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Volumn 234, Issue , 2015, Pages 180-193

Destructuring plant biomass: Focus on fungal and extremophilic cell wall hydrolases

Author keywords

Carbohydrate active enzymes; Extremozymes; Fungal secretome; Lignocellulosic biomass; Saccharification; Synergistic activation

Indexed keywords

ASCOMYCOTA; BASIDIOMYCOTA; FUNGI; ZYGOMYCOTA;

EID: 84924322683     PISSN: 01689452     EISSN: 18732259     Source Type: Journal    
DOI: 10.1016/j.plantsci.2015.02.010     Document Type: Review
Times cited : (61)

References (126)
  • 1
    • 84907809719 scopus 로고    scopus 로고
    • Wood biosynthesis and typologies: a molecular rhapsody
    • Guerriero G., Sergeant K., Hausman J.F. Wood biosynthesis and typologies: a molecular rhapsody. Tree Physiol. 2014, 34:839-855.
    • (2014) Tree Physiol. , vol.34 , pp. 839-855
    • Guerriero, G.1    Sergeant, K.2    Hausman, J.F.3
  • 2
    • 84896276495 scopus 로고    scopus 로고
    • Exploration of Natural Biomass Utilization Systems (NBUS) for advanced biofuel-from systems biology to synthetic design
    • Xie S., Syrenne R., Sun S., Yuan J.S. Exploration of Natural Biomass Utilization Systems (NBUS) for advanced biofuel-from systems biology to synthetic design. Curr. Opin. Biotechnol. 2014, 27:195-203.
    • (2014) Curr. Opin. Biotechnol. , vol.27 , pp. 195-203
    • Xie, S.1    Syrenne, R.2    Sun, S.3    Yuan, J.S.4
  • 3
    • 84872450433 scopus 로고    scopus 로고
    • Using a model filamentous fungus to unravel mechanisms of lignocellulose deconstruction
    • Znameroski E.A., Glass N.L. Using a model filamentous fungus to unravel mechanisms of lignocellulose deconstruction. Biotechnol. Biofuels 2013, 6:6.
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 6
    • Znameroski, E.A.1    Glass, N.L.2
  • 4
    • 78650389400 scopus 로고    scopus 로고
    • U.S. Department of Agriculture, Washington, DC
    • USDA USDA Biofuels Strategic Production Report 2010, 1-23. U.S. Department of Agriculture, Washington, DC.
    • (2010) USDA Biofuels Strategic Production Report , pp. 1-23
  • 5
    • 84884905699 scopus 로고    scopus 로고
    • Improved recombinant cellulase expression in chloroplast of tobacco through promoter engineering and 5' amplification promoting sequence
    • Jung S., Lee D.S., Kim Y.O., Joshi C.P., Bae H.J. Improved recombinant cellulase expression in chloroplast of tobacco through promoter engineering and 5' amplification promoting sequence. Plant Mol. Biol. 2013, 83:317-328.
    • (2013) Plant Mol. Biol. , vol.83 , pp. 317-328
    • Jung, S.1    Lee, D.S.2    Kim, Y.O.3    Joshi, C.P.4    Bae, H.J.5
  • 6
    • 84902301203 scopus 로고    scopus 로고
    • The genome of the white-rot fungus Pycnoporus cinnabarinus: a basidiomycete model with a versatile arsenal for lignocellulosic biomass breakdown
    • Levasseur A., et al. The genome of the white-rot fungus Pycnoporus cinnabarinus: a basidiomycete model with a versatile arsenal for lignocellulosic biomass breakdown. BMC Genomics 2014, 15:486.
    • (2014) BMC Genomics , vol.15 , pp. 486
    • Levasseur, A.1
  • 7
    • 84903975698 scopus 로고    scopus 로고
    • Extensive sampling of basidiomycete genomes demonstrates inadequacy of the white-rot/brown-rot paradigm for wood decay fungi
    • Riley R., et al. Extensive sampling of basidiomycete genomes demonstrates inadequacy of the white-rot/brown-rot paradigm for wood decay fungi. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:9923-9928.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 9923-9928
    • Riley, R.1
  • 10
    • 70350502815 scopus 로고    scopus 로고
    • Fungal bioconversion of lignocellulosic residues; opportunities & perspectives
    • Dashtban M., Schraft H., Qin W. Fungal bioconversion of lignocellulosic residues; opportunities & perspectives. Intl. J. Biol. Sci. 2009, 5:578-595.
    • (2009) Intl. J. Biol. Sci. , vol.5 , pp. 578-595
    • Dashtban, M.1    Schraft, H.2    Qin, W.3
  • 11
    • 84921761146 scopus 로고    scopus 로고
    • Fungal degradation of lignocellulosic residues: an aspect of improved nutritive quality
    • Sharma R.K., Arora D.S. Fungal degradation of lignocellulosic residues: an aspect of improved nutritive quality. Crit. Rev. Microbiol. 2015, 41:52-60.
    • (2015) Crit. Rev. Microbiol. , vol.41 , pp. 52-60
    • Sharma, R.K.1    Arora, D.S.2
  • 12
    • 84924286372 scopus 로고    scopus 로고
    • Evaluation of mycotoxin sequestering agents for aflatoxin and deoxynivalenol: an in vitro approach
    • Kong C., Shin S.Y., Kim B.G. Evaluation of mycotoxin sequestering agents for aflatoxin and deoxynivalenol: an in vitro approach. SpringerPlus 2014, 3:346.
    • (2014) SpringerPlus , vol.3 , pp. 346
    • Kong, C.1    Shin, S.Y.2    Kim, B.G.3
  • 13
    • 84866145069 scopus 로고    scopus 로고
    • Uncovering the genome-wide transcriptional responses of the filamentous fungus Aspergillus niger to lignocellulose using RNA sequencing
    • Delmas S., et al. Uncovering the genome-wide transcriptional responses of the filamentous fungus Aspergillus niger to lignocellulose using RNA sequencing. PLoS Genet. 2012, 8:e1002875.
    • (2012) PLoS Genet. , vol.8 , pp. e1002875
    • Delmas, S.1
  • 14
    • 84893379544 scopus 로고    scopus 로고
    • Investigating Aspergillus nidulans secretome during colonisation of cork cell walls
    • Martins I., et al. Investigating Aspergillus nidulans secretome during colonisation of cork cell walls. J. Proteomics 2014, 98:175-188.
