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Volumn 7, Issue 1, 2014, Pages

Fast solubilization of recalcitrant cellulosic biomass by the basidiomycete fungus Laetisaria arvalis involves successive secretion of oxidative and hydrolytic enzymes

Author keywords

Bioenergy; Biorefinery; Carbohydrate active enzymes; Cellulose; Filamentous fungi; Lytic polysaccharide monooxygenase (LPMO)

Indexed keywords

BIO-ENERGY; BIOREFINERIES; CELLULOSIC BIOMASS; FILAMENTOUS FUNGI; HYDROLYTIC ENZYME; MONOOXYGENASES;

EID: 84907937195     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/s13068-014-0143-5     Document Type: Article
Times cited : (56)

References (50)
  • 3
    • 84855228527 scopus 로고    scopus 로고
    • Trichoderma reesei RUT-C30 - Thirty years of strain improvement
    • Trichoderma reesei RUT-C30-thirty years of strain improvement. R Peterson, H Nevalainen, Microbiology 2012 158 58 68 10.1099/mic.0.054031-0
    • (2012) Microbiology , vol.158 , pp. 58-68
    • Peterson, R.1    Nevalainen, H.2
  • 6
    • 77957727454 scopus 로고    scopus 로고
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
    • An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. G Vaaje-Kolstad, B Westereng, SJ Horn, Z Liu, H Zhai, M Sørlie, VG Eijsink, Science 2010 330 219 222 10.1126/science.1192231
    • (2010) Science , vol.330 , pp. 219-222
    • Vaaje-Kolstad, G.1    Westereng, B.2    Horn, S.J.3    Liu, Z.4    Zhai, H.5    Sørlie, M.6    Eijsink, V.G.7
  • 7
    • 0023478845 scopus 로고
    • Enzymatic 'combustion': The microbial degradation of lignin
    • Enzymatic 'combustion': the microbial degradation of lignin. TK Kirk, RL Farrell, Annu Rev Microbiol 1987 41 465 505 10.1146/annurev.mi.41.100187.002341
    • (1987) Annu Rev Microbiol , vol.41 , pp. 465-505
    • Kirk, T.K.1    Farrell, R.L.2
  • 9
    • 44849095141 scopus 로고    scopus 로고
    • Evidence for cleavage of lignin by a brown rot basidiomycete
    • Evidence for cleavage of lignin by a brown rot basidiomycete. DJ Yelle, J Ralph, F Lu, KE Hammel, Environ Microbiol 2008 10 1844 1849 10.1111/j.1462-2920.2008.01605.x
    • (2008) Environ Microbiol , vol.10 , pp. 1844-1849
    • Yelle, D.J.1    Ralph, J.2    Lu, F.3    Hammel, K.E.4
  • 10
    • 78650763649 scopus 로고    scopus 로고
    • Selective lignin and polysaccharide removal in natural fungal decay of wood as evidenced by in situ structural analyses
    • Selective lignin and polysaccharide removal in natural fungal decay of wood as evidenced by in situ structural analyses. AT Martinez, J Rencoret, L Nieto, J Jiménez-Barbero, A Gutiérrez, JC del Río, Environ Microbiol 2011 13 96 107 10.1111/j.1462-2920.2010.02312.x
    • (2011) Environ Microbiol , vol.13 , pp. 96-107
    • Martinez, A.T.1    Rencoret, J.2    Nieto, L.3    Jiménez-Barbero, J.4    Gutiérrez, A.5    Del Río, J.C.6
  • 11
    • 35848933507 scopus 로고    scopus 로고
    • The supramolecular structure of humic substances. A novel understanding of humus chemistry and implications in soil science
    • The supramolecular structure of humic substances. A novel understanding of humus chemistry and implications in soil science. A Piccolo, Adv Agron 2002 75 57 134 10.1016/S0065-2113(02)75003-7
    • (2002) Adv Agron , vol.75 , pp. 57-134
    • Piccolo, A.1
  • 15
    • 23944444519 scopus 로고    scopus 로고
    • Ginkgo, a multivariate analysis package
    • Ginkgo, a multivariate analysis package. G Bouxin, J Veget Science 2005 16 353 359 10.1111/j.1654-1103.2005.tb02374.x
    • (2005) J Veget Science , vol.16 , pp. 353-359
    • Bouxin, G.1
  • 17
    • 84879016211 scopus 로고    scopus 로고
    • A comparative genomic analysis of the oxidative enzymes potentially involved in lignin degradation by Agaricus bisporus
    • A comparative genomic analysis of the oxidative enzymes potentially involved in lignin degradation by Agaricus bisporus. H Doddapaneni, V Subramanian, B Fu, D Cullen, Fungal Genet Biol 2013 55 22 31 10.1016/j.fgb.2013.03.004
    • (2013) Fungal Genet Biol , vol.55 , pp. 22-31
    • Doddapaneni, H.1    Subramanian, V.2    Fu, B.3    Cullen, D.4
  • 22
    • 84869205445 scopus 로고    scopus 로고
    • NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions
    • NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions. FL Aachmann, M Sorlie, G Skjak-Braek, VG Eijsink, G Vaaje-Kolstad, Proc Natl Acad Sci U S A 2012 109 18779 19784 10.1073/pnas.1208822109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 18779-19784
    • Aachmann, F.L.1    Sorlie, M.2    Skjak-Braek, G.3    Eijsink, V.G.4    Vaaje-Kolstad, G.5
  • 23
    • 84885472701 scopus 로고    scopus 로고
    • Recent insights into copper-containing lytic polysaccharide mono-oxygenases
    • Recent insights into copper-containing lytic polysaccharide mono-oxygenases. GR Hemsworth, GJ Davies, PH Walton, Curr Opin Struct Biol 2013 23 660 668 10.1016/j.sbi.2013.05.006
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 660-668
    • Hemsworth, G.R.1    Davies, G.J.2    Walton, P.H.3
  • 25
    • 42149110897 scopus 로고    scopus 로고
    • Degradation of cellulose by basidiomycetous fungi
    • Degradation of cellulose by basidiomycetous fungi. P Baldrian, V Valásková FEMS Microbiol Rev 2008 32 501 521 10.1111/j.1574-6976.2008.00106.x
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 501-521
    • Baldrian, P.1    Valásková, V.2
  • 27
    • 84896533592 scopus 로고    scopus 로고
    • Comparative analysis of secretomes in basidiomycete fungi
    • Comparative analysis of secretomes in basidiomycete fungi. M Alfaro, JA Oguiza, L Ramírez, AG Pisabarro, J Proteomics 2014 102C 28 43 10.1016/j.jprot.2014.03.001
    • (2014) J Proteomics , vol.102 , pp. 28-43
    • Alfaro, M.1    Oguiza, J.A.2    Ramírez, L.3    Pisabarro, A.G.4
  • 29
    • 79959976450 scopus 로고    scopus 로고
    • Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose
    • Effects of xylan and starch on secretome of the basidiomycete Phanerochaete chrysosporium grown on cellulose. C Hori, K Igarashi, A Katayama, M Samejima, FEMS Microbiol Lett 2011 321 14 23 10.1111/j.1574-6968.2011.02307.x
    • (2011) FEMS Microbiol Lett , vol.321 , pp. 14-23
    • Hori, C.1    Igarashi, K.2    Katayama, A.3    Samejima, M.4
  • 30
    • 0030065736 scopus 로고    scopus 로고
    • Identification of two functionally different classes of exocellulases
    • Identification of two functionally different classes of exocellulases. BK Barr, YL Hsieh, B Ganem, DB Wilson, Biochemistry 1996 35 586 592 10.1021/bi9520388
    • (1996) Biochemistry , vol.35 , pp. 586-592
    • Barr, B.K.1    Hsieh, Y.L.2    Ganem, B.3    Wilson, D.B.4
  • 31
    • 84897094000 scopus 로고    scopus 로고
    • Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose
    • Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose. A Nakamura, H Watanabe, T Ishida, T Uchihashi, M Wada, T Ando, K Igarashi, M Samejima, J Am Chem Soc 2014 136 4584 4592 10.1021/ja4119994
    • (2014) J Am Chem Soc , vol.136 , pp. 4584-4592
    • Nakamura, A.1    Watanabe, H.2    Ishida, T.3    Uchihashi, T.4    Wada, M.5    Ando, T.6    Igarashi, K.7    Samejima, M.8
  • 32
    • 70749129072 scopus 로고    scopus 로고
    • The minimal enzyme cocktail concept for biomass processing
    • The minimal enzyme cocktail concept for biomass processing. AS Meyer, L Rosgaard, HR Sørensen, J Cereal Sci 2009 50 337 344 10.1016/j.jcs.2009.01.010
    • (2009) J Cereal Sci , vol.50 , pp. 337-344
    • Meyer, A.S.1    Rosgaard, L.2    Sørensen, H.R.3
  • 33
    • 0034629232 scopus 로고    scopus 로고
    • A critical review of cellobiose dehydrogenases
    • A critical review of cellobiose dehydrogenases. G Henriksson, G Johansson, G Pettersson, J Biotechnol 2000 78 93 113 10.1016/S0168-1656(00)00206-6
    • (2000) J Biotechnol , vol.78 , pp. 93-113
    • Henriksson, G.1    Johansson, G.2    Pettersson, G.3
  • 34
    • 0032053577 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase enhances Phanerochaete chrysosporium cellobiohydrolase i activity by relieving product inhibition
    • Cellobiose dehydrogenase enhances Phanerochaete chrysosporium cellobiohydrolase I activity by relieving product inhibition. K Igarashi, M Samejima, KE Eriksson, Eur J Biochem 1998 253 101 106 10.1046/j.1432-1327.1998.2530101.x
    • (1998) Eur J Biochem , vol.253 , pp. 101-106
    • Igarashi, K.1    Samejima, M.2    Eriksson, K.E.3
