultry compost. Appl. Biochem. Biotechnol. 2012, 166:663-679.
    • (2012) Appl. Biochem. Biotechnol. , vol.166 , pp. 663-679
    • Taibi, Z.1    Saoudi, B.2    Boudelaa, M.3    Trigui, H.4    Belghith, H.5    Gargouri, A.6
  • 62
    • 84881193401 scopus 로고    scopus 로고
    • A novel thermostable cellulase free xylanase stable in broad range of pH from Streptomyces sp. CS428
    • Pradeep G.C., Choi Y.H., Choi Y.S., Seong C.N., Cho S.S., Lee H.J., et al. A novel thermostable cellulase free xylanase stable in broad range of pH from Streptomyces sp. CS428. Process Biochem. 2013, 48:1188-1196.
    • (2013) Process Biochem. , vol.48 , pp. 1188-1196
    • Pradeep, G.C.1    Choi, Y.H.2    Choi, Y.S.3    Seong, C.N.4    Cho, S.S.5    Lee, H.J.6
  • 63
    • 0031715687 scopus 로고    scopus 로고
    • Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp
    • Gessesse A. Purification and properties of two thermostable alkaline xylanases from an alkaliphilic Bacillus sp. Appl. Environ. Microb. 1998, 64:3533-3535.
    • (1998) Appl. Environ. Microb. , vol.64 , pp. 3533-3535
    • Gessesse, A.1
  • 64
    • 84867411201 scopus 로고    scopus 로고
    • Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus
    • Han Y., Agarwal V., Dodd D., Kim J., Bae B., Mackie R.I., et al. Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus. J. Biol. Chem. 2012, 287:34946-34960.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34946-34960
    • Han, Y.1    Agarwal, V.2    Dodd, D.3    Kim, J.4    Bae, B.5    Mackie, R.I.6
  • 65
    • 0034833426 scopus 로고    scopus 로고
    • Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6
    • Zaide G., Shallom D., Shulami S., Zolotnitsky G., Golan G., Baasov T., et al. Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6. Eur. J. Biochem. 2001, 268:3006-3016.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3006-3016
    • Zaide, G.1    Shallom, D.2    Shulami, S.3    Zolotnitsky, G.4    Golan, G.5    Baasov, T.6
  • 66
    • 0034577636 scopus 로고    scopus 로고
    • Gene cloning and characterization of alpha-glucuronidase of Bacillus stearothermophilus No. 236
    • Choi I.D., Kim H.Y., Choi Y.J. Gene cloning and characterization of alpha-glucuronidase of Bacillus stearothermophilus No. 236. Biosci. Biotechnol. Biochem. 2000, 64:2530-2537.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 2530-2537
    • Choi, I.D.1    Kim, H.Y.2    Choi, Y.J.3
  • 67
    • 67649622092 scopus 로고    scopus 로고
    • Aldouronate utilization in Paenibacillus sp strain JDR-2: physiological and enzymatic evidence for coupling of extracellular depolymerization and intracellular metabolism
    • Nong G., Rice J.D., Chow V., Preston J.F. Aldouronate utilization in Paenibacillus sp strain JDR-2: physiological and enzymatic evidence for coupling of extracellular depolymerization and intracellular metabolism. Appl. Environ. Microb. 2009, 75:4410-4418.
    • (2009) Appl. Environ. Microb. , vol.75 , pp. 4410-4418
    • Nong, G.1    Rice, J.D.2    Chow, V.3    Preston, J.F.4
  • 68
    • 30944438685 scopus 로고    scopus 로고
    • Characterization of the Aureobasidium pullulans alpha-glucuronidase expressed in Saccharomyces cerevisiae
    • de Wet B.J.M., van Zyl W.H., Prior B.A. Characterization of the Aureobasidium pullulans alpha-glucuronidase expressed in Saccharomyces cerevisiae. Enzyme Microb. Technol. 2006, 38:649-656.