    • (2014) J. Proteomics , vol.98 , pp. 175-188
    • Martins, I.1
  • 16
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries R.P., Visser J. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 2001, 65:497-522.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 497-522
    • de Vries, R.P.1    Visser, J.2
  • 17
    • 84879245430 scopus 로고    scopus 로고
    • Functional characterisation of the non-essential protein kinases and phosphatases regulating Aspergillus nidulans hydrolytic enzyme production
    • Brown N.A., de Gouvea P.F., Krohn N.G., Savoldi M., Goldman G.H. Functional characterisation of the non-essential protein kinases and phosphatases regulating Aspergillus nidulans hydrolytic enzyme production. Biotechnol. Biofuels 2013, 6:91.
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 91
    • Brown, N.A.1    de Gouvea, P.F.2    Krohn, N.G.3    Savoldi, M.4    Goldman, G.H.5
  • 18
    • 33749506041 scopus 로고    scopus 로고
    • Amino acid acquisition, cross-pathway control, and virulence in A. fumigatus
    • Braus G.H., Sasse C., Krappmann S. Amino acid acquisition, cross-pathway control, and virulence in A. fumigatus. Med. Mycol. 2006, 44:S91-S94.
    • (2006) Med. Mycol. , vol.44 , pp. S91-S94
    • Braus, G.H.1    Sasse, C.2    Krappmann, S.3
  • 19
    • 0035971180 scopus 로고    scopus 로고
    • The TOR kinases link nutrient sensing to cell growth
    • Rohde J., Heitman J., Cardenas M.E. The TOR kinases link nutrient sensing to cell growth. J. Biol. Chem. 2001, 276:9583-9586.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9583-9586
    • Rohde, J.1    Heitman, J.2    Cardenas, M.E.3
  • 20
    • 79960685159 scopus 로고    scopus 로고
    • The cross-pathway control system regulates production of the secondary metabolite toxin, sirodesmin PL, in the ascomycete, Leptosphaeria maculans
    • Elliott C.E., Fox E.M., Jarvis R.S., Howlett B.J. The cross-pathway control system regulates production of the secondary metabolite toxin, sirodesmin PL, in the ascomycete, Leptosphaeria maculans. BMC Microbiol. 2011, 11:169.
    • (2011) BMC Microbiol. , vol.11 , pp. 169
    • Elliott, C.E.1    Fox, E.M.2    Jarvis, R.S.3    Howlett, B.J.4
  • 21
    • 84893489724 scopus 로고    scopus 로고
    • Evidence for transceptor function of cellodextrin transporters in Neurospora crassa
    • Znameroski E.A., et al. Evidence for transceptor function of cellodextrin transporters in Neurospora crassa. J. Biol. Chem. 2014, 289:2610-2619.
    • (2014) J. Biol. Chem. , vol.289 , pp. 2610-2619
    • Znameroski, E.A.1
  • 22
    • 80054118479 scopus 로고    scopus 로고
    • Transcriptome analysis of Aspergillus niger grown on sugarcane bagasse
    • de Souza W.R., et al. Transcriptome analysis of Aspergillus niger grown on sugarcane bagasse. Biotechnol. Biofuels. 2011, 4:40.
    • (2011) Biotechnol. Biofuels. , vol.4 , pp. 40
    • de Souza, W.R.1
  • 23
    • 34548800815 scopus 로고    scopus 로고
    • Substrate pretreatment: the key to effective enzymatic hydrolysis of lignocellulosics?
    • Chandra R.P., et al. Substrate pretreatment: the key to effective enzymatic hydrolysis of lignocellulosics?. Adv. Biochem. Eng./Biotechnol. 2007, 108:67-93.
    • (2007) Adv. Biochem. Eng./Biotechnol. , vol.108 , pp. 67-93
    • Chandra, R.P.1
  • 24
    • 65249115211 scopus 로고    scopus 로고
    • Methods for pretreatment of lignocellulosic biomass for efficient hydrolysis and biofuel production
    • Kumar P., Barrett D.M., Delwiche M.J., Stroeve P. Methods for pretreatment of lignocellulosic biomass for efficient hydrolysis and biofuel production. Ind. Eng. Chem. Res. 2009, 48:3713-3729.
    • (2009) Ind. Eng. Chem. Res. , vol.48 , pp. 3713-3729
    • Kumar, P.1    Barrett, D.M.2    Delwiche, M.J.3    Stroeve, P.4
  • 25
    • 0033527088 scopus 로고    scopus 로고
    • Fermentability of the hemicellulose-derived sugars from steam-exploded softwood (douglas fir)
    • Boussaid A., Robinson J., Cai Y.J., Gregg D.J., Saddler J.N. Fermentability of the hemicellulose-derived sugars from steam-exploded softwood (douglas fir). Biotechnol. Bioeng. 1999, 64:284-289.
    • (1999) Biotechnol. Bioeng. , vol.64 , pp. 284-289
    • Boussaid, A.1    Robinson, J.2    Cai, Y.J.3    Gregg, D.J.4    Saddler, J.N.5
  • 26
    • 33646912813 scopus 로고    scopus 로고
    • Updates on softwood-to-ethanol process development
    • Mabee W.E., et al. Updates on softwood-to-ethanol process development. Appl. Biochem. Biotechnol. 2006, 129-132:55-70.
    • (2006) Appl. Biochem. Biotechnol. , pp. 55-70
    • Mabee, W.E.1
  • 27
    • 84872184440 scopus 로고    scopus 로고
    • Systems biological approaches towards understanding cellulase production by Trichoderma reesei
    • Kubicek C.P. Systems biological approaches towards understanding cellulase production by Trichoderma reesei. J. Biotechnol. 2013, 163:133-142.
    • (2013) J. Biotechnol. , vol.163 , pp. 133-142
    • Kubicek, C.P.1
  • 28
    • 84860805742 scopus 로고    scopus 로고
    • Conserved and essential transcription factors for cellulase gene expression in ascomycete fungi
    • Coradetti S.T., et al. Conserved and essential transcription factors for cellulase gene expression in ascomycete fungi. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:7397-7402.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 7397-7402
    • Coradetti, S.T.1
  • 29
    • 84924302956 scopus 로고    scopus 로고
    • VIB1, a link between glucose signaling and carbon catabolite repression, is essential for plant cell wall degradation by Neurospora crassa
    • Xiong Y., Sun J., Glass N.L. VIB1, a link between glucose signaling and carbon catabolite repression, is essential for plant cell wall degradation by Neurospora crassa. PLoS Genet. 2014, 10:e1004500.