  • 35
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. JA Langston, T Shaghasi, E Abbate, F Xu, E Vlasenko, MD Sweeney, Appl Environ Microbiol 2011 77 7007 7015 10.1128/AEM.05815-11
    • (2011) Appl Environ Microbiol , vol.77 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6
  • 36
    • 84871874790 scopus 로고    scopus 로고
    • Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina
    • Cello-oligosaccharide oxidation reveals differences between two lytic polysaccharide monooxygenases (family GH61) from Podospora anserina. M Bey, S Zhou, L Poidevin, B Henrissat, PM Coutinho, JG Berrin, JC Sigoillot, Appl Environ Microbiol 2013 79 488 496 10.1128/AEM.02942-12
    • (2013) Appl Environ Microbiol , vol.79 , pp. 488-496
    • Bey, M.1    Zhou, S.2    Poidevin, L.3    Henrissat, B.4    Coutinho, P.M.5    Berrin, J.G.6    Sigoillot, J.C.7
  • 37
    • 84875193804 scopus 로고    scopus 로고
    • Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes
    • Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes. A Levasseur, E Drula, V Lombard, PM Coutinho, B Henrissat, Biotechnol Biofuels 2013 6 41 10.1186/1754-6834-6-41
    • (2013) Biotechnol Biofuels , vol.6 , pp. 41
    • Levasseur, A.1    Drula, E.2    Lombard, V.3    Coutinho, P.M.4    Henrissat, B.5
  • 39
    • 84857921108 scopus 로고    scopus 로고
    • Phanerochaete chrysosporium produces a diverse array of extracellular enzymes when grown on sorghum
    • Phanerochaete chrysosporium produces a diverse array of extracellular enzymes when grown on sorghum. A Ray, S Saykhedkar, P Ayoubi-Canaan, SD Hartson, R Prade, AJ Mort, Appl Microbiol Biotechnol 2012 93 2075 2089 10.1007/s00253-012-3907-5
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 2075-2089
    • Ray, A.1    Saykhedkar, S.2    Ayoubi-Canaan, P.3    Hartson, S.D.4    Prade, R.5    Mort, A.J.6
  • 43
    • 33747518103 scopus 로고
    • Laetisaria arvalis (Aphyllophorales, Corticiaceae): A possible biological control agent for Rhizoctonia solani and Pythium species
    • Laetisaria arvalis (Aphyllophorales, Corticiaceae): a possible biological control agent for Rhizoctonia solani and Pythium species. HH Burdsall, HC Hoch, MG Boosalis, EC Setliff, Mycologia 1980 72 728 736 10.2307/3759765
    • (1980) Mycologia , vol.72 , pp. 728-736
    • Burdsall, H.H.1    Hoch, H.C.2    Boosalis, M.G.3    Setliff, E.C.4
  • 45
    • 84872706898 scopus 로고    scopus 로고
    • Aerobic deconstruction of cellulosic biomass by an insect-associated Streptomyces
    • Aerobic deconstruction of cellulosic biomass by an insect-associated Streptomyces. TE Takasuka, AJ Book, GR Lewin, CR Currie, BG Fox, Sci Rep 2013 3 1030 10.1038/srep01030
    • (2013) Sci Rep , vol.3 , pp. 1030
    • Takasuka, T.E.1    Book, A.J.2    Lewin, G.R.3    Currie, C.R.4    Fox, B.G.5
  • 46
    • 0024039571 scopus 로고
    • Improved method of measurement of dietary fiber as non-starch polysaccharides in plant foods
    • Improved method of measurement of dietary fiber as non-starch polysaccharides in plant foods. HN Englyst, JH Cummings, J Ass Off Anal Chem 1988 71 808 814
    • (1988) J Ass off Anal Chem , vol.71 , pp. 808-814
    • Englyst, H.N.1    Cummings, J.H.2
  • 47
    • 84878577088 scopus 로고    scopus 로고
    • Characterization of salt-adapted secreted lignocellulolytic enzymes from the mangrove fungus Pestalotiopsis sp
    • Characterization of salt-adapted secreted lignocellulolytic enzymes from the mangrove fungus Pestalotiopsis sp. Y Arfi, D Chevret, B Henrissat, JG Berrin, A Levasseur, E Record, Nat Commun 2013 4 1810 10.1038/ncomms2850
    • (2013) Nat Commun , vol.4 , pp. 1810
    • Arfi, Y.1    Chevret, D.2    Henrissat, B.3    Berrin, J.G.4    Levasseur, A.5    Record, E.6
  • 49
    • 84455173789 scopus 로고    scopus 로고
    • Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes
    • Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes. M Bey, JG Berrin, L Poidevin, JC Sigoillot, Microb Cell Fact 2011 10 113 10.1186/1475-2859-10-113
    • (2011) Microb Cell Fact , vol.10 , pp. 113
    • Bey, M.1    Berrin, J.G.2    Poidevin, L.3    Sigoillot, J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.