    • (2006) Enzyme Microb. Technol. , vol.38 , pp. 649-656
    • de Wet, B.J.M.1    van Zyl, W.H.2    Prior, B.A.3
  • 70
    • 0036716744 scopus 로고    scopus 로고
    • The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-d-glucuronoxylooligosaccharides but not 4-O-methyl-d-glucuronoxylan
    • Nagy T., Emami K., Fontes C.M.G.A., Ferreira L.M.A., Humphry D.R., Gilbert H.J. The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-d-glucuronoxylooligosaccharides but not 4-O-methyl-d-glucuronoxylan. J. Bacteriol. 2002, 184:4925-4929.
    • (2002) J. Bacteriol. , vol.184 , pp. 4925-4929
    • Nagy, T.1    Emami, K.2    Fontes, C.M.G.A.3    Ferreira, L.M.A.4    Humphry, D.R.5    Gilbert, H.J.6
  • 71
    • 84904303999 scopus 로고    scopus 로고
    • Novel Alkali-Tolerant GH10 Endo-beta-1,4-Xylanase with broad substrate specificity from microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis
    • Kim D.Y., Shin D.H., Jung S., Kim H., Lee J.S., Cho H.Y., et al. Novel Alkali-Tolerant GH10 Endo-beta-1,4-Xylanase with broad substrate specificity from microbacterium trichothecenolyticum HY-17, a gut bacterium of the mole cricket Gryllotalpa orientalis. J. Microbiol. Biotechnol. 2014, 24:943-953.
    • (2014) J. Microbiol. Biotechnol. , vol.24 , pp. 943-953
    • Kim, D.Y.1    Shin, D.H.2    Jung, S.3    Kim, H.4    Lee, J.S.5    Cho, H.Y.6
  • 72
    • 0342468763 scopus 로고    scopus 로고
    • Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high activity against aryl xylosides
    • Blanco A., Diaz P., Martinez J., Lopez O., Soler C., Pastor F.I. Cloning of a Bacillus sp. BP-23 gene encoding a xylanase with high activity against aryl xylosides. FEMS Microbiol. Lett. 1996, 137:285-290.
    • (1996) FEMS Microbiol. Lett. , vol.137 , pp. 285-290
    • Blanco, A.1    Diaz, P.2    Martinez, J.3    Lopez, O.4    Soler, C.5    Pastor, F.I.6
  • 73
    • 0033900331 scopus 로고    scopus 로고
    • A novel Cellvibrio mixtus family 10 xylanase that is both intracellular and expressed under non-inducing conditions
    • Fontes C.M., Gilbert H.J., Hazlewood G.P., Clarke J.H., Prates J.A., McKie V.A., et al. A novel Cellvibrio mixtus family 10 xylanase that is both intracellular and expressed under non-inducing conditions. Microbiology 2000, 146(Pt (8)):1959-1967.
    • (2000) Microbiology , vol.146 , pp. 1959-1967
    • Fontes, C.M.1    Gilbert, H.J.2    Hazlewood, G.P.3    Clarke, J.H.4    Prates, J.A.5    McKie, V.A.6
  • 74
    • 0038170509 scopus 로고    scopus 로고
    • A cytoplasmic xylanase (XynX) of Aeromonas caviae ME-1 is released from the cytoplasm to the periplasm by osmotic downshock
    • Usui K., Suzuki T., Akisaka T., Kawai K. A cytoplasmic xylanase (XynX) of Aeromonas caviae ME-1 is released from the cytoplasm to the periplasm by osmotic downshock. J. Biosci. Bioeng. 2003, 95:488-495.
    • (2003) J. Biosci. Bioeng. , vol.95 , pp. 488-495
    • Usui, K.1    Suzuki, T.2    Akisaka, T.3    Kawai, K.4
  • 75
    • 0037165613 scopus 로고    scopus 로고
    • Evidence that the putative alpha-glucosidase of Thermotoga maritima MSB8 is a pNP alpha-d-glucuronopyranoside hydrolyzing alpha-glucuronidase
    • Suresh C., Rus'd A.A., Kitaoka M., Hayashi K. Evidence that the putative alpha-glucosidase of Thermotoga maritima MSB8 is a pNP alpha-d-glucuronopyranoside hydrolyzing alpha-glucuronidase. FEBS Lett. 2002, 517:159-162.
    • (2002) FEBS Lett. , vol.517 , pp. 159-162
    • Suresh, C.1    Rus'd, A.A.2    Kitaoka, M.3    Hayashi, K.4


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