    • (2014) PLoS Genet. , vol.10 , pp. e1004500
    • Xiong, Y.1    Sun, J.2    Glass, N.L.3
  • 30
    • 84908550191 scopus 로고    scopus 로고
    • The proteome and phosphoproteome of Neurospora crassa in response to cellulose, sucrose and carbon starvation
    • Xiong Y., et al. The proteome and phosphoproteome of Neurospora crassa in response to cellulose, sucrose and carbon starvation. Fungal Genet. Biol. 2014, 72:21-33.
    • (2014) Fungal Genet. Biol. , vol.72 , pp. 21-33
    • Xiong, Y.1
  • 31
    • 84859420715 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: insight into manganese peroxidase activation and lignin peroxidase inhibition
    • Ertan H., Siddiqui K.S., Muenchhoff J., Charlton T., Cavicchioli R. Kinetic and thermodynamic characterization of the functional properties of a hybrid versatile peroxidase using isothermal titration calorimetry: insight into manganese peroxidase activation and lignin peroxidase inhibition. Biochimie 2012, 94:1221-1231.
    • (2012) Biochimie , vol.94 , pp. 1221-1231
    • Ertan, H.1    Siddiqui, K.S.2    Muenchhoff, J.3    Charlton, T.4    Cavicchioli, R.5
  • 32
    • 84896448424 scopus 로고    scopus 로고
    • Versatile peroxidase degradation of humic substances: use of isothermal titration calorimetry to assess kinetics and applications to industrial wastes
    • Siddiqui K.S., et al. Versatile peroxidase degradation of humic substances: use of isothermal titration calorimetry to assess kinetics and applications to industrial wastes. J. Biotechnol. 2014, 178:1-11.
    • (2014) J. Biotechnol. , vol.178 , pp. 1-11
    • Siddiqui, K.S.1
  • 35
    • 77649287391 scopus 로고    scopus 로고
    • Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis
    • Arantes V., Saddler J.N. Access to cellulose limits the efficiency of enzymatic hydrolysis: the role of amorphogenesis. Biotechnol. Biofuels 2010, 3:4.
    • (2010) Biotechnol. Biofuels , vol.3 , pp. 4
    • Arantes, V.1    Saddler, J.N.2
  • 36
    • 84865740281 scopus 로고    scopus 로고
    • Use of substructure-specific carbohydrate binding modules to track changes in cellulose accessibility and surface morphology during the amorphogenesis step of enzymatic hydrolysis
    • Gourlay K., Arantes V., Saddler J.N. Use of substructure-specific carbohydrate binding modules to track changes in cellulose accessibility and surface morphology during the amorphogenesis step of enzymatic hydrolysis. Biotechnol. Biofuels 2012, 5:51.
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 51
    • Gourlay, K.1    Arantes, V.2    Saddler, J.N.3
  • 37
    • 0042858149 scopus 로고    scopus 로고
    • Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei
    • Foreman P.K., et al. Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei. J. Biol. Chem. 2003, 278:31988-31997.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31988-31997
    • Foreman, P.K.1
  • 38
    • 84907573382 scopus 로고    scopus 로고
    • Engineering Aspergillus oryzae A-4 through the chromosomal insertion of foreign cellulase expression cassette to improve conversion of cellulosic biomass into lipids
    • Lin H., et al. Engineering Aspergillus oryzae A-4 through the chromosomal insertion of foreign cellulase expression cassette to improve conversion of cellulosic biomass into lipids. PLoS ONE 2014, 9:e108442.
    • (2014) PLoS ONE , vol.9 , pp. e108442
    • Lin, H.1
  • 39
    • 84874475326 scopus 로고    scopus 로고
    • Efficient conversion of biomass into lipids by using the simultaneous saccharification and enhanced lipid production process
    • Gong Z., et al. Efficient conversion of biomass into lipids by using the simultaneous saccharification and enhanced lipid production process. Biotechnol. Biofuels 2013, 6:36.
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 36
    • Gong, Z.1
  • 40
    • 0008905774 scopus 로고
    • Metabolism of lignin related aromatic compounds by Aspergillus japonicus
    • Milstein O., et al. Metabolism of lignin related aromatic compounds by Aspergillus japonicus. Arch. Microbiol. 1983, 135:147-154.
    • (1983) Arch. Microbiol. , vol.135 , pp. 147-154
    • Milstein, O.1
  • 41
    • 84920253135 scopus 로고    scopus 로고
    • Genome shuffling of Aspergillus glaucus HGZ-2 for enhanced cellulase production
    • Zhao Y., Jiang C., Yu H., Fang F., Yang J. Genome shuffling of Aspergillus glaucus HGZ-2 for enhanced cellulase production. Appl. Biochem. Biotechnol. 2014, 174:1246-1259.
    • (2014) Appl. Biochem. Biotechnol. , vol.174 , pp. 1246-1259
    • Zhao, Y.1    Jiang, C.2    Yu, H.3    Fang, F.4    Yang, J.5
  • 43
    • 84861162432 scopus 로고    scopus 로고
    • Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger
    • Zhang S.B., Pei X.Q., Wu Z.L. Multiple amino acid substitutions significantly improve the thermostability of feruloyl esterase A from Aspergillus niger. Bioresour. Technol. 2012, 117:140-147.
    • (2012) Bioresour. Technol. , vol.117 , pp. 140-147
    • Zhang, S.B.1    Pei, X.Q.2    Wu, Z.L.3
  • 44
    • 84860437176 scopus 로고    scopus 로고
    • Fusarium verticillioides secretome as a source of auxiliary enzymes to enhance saccharification of wheat straw
    • Ravalason H., et al. Fusarium verticillioides secretome as a source of auxiliary enzymes to enhance saccharification of wheat straw. Bioresour. Technol. 2012, 114:589-596.
    • (2012) Bioresour. Technol. , vol.114 , pp. 589-596
    • Ravalason, H.1
  • 45
    • 34748923122 scopus 로고    scopus 로고
    • Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum
    • Paper J.M., Scott-Craig J.S., Adhikari N.D., Cuomo C.A., Walton J.D. Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum. Proteomics 2007, 7:3171-3183.
    • (2007) Proteomics , vol.7 , pp. 3171-3183
    • Paper, J.M.1    Scott-Craig, J.S.2    Adhikari, N.D.3    Cuomo, C.A.4    Walton, J.D.5
  • 46
    • 84859512402 scopus 로고    scopus 로고
    • The predicted secretome of the plant pathogenic fungus Fusarium graminearum: a refined comparative analysis
    • Brown N.A., Antoniw J., Hammond-Kosack K.E. The predicted secretome of the plant pathogenic fungus Fusarium graminearum: a refined comparative analysis. PLoS ONE 2012, 7:e33731.
    • (2012) PLoS ONE , vol.7 , pp. e33731
    • Brown, N.A.1    Antoniw, J.2    Hammond-Kosack, K.E.3
  • 47
    • 84872042007 scopus 로고    scopus 로고
    • The chromatin code of fungal secondary metabolite gene clusters
    • Gacek A., Strauss J. The chromatin code of fungal secondary metabolite gene clusters. Appl. Microbiol. Biotechnol. 2012, 95:1389-1404.
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , pp. 1389-1404
    • Gacek, A.1    Strauss, J.2
  • 49
    • 60549116487 scopus 로고    scopus 로고
    • Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion
    • Martinez D., et al. Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion. Proc. Natl. Acad. Sci. USA 2009, 106:1954-1959.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1954-1959
    • Martinez, D.1
  • 50
    • 83055188828 scopus 로고    scopus 로고
    • Proteomic and functional analysis of the cellulase system expressed by Postia placenta during brown rot of solid wood
    • Ryu J.S., et al. Proteomic and functional analysis of the cellulase system expressed by Postia placenta during brown rot of solid wood. Appl. Environ. Microbiol. 2011, 77:7933-7941.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7933-7941
    • Ryu, J.S.1
  • 51
    • 0030747617 scopus 로고    scopus 로고
    • The effect of oxidative pretreatment on cellulose degradation by Poria placenta and Trichoderma reesei cellulases
    • Rättö M., Ritschkoff A.C., Viikari L. The effect of oxidative pretreatment on cellulose degradation by Poria placenta and Trichoderma reesei cellulases. Appl. Microbiol. Biotechnol. 1997, 48:53-57.
    • (1997) Appl. Microbiol. Biotechnol. , vol.48 , pp. 53-57
    • Rättö, M.1    Ritschkoff, A.C.2    Viikari, L.3
  • 52
    • 33745090845 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase - a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
    • Zamocky M., et al. Cellobiose dehydrogenase - a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi. Curr. Protein Pept. Sci. 2006, 7:255-280.
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 255-280
    • Zamocky, M.1
  • 53
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • Langston J.A., et al. Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. Appl. Environ. Microbiol. 2011, 77:7007-7015.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7007-7015
    • Langston, J.A.1
  • 54
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper dependent polysaccharide monooxygenase potentiate fungal cellulose
    • Phillips C., Beeson W., Cate J., Marletta M. Cellobiose dehydrogenase and a copper dependent polysaccharide monooxygenase potentiate fungal cellulose. ACS Chem. Biol. 2011, 6:1399-1406.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1399-1406
    • Phillips, C.1    Beeson, W.2    Cate, J.3    Marletta, M.4
  • 56
    • 84875193804 scopus 로고    scopus 로고
    • Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
    • Levasseur A., Drula E., Lombard V., Coutinho P.M., Henrissat B. Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes. Biotechnol. Biofuels 2013, 6:41.
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 41
    • Levasseur, A.1    Drula, E.2    Lombard, V.3    Coutinho, P.M.4    Henrissat, B.5
  • 57
    • 84860911279 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of appressorium development by the rice blast fungus Magnaporthe oryzae
    • Soanes D.M., Chakrabarti A., Paszkiewicz K.H., Dawe A.L., Talbot N.J. Genome-wide transcriptional profiling of appressorium development by the rice blast fungus Magnaporthe oryzae. PLoS Pathog. 2012, 8:e1002514.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002514
    • Soanes, D.M.1    Chakrabarti, A.2    Paszkiewicz, K.H.3    Dawe, A.L.4    Talbot, N.J.5
  • 58
    • 84865188551 scopus 로고    scopus 로고
    • The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei
    • Seiboth B., et al. The putative protein methyltransferase LAE1 controls cellulase gene expression in Trichoderma reesei. Mol. Microbiol. 2012, 84:1150-1164.
    • (2012) Mol. Microbiol. , vol.84 , pp. 1150-1164
    • Seiboth, B.1
  • 59
    • 84875585919 scopus 로고    scopus 로고
    • Ethanol production from high cellulose concentration by the basidiomycete fungus Flammulina velutipes
    • Maehara T., et al. Ethanol production from high cellulose concentration by the basidiomycete fungus Flammulina velutipes. Fungal Biol. 2013, 117:220-226.
    • (2013) Fungal Biol. , vol.117 , pp. 220-226
    • Maehara, T.1
  • 60
    • 84856341952 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of lignocellulolytic enzymes by Phanerochaete chrysosporium on different lignocellulosic biomass
    • Adav S.S., Ravindran A., Sze S.K. Quantitative proteomic analysis of lignocellulolytic enzymes by Phanerochaete chrysosporium on different lignocellulosic biomass. J. Proteomics 2012, 75:1493-1504.
    • (2012) J. Proteomics , vol.75 , pp. 1493-1504
    • Adav, S.S.1    Ravindran, A.2    Sze, S.K.3
  • 61
    • 84905378257 scopus 로고    scopus 로고
    • Plant surface cues prime Ustilago maydis for biotrophic development
    • Lanver D., et al. Plant surface cues prime Ustilago maydis for biotrophic development. PLoS Pathog. 2014, 10:e1004272.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004272
    • Lanver, D.1
  • 62
    • 84911992820 scopus 로고    scopus 로고
    • The Aspergillus nidulans signalling mucin MsbA regulates starvation responses, adhesion and affects cellulase secretion in response to environmental cues
    • Brown N.A., et al. The Aspergillus nidulans signalling mucin MsbA regulates starvation responses, adhesion and affects cellulase secretion in response to environmental cues. Mol. Microbiol. 2014, 94:1103-1120.
    • (2014) Mol. Microbiol. , vol.94 , pp. 1103-1120
    • Brown, N.A.1
  • 63
    • 78651390306 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level
    • Battaglia E., et al. Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level. BMC Genomics 2011, 12:38.
    • (2011) BMC Genomics , vol.12 , pp. 38
    • Battaglia, E.1
  • 64
    • 84899490772 scopus 로고    scopus 로고
    • Genome sequence and transcriptome analyses of the thermophilic zygomycete fungus Rhizomucor miehei
    • Zhou P., et al. Genome sequence and transcriptome analyses of the thermophilic zygomycete fungus Rhizomucor miehei. BMC Genomics 2014, 15:294.
    • (2014) BMC Genomics , vol.15 , pp. 294
    • Zhou, P.1
  • 65
    • 68249097196 scopus 로고    scopus 로고
    • Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a whole-genome duplication
    • Ma L.J., et al. Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a whole-genome duplication. PLoS Genet. 2009, 5:e1000549.
    • (2009) PLoS Genet. , vol.5 , pp. e1000549
    • Ma, L.J.1
  • 66
    • 84906490873 scopus 로고    scopus 로고
    • A highly active beta-glucanase from a new strain of rumen fungus Orpinomyces sp.Y102 exhibits cellobiohydrolase and cellotriohydrolase activities
    • Chen Y.C., Chen W.T., Liu J.C., Tsai L.C., Cheng H.L. A highly active beta-glucanase from a new strain of rumen fungus Orpinomyces sp.Y102 exhibits cellobiohydrolase and cellotriohydrolase activities. Bioresour. Technol. 2014, 170:513-521.
    • (2014) Bioresour. Technol. , vol.170 , pp. 513-521
    • Chen, Y.C.1    Chen, W.T.2    Liu, J.C.3    Tsai, L.C.4    Cheng, H.L.5
  • 67
    • 84903152521 scopus 로고    scopus 로고
    • Anaerobic gut fungi: advances in isolation, culture, and cellulolytic enzyme discovery for biofuel production
    • Haitjema C.H., Solomon K.V., Henske J.K., Theodorou M.K., O'Malley M.A. Anaerobic gut fungi: advances in isolation, culture, and cellulolytic enzyme discovery for biofuel production. Biotechnol. Bioeng. 2014, 111:1471-1482.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1471-1482
    • Haitjema, C.H.1    Solomon, K.V.2    Henske, J.K.3    Theodorou, M.K.4    O'Malley, M.A.5
  • 68
    • 84906940574 scopus 로고    scopus 로고
    • Purification and characterization of a cellulolytic multienzyme complex produced by Neocallimastix patriciarum J11
    • Wang H.C., Chen Y.C., Hseu R.S. Purification and characterization of a cellulolytic multienzyme complex produced by Neocallimastix patriciarum J11. Biochem. Biophys. Res. Commun. 2014, 451:190-195.
    • (2014) Biochem. Biophys. Res. Commun. , vol.451 , pp. 190-195
    • Wang, H.C.1    Chen, Y.C.2    Hseu, R.S.3
  • 69
    • 84879675890 scopus 로고    scopus 로고
    • Cloning and characterization of a thermostable and pH-stable cellobiohydrolase from Neocallimastix patriciarum J11
    • Wang H.C., Chen Y.C., Huang C.T., Hseu R.S. Cloning and characterization of a thermostable and pH-stable cellobiohydrolase from Neocallimastix patriciarum J11. Protein Expr. Purif. 2013, 90:153-159.
    • (2013) Protein Expr. Purif. , vol.90 , pp. 153-159
    • Wang, H.C.1    Chen, Y.C.2    Huang, C.T.3    Hseu, R.S.4
  • 70
    • 84880696321 scopus 로고    scopus 로고
    • The genome of the anaerobic fungus Orpinomyces sp. strain C1A reveals the unique evolutionary history of a remarkable plant biomass degrader
    • Youssef N.H., et al. The genome of the anaerobic fungus Orpinomyces sp. strain C1A reveals the unique evolutionary history of a remarkable plant biomass degrader. Appl. Environ. Microbiol. 2013, 79:4620-4634.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 4620-4634
    • Youssef, N.H.1
  • 72
    • 84899476200 scopus 로고    scopus 로고
    • Recombinant hyperthermophilic enzyme expression in plants: a novel approach for lignocellulose digestion
    • Mir B.A., Mewalal R., Mizrachi E., Myburg A.A., Cowan D.A. Recombinant hyperthermophilic enzyme expression in plants: a novel approach for lignocellulose digestion. Trends Biotechnol. 2014, 32:281-289.
    • (2014) Trends Biotechnol. , vol.32 , pp. 281-289
    • Mir, B.A.1    Mewalal, R.2    Mizrachi, E.3    Myburg, A.A.4    Cowan, D.A.5
  • 73
    • 84899957267 scopus 로고    scopus 로고
    • Thermophilic lignocellulose deconstruction
    • Blumer-Schuette S.E., et al. Thermophilic lignocellulose deconstruction. FEMS Microbiol. Rev. 2014, 38:393-448.
    • (2014) FEMS Microbiol. Rev. , vol.38 , pp. 393-448
    • Blumer-Schuette, S.E.1
  • 74
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille C., Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 2001, 65:1-43.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 76
    • 84904905053 scopus 로고    scopus 로고
    • Genomic insights into the fungal lignocellulolytic system of Myceliophthora thermophila
    • Karnaouri A., Topakas E., Antonopoulou I., Christakopoulos P. Genomic insights into the fungal lignocellulolytic system of Myceliophthora thermophila. Front. Microbiol. 2014, 5:281.
    • (2014) Front. Microbiol. , vol.5 , pp. 281
    • Karnaouri, A.1    Topakas, E.2    Antonopoulou, I.3    Christakopoulos, P.4
  • 78
    • 50249084550 scopus 로고    scopus 로고
    • Thermoacidophilic proteins for biofuel production
    • Hess M. Thermoacidophilic proteins for biofuel production. Trends Microbiol. 2008, 16:414-419.
    • (2008) Trends Microbiol. , vol.16 , pp. 414-419
    • Hess, M.1
  • 79
    • 79960102281 scopus 로고    scopus 로고
    • Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment
    • Graham J.E., et al. Identification and characterization of a multidomain hyperthermophilic cellulase from an archaeal enrichment. Nat. Commun. 2011, 2:375.
    • (2011) Nat. Commun. , vol.2 , pp. 375
    • Graham, J.E.1
  • 81
    • 0026928601 scopus 로고
    • A theoretical analysis of cellulose product inhibition: effect of cellulase binding constant, enzyme/substrate ratio, and β-glucosidase activity on the inhibition pattern
    • Gusakov A.V., Sinitsyn A.P. A theoretical analysis of cellulose product inhibition: effect of cellulase binding constant, enzyme/substrate ratio, and β-glucosidase activity on the inhibition pattern. Biotechnol. Bioeng. 1992, 40:663-671.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 663-671
    • Gusakov, A.V.1    Sinitsyn, A.P.2
  • 82
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen S.W., Luesink E.J., Stams A.J., Zehnder A.J. Purification and characterization of an extremely thermostable beta-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 1993, 213:305-312.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.1    Luesink, E.J.2    Stams, A.J.3    Zehnder, A.J.4
  • 83
    • 84868369249 scopus 로고    scopus 로고
    • Specific fusion of β-1,4-endo-glucanase and β-1,4-glucosidase enhances cellulolytic activity and helps in channeling of intermediates
    • Adlakha N., Sawant S., Anil A., Lali A., Yazdani S.S. Specific fusion of β-1,4-endo-glucanase and β-1,4-glucosidase enhances cellulolytic activity and helps in channeling of intermediates. Appl. Environ. Microbiol. 2012, 78:7447-7454.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 7447-7454
    • Adlakha, N.1    Sawant, S.2    Anil, A.3    Lali, A.4    Yazdani, S.S.5
  • 84
    • 68349131626 scopus 로고    scopus 로고
    • The rosettazyme: a synthetic cellulosome
    • Mitsuzawa S., et al. The rosettazyme: a synthetic cellulosome. J. Biotechnol. 2009, 143:139-144.
    • (2009) J. Biotechnol. , vol.143 , pp. 139-144
    • Mitsuzawa, S.1
  • 85
    • 84890852394 scopus 로고    scopus 로고
    • Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA
    • Brunecky R., et al. Revealing nature's cellulase diversity: the digestion mechanism of Caldicellulosiruptor bescii CelA. Science 2013, 342:1513-1516.
    • (2013) Science , vol.342 , pp. 1513-1516
    • Brunecky, R.1
  • 87
    • 84908161496 scopus 로고    scopus 로고
    • Synergy of crude enzyme cocktail from cold-adapted Cladosporium cladosporioides Ch2-2 with commercial xylanase achieving high sugars yield at low cost
    • Ji L., et al. Synergy of crude enzyme cocktail from cold-adapted Cladosporium cladosporioides Ch2-2 with commercial xylanase achieving high sugars yield at low cost. Biotechnol. Biofuels 2014, 7:130.
    • (2014) Biotechnol. Biofuels , vol.7 , pp. 130
    • Ji, L.1
  • 88
    • 84155188952 scopus 로고    scopus 로고
    • Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications
    • Sharma A., Kawarabayasi Y., Satyanarayana T. Acidophilic bacteria and archaea: acid stable biocatalysts and their potential applications. Extremophiles 2012, 16:1-19.
    • (2012) Extremophiles , vol.16 , pp. 1-19
    • Sharma, A.1    Kawarabayasi, Y.2    Satyanarayana, T.3
  • 89
    • 84920667494 scopus 로고    scopus 로고
    • Chaophilic or chaotolerant fungi: a new category of extremophiles?
    • Zajc J., et al. Chaophilic or chaotolerant fungi: a new category of extremophiles?. Front. Microbiol. 2014, 5:708.
    • (2014) Front. Microbiol. , vol.5 , pp. 708
    • Zajc, J.1
  • 90
    • 84878577088 scopus 로고    scopus 로고
    • Characterization of salt-adapted secreted lignocellulolytic enzymes from the mangrove fungus Pestalotiopsis sp
    • Arfi Y., et al. Characterization of salt-adapted secreted lignocellulolytic enzymes from the mangrove fungus Pestalotiopsis sp. Nat. Commun. 2013, 4:1810.
    • (2013) Nat. Commun. , vol.4 , pp. 1810
    • Arfi, Y.1
  • 91
    • 84881261973 scopus 로고    scopus 로고
    • Specific jarosite biomineralization by Purpureocillium lilacinum, an acidophilic fungi isolated from Río Tinto
    • Oggerin M., et al. Specific jarosite biomineralization by Purpureocillium lilacinum, an acidophilic fungi isolated from Río Tinto. Environ. Microbiol. 2013, 15:2228-2237.
    • (2013) Environ. Microbiol. , vol.15 , pp. 2228-2237
    • Oggerin, M.1
  • 93
    • 84870952001 scopus 로고    scopus 로고
    • Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production
    • Singhania R.R., Patel A.K., Sukumaran R.K., Larroche C., Pandey A. Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production. Bioresour. Technol. 2013, 127:500-507.
    • (2013) Bioresour. Technol. , vol.127 , pp. 500-507
    • Singhania, R.R.1    Patel, A.K.2    Sukumaran, R.K.3    Larroche, C.4    Pandey, A.5
  • 94
    • 84894458820 scopus 로고    scopus 로고
    • Two promising alkaline β-glucosidases isolated by functional metagenomics from agricultural soil including one showing high tolerance towards harsh detergents, oxidants and glucose
    • Biver S., Stroobants A., Portetelle D., Vandenbol M. Two promising alkaline β-glucosidases isolated by functional metagenomics from agricultural soil including one showing high tolerance towards harsh detergents, oxidants and glucose. J. Ind. Microbiol. Biotechnol. 2014, 41:479-488.
    • (2014) J. Ind. Microbiol. Biotechnol. , vol.41 , pp. 479-488
    • Biver, S.1    Stroobants, A.2    Portetelle, D.3    Vandenbol, M.4
  • 97
    • 77950888128 scopus 로고    scopus 로고
    • The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation to the deep-sea environment and ecological role in sedimentary organic nitrogen degradation
    • Qin Q.L., et al. The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation to the deep-sea environment and ecological role in sedimentary organic nitrogen degradation. BMC Genomics 2010, 11:247.
    • (2010) BMC Genomics , vol.11 , pp. 247
    • Qin, Q.L.1
  • 98
    • 77953590873 scopus 로고    scopus 로고
    • Complete genome sequence and comparative analysis of Shewanella violacea, a psychrophilic and piezophilic bacterium from deep sea floor sediments
    • Aono E., et al. Complete genome sequence and comparative analysis of Shewanella violacea, a psychrophilic and piezophilic bacterium from deep sea floor sediments. Mol. Biosyst. 2010, 6:1216-1226.
    • (2010) Mol. Biosyst. , vol.6 , pp. 1216-1226
    • Aono, E.1
  • 99
    • 67649603168 scopus 로고    scopus 로고
    • Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis
    • Mardanov A.V., et al. Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis. Appl. Environ. Microbiol. 2009, 75:4580-4588.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 4580-4588
    • Mardanov, A.V.1
  • 100
    • 84876690276 scopus 로고    scopus 로고
    • Characteristics of thermostable endo-xylanase and β-xylosidase of the extremely thermophilic bacterium Geobacillus thermodenitrificans TSAA1 and its applicability in generating xylooligosaccharides and xylose from agro-residues
    • Anand A., Kumar V., Satyanarayana T. Characteristics of thermostable endo-xylanase and β-xylosidase of the extremely thermophilic bacterium Geobacillus thermodenitrificans TSAA1 and its applicability in generating xylooligosaccharides and xylose from agro-residues. Extremophiles 2013, 17:357-366.
    • (2013) Extremophiles , vol.17 , pp. 357-366
    • Anand, A.1    Kumar, V.2    Satyanarayana, T.3
  • 101
    • 84998829052 scopus 로고    scopus 로고
    • Draft genome sequence of the polyextremophilic Halorubrum sp. strain AJ67, isolated from hyperarsenic lakes in the Argentinian Puna
    • Burguener G.F., et al. Draft genome sequence of the polyextremophilic Halorubrum sp. strain AJ67, isolated from hyperarsenic lakes in the Argentinian Puna. Genome Announc. 2014, 2:e01096-13.
    • (2014) Genome Announc. , vol.2 , pp. e01096-e01113
    • Burguener, G.F.1
  • 102
    • 67549125140 scopus 로고    scopus 로고
    • Peroxicretion: a novel secretion pathway in the eukaryotic cell
    • Sagt C.M., et al. Peroxicretion: a novel secretion pathway in the eukaryotic cell. BMC Biotechnol. 2009, 9:48.
    • (2009) BMC Biotechnol. , vol.9 , pp. 48
    • Sagt, C.M.1
  • 103
    • 84897643536 scopus 로고    scopus 로고
    • Making recombinant proteins in filamentous fungi- are we expecting too much?
    • Nevalainen H., Peterson R. Making recombinant proteins in filamentous fungi- are we expecting too much?. Front. Microbiol. 2014, 5:75.
    • (2014) Front. Microbiol. , vol.5 , pp. 75
    • Nevalainen, H.1    Peterson, R.2
  • 104
    • 84894028767 scopus 로고    scopus 로고
    • Symbiotic digestion of lignocellulose in termite guts
    • Brune A. Symbiotic digestion of lignocellulose in termite guts. Nat. Rev. Microbiol. 2014, 12:168-180.
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 168-180
    • Brune, A.1
  • 105
    • 84903266916 scopus 로고    scopus 로고
    • Identification of novel biomass-degrading enzymes from genomic dark matter: populating genomic sequence space with functional annotation
    • Piao H., et al. Identification of novel biomass-degrading enzymes from genomic dark matter: populating genomic sequence space with functional annotation. Biotechnol. Bioeng. 2014, 111:1550-1565.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1550-1565
    • Piao, H.1
  • 106
    • 84869476196 scopus 로고    scopus 로고
    • Engineering a thermoregulated intein-modified xylanase into maize for consolidated lignocellulosic biomass processing
    • Shen B., et al. Engineering a thermoregulated intein-modified xylanase into maize for consolidated lignocellulosic biomass processing. Nat. Biotechnol. 2012, 30:1131-1136.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1131-1136
    • Shen, B.1
  • 107
    • 84902590153 scopus 로고    scopus 로고
    • Direct conversion of plant biomass to ethanol by engineered Caldicellulosiruptor bescii
    • Chung D., Cha M., Guss A.M., Westpheling J. Direct conversion of plant biomass to ethanol by engineered Caldicellulosiruptor bescii. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:8931-8936.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 8931-8936
    • Chung, D.1    Cha, M.2    Guss, A.M.3    Westpheling, J.4
  • 108
    • 84870500566 scopus 로고    scopus 로고
    • A diverse set of family 48 bacterial glycoside hydrolase cellulases created by structure-guided recombination
    • Smith M.A., et al. A diverse set of family 48 bacterial glycoside hydrolase cellulases created by structure-guided recombination. FEBS J. 2012, 279:4453-4465.
    • (2012) FEBS J. , vol.279 , pp. 4453-4465
    • Smith, M.A.1
  • 109
    • 84870201937 scopus 로고    scopus 로고
    • Highly thermostable fungal cellobiohydrolase I (Cel7A) engineered using predictive methods
    • Komor R.S., Romero P.A., Xie C.B., Arnold F.H. Highly thermostable fungal cellobiohydrolase I (Cel7A) engineered using predictive methods. Protein Eng. Des. Sel. 2012, 25:827-833.
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 827-833
    • Komor, R.S.1    Romero, P.A.2    Xie, C.B.3    Arnold, F.H.4
  • 110
    • 79955757259 scopus 로고    scopus 로고
    • Thermophilic laccase from xerophyte species Opuntia vulgaris
    • Kumar G.N., Srikumar K. Thermophilic laccase from xerophyte species Opuntia vulgaris. Biomed. Chromatogr. 2011, 25:707-711.
    • (2011) Biomed. Chromatogr. , vol.25 , pp. 707-711
    • Kumar, G.N.1    Srikumar, K.2
  • 111
    • 84924302954 scopus 로고    scopus 로고
    • Bringing functions together with fusion enzymes-from nature's inventions to biotechnological applications
    • Elleuche S. Bringing functions together with fusion enzymes-from nature's inventions to biotechnological applications. Appl. Microbiol. Biotechnol. 2015, 99:1545-1556.
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 1545-1556
    • Elleuche, S.1
  • 112
    • 84924283158 scopus 로고    scopus 로고
    • Generating bifunctional fusion enzymes composed of heat-active endo-glucanase (Cel5A) and endo-xylanase (XylT)
    • Rizk M., Elleuche S., Antranikian G. Generating bifunctional fusion enzymes composed of heat-active endo-glucanase (Cel5A) and endo-xylanase (XylT). Biotechnol. Lett. 2015, 37:139-145.
    • (2015) Biotechnol. Lett. , vol.37 , pp. 139-145
    • Rizk, M.1    Elleuche, S.2    Antranikian, G.3
  • 113
    • 78651473740 scopus 로고    scopus 로고
    • Construction and characterization of different fusion proteins between cellulases and β-glucosidase to improve glucose production and thermostability
    • Lee H.L., Chang C.K., Teng K.H., Liang P.H. Construction and characterization of different fusion proteins between cellulases and β-glucosidase to improve glucose production and thermostability. Bioresour. Technol. 2011, 102:3973-3976.
    • (2011) Bioresour. Technol. , vol.102 , pp. 3973-3976
    • Lee, H.L.1    Chang, C.K.2    Teng, K.H.3    Liang, P.H.4
  • 114
    • 74349084291 scopus 로고    scopus 로고
    • Commercializing lignocellulosic bioethanol: technology bottlenecks and possible remedies
    • Banerjee S., et al. Commercializing lignocellulosic bioethanol: technology bottlenecks and possible remedies. Biofuels Bioprod. Biorefining 2010, 4:77-93.
    • (2010) Biofuels Bioprod. Biorefining , vol.4 , pp. 77-93
    • Banerjee, S.1
  • 115
    • 84865224370 scopus 로고    scopus 로고
    • Endo-exo synergism in cellulose hydrolysis revisited
    • Jalak J., Kurašin M., Teugjas H., Väljamäe P. Endo-exo synergism in cellulose hydrolysis revisited. J. Biol. Chem. 2012, 287:28802-28815.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28802-28815
    • Jalak, J.1    Kurašin, M.2    Teugjas, H.3    Väljamäe, P.4
  • 116
    • 84917738216 scopus 로고    scopus 로고
    • Proximity effect between cellulose-degrading enzymes displayed on the yeast cell surface
    • Bae J., Kuroda K., Ueda M. Proximity effect between cellulose-degrading enzymes displayed on the yeast cell surface. Appl. Environ. Microbiol. 2015, 81:59-66.
    • (2015) Appl. Environ. Microbiol. , vol.81 , pp. 59-66
    • Bae, J.1    Kuroda, K.2    Ueda, M.3
  • 117
    • 84921271251 scopus 로고    scopus 로고
    • Metagenomics of un-culturable bacteria in cow rumen: construction of cel9E-xyn10A fusion gene by site-directed mutagenesis
    • Kang Y.M., Kim M.K., An J.M., Haque M.A., Cho K.M. Metagenomics of un-culturable bacteria in cow rumen: construction of cel9E-xyn10A fusion gene by site-directed mutagenesis. J. Mol. Catal. B: Enzym. 2015, 114:29-38.
    • (2015) J. Mol. Catal. B: Enzym. , vol.114 , pp. 29-38
    • Kang, Y.M.1    Kim, M.K.2    An, J.M.3    Haque, M.A.4    Cho, K.M.5
  • 118
    • 84918799089 scopus 로고    scopus 로고
    • Engineered thermostable fungal cellulases exhibit efficient synergistic cellulose hydrolysis at elevated temperatures
    • Trudeau D.L., Lee T.M., Arnold F.H. Engineered thermostable fungal cellulases exhibit efficient synergistic cellulose hydrolysis at elevated temperatures. Biotechnol. Bioeng. 2014, 111:2390-2397.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 2390-2397
    • Trudeau, D.L.1    Lee, T.M.2    Arnold, F.H.3
  • 119
    • 84864618029 scopus 로고    scopus 로고
    • Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop
    • Cheng Y.S., et al. Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop. Appl. Microbiol. Biotechnol. 2012, 95:661-669.
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , pp. 661-669
    • Cheng, Y.S.1
  • 120
    • 84859922225 scopus 로고    scopus 로고
    • Rationally selected single-site mutants of the Thermoascus aurantiacus endo-glucanase increase hydrolytic activity on cellulosic substrates
    • Srikrishnan S., Randall A., Baldi P., Da Silva N.A. Rationally selected single-site mutants of the Thermoascus aurantiacus endo-glucanase increase hydrolytic activity on cellulosic substrates. Biotechnol. Bioeng. 2012, 109:1595-1599.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1595-1599
    • Srikrishnan, S.1    Randall, A.2    Baldi, P.3    Da Silva, N.A.4
  • 122
    • 84901262630 scopus 로고    scopus 로고
    • Immobilization of cellulase mixtures on magnetic particles for hydrolysis of lignocellulose and ease of recycling
    • Alftrén J., Hobley T.J. Immobilization of cellulase mixtures on magnetic particles for hydrolysis of lignocellulose and ease of recycling. Biomass Bioenergy 2014, 65:72-78.
    • (2014) Biomass Bioenergy , vol.65 , pp. 72-78
    • Alftrén, J.1    Hobley, T.J.2
  • 123
    • 0025046786 scopus 로고
    • Application of a magnetic immobilized β-glucosidase in the enzymatic saccharification of steam-exploded lignocellulosic residues
    • Dekker R.F.H. Application of a magnetic immobilized β-glucosidase in the enzymatic saccharification of steam-exploded lignocellulosic residues. Appl. Biochem. Biotechnol. 1990, 23:25-39.
    • (1990) Appl. Biochem. Biotechnol. , vol.23 , pp. 25-39
    • Dekker, R.F.H.1
  • 124
    • 84883684127 scopus 로고    scopus 로고
    • Covalent immobilization of β-glucosidase on magnetic particles for lignocellulose hydrolysis
    • Alftrén J., Hobley T.J. Covalent immobilization of β-glucosidase on magnetic particles for lignocellulose hydrolysis. Appl. Biochem. Biotechnol. 2013, 169:2076-2087.
    • (2013) Appl. Biochem. Biotechnol. , vol.169 , pp. 2076-2087
    • Alftrén, J.1    Hobley, T.J.2
  • 125
    • 77954459285 scopus 로고    scopus 로고
    • An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases
    • Murphy L., Baumann M.J., Borch K., Sweeney M., Westh P. An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases. Anal. Biochem. 2010, 404:140-148.
    • (2010) Anal. Biochem. , vol.404 , pp. 140-148
    • Murphy, L.1    Baumann, M.J.2    Borch, K.3    Sweeney, M.4    Westh, P.5
  • 126
    • 78651363174 scopus 로고    scopus 로고
    • Advantages of isothermal titration calorimetry for xylanase kinetics in comparison to chemical-reducing-end assays
    • Baumann M.J., et al. Advantages of isothermal titration calorimetry for xylanase kinetics in comparison to chemical-reducing-end assays. Anal. Biochem. 2011, 410:19-26.
    • (2011) Anal. Biochem. , vol.410 , pp. 19-26
    • Baumann, M.J.1


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