메뉴 건너뛰기




Volumn 79, Issue 4, 2013, Pages 1316-1324

Efficient plant biomass degradation by thermophilic fungus myceliophthora heterothallica

Author keywords

[No Author keywords available]

Indexed keywords

BIOMASS DEGRADATIONS; EFFICIENT PLANTS; ENZYMATIC DEGRADATION; ENZYME MIXTURES; FERMENTABLE SUGARS; GIANT REED; HIGH-CONTENT; HYDROLYTIC ENZYME; IN-VITRO ASSAYS; MESOPHILIC; PHYSIOLOGICAL DIVERSITY; PLANT BIOMASS; PLANT POLYSACCHARIDES; PROTEIN PROFILES; SEXUAL CROSSINGS; SUSTAINABLE PRODUCTION; THERMOPHILIC FUNGUS; THERMOSTABLE ENZYMES; TRICHODERMA; WHEAT STRAWS; XYLOBIOSES; XYLOSIDASE;

EID: 84874698667     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02865-12     Document Type: Article
Times cited : (43)

References (41)
  • 2
    • 33646017710 scopus 로고    scopus 로고
    • Efficiency of new fungal cellulase systems in boosting enzymatic degradation of barley straw lignocellulose
    • Rosgaard L, Pedersen S, Cherry JR, Harris P, Meyer AS. 2006. Efficiency of new fungal cellulase systems in boosting enzymatic degradation of barley straw lignocellulose. Biotechnol. Prog. 22:493- 498.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 493-498
    • Rosgaard, L.1    Pedersen, S.2    Cherry, J.R.3    Harris, P.4    Meyer, A.S.5
  • 3
    • 0035125282 scopus 로고    scopus 로고
    • Influence of enzyme loading and physical parameters on the enzymatic hydrolysis of steam-pretreated softwood
    • Tengborg C, Galbe M, Zacchi G. 2001. Influence of enzyme loading and physical parameters on the enzymatic hydrolysis of steam-pretreated softwood. Biotechnol. Prog. 17:110 -117.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 110-117
    • Tengborg, C.1    Galbe, M.2    Zacchi, G.3
  • 5
    • 0016141237 scopus 로고
    • Stability of enzymes from thermophilic microorganisms
    • Pye EK, Wingard LB (ed), Plenum Press, Inc, New York, NY, 2
    • Doig AR. 1974. Stability of enzymes from thermophilic microorganisms, p 17-21. In Pye EK, Wingard LB (ed), Enzyme engineering, vol 2. Plenum Press, Inc, New York, NY.
    • (1974) Enzyme engineering , pp. 17-21
    • Doig, A.R.1
  • 9
    • 84874703650 scopus 로고
    • Thermostable cellulase and a method for producing the same
    • Komura I, Awao T, Yamada K. August 1978. Thermostable cellulase and a method for producing the same. U.S. patent 4,106,989.
    • (1978) U. S. patent , vol.4 , Issue.106 , pp. 989
    • Komura, I.1    Awao, T.2    August, Y.K.3
  • 11
    • 52949113865 scopus 로고    scopus 로고
    • Simultaneous production of endo-β-1,4-xylanase and branched xylooligosaccharides by Thermomyces lanuginosus
    • Puchart V, Biely P. 2008. Simultaneous production of endo-β-1,4-xylanase and branched xylooligosaccharides by Thermomyces lanuginosus. J. Biotechnol. 137:34-43.
    • (2008) J. Biotechnol. , vol.137 , pp. 34-43
    • Puchart, V.1    Biely, P.2
  • 12
    • 70349412367 scopus 로고    scopus 로고
    • Highly thermostable xylanase of the thermophilic fungus Talaromyces thermophilus: purification and characterization
    • Maalej I, Belhaj I, Masmoudi NF, Belghith H. 2009. Highly thermostable xylanase of the thermophilic fungus Talaromyces thermophilus: purification and characterization. Appl. Biochem. Biotechnol. 158:200 -212.
    • (2009) Appl. Biochem. Biotechnol. , vol.158 , pp. 200-212
    • Maalej, I.1    Belhaj, I.2    Masmoudi, N.F.3    Belghith, H.4
  • 15
    • 84867788061 scopus 로고    scopus 로고
    • Cellulases from thermophilic fungi: recent insights and biotechnological potential
    • Li DC, Li AN, Papageorgiou AC. 2011. Cellulases from thermophilic fungi: recent insights and biotechnological potential. Enzyme Res. 2011: 308730.
    • (2011) Enzyme Res. 2011 , pp. 308730
    • Li, D.C.1    Li, A.N.2    Papageorgiou, A.C.3
  • 17
    • 0026872766 scopus 로고
    • Induction and regulation of alpha-amylase synthesis in a cellulolytic thermophilic fungus Myceliophthora thermophila D14 (ATCC 48104)
    • Sadhukhan R, Roy SK, Raha SK, Manna S, Chakrabarty SL. 1992. Induction and regulation of alpha-amylase synthesis in a cellulolytic thermophilic fungus Myceliophthora thermophila D14 (ATCC 48104). Indian J. Exp. Biol. 30:482- 486.
    • (1992) Indian J. Exp. Biol. , vol.30 , pp. 482-486
    • Sadhukhan, R.1    Roy, S.K.2    Raha, S.K.3    Manna, S.4    Chakrabarty, S.L.5
  • 18
    • 79954897825 scopus 로고    scopus 로고
    • Optimal culture conditions for keratinase production by a novel thermophilic Myceliophthora thermophila strain GZUIFR-H49-1
    • Liang JD, Han YF, Zhang JW, Du W, Liang ZQ, Li ZZ. 2011. Optimal culture conditions for keratinase production by a novel thermophilic Myceliophthora thermophila strain GZUIFR-H49-1. J. Appl. Microbiol. 110:9.
    • (2011) J. Appl. Microbiol. , vol.110 , pp. 9
    • Liang, J.D.1    Han, Y.F.2    Zhang, J.W.3    Du, W.4    Liang, Z.Q.5    Li, Z.Z.6
  • 19
    • 0030838432 scopus 로고    scopus 로고
    • Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae
    • Berka RM, Schneider P, Golightly EJ, Brown SH, Madden M, Brown KM, Halkier T, Mondorf K, Xu F. 1997. Characterization of the gene encoding an extracellular laccase of Myceliophthora thermophila and analysis of the recombinant enzyme expressed in Aspergillus oryzae. Appl. Environ. Microbiol. 63:3151-3157.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3151-3157
    • Berka, R.M.1    Schneider, P.2    Golightly, E.J.3    Brown, S.H.4    Madden, M.5    Brown, K.M.6    Halkier, T.7    Mondorf, K.8    Xu, F.9
  • 21
    • 79955587227 scopus 로고    scopus 로고
    • Towards industrially feasible delignification and pitch removal by treating paper pulp with Myceliophthora thermophila laccase and a phenolic mediator
    • Babot ED, Rico A, Rencoret J, Kalum L, Lund H, Romero J, del Rio JC, Martinez AT, Gutierrez A. 2011. Towards industrially feasible delignification and pitch removal by treating paper pulp with Myceliophthora thermophila laccase and a phenolic mediator. Bioresour. Technol. 102:6717- 6722.
    • (2011) Bioresour. Technol. , vol.102 , pp. 6717-6722
    • Babot, E.D.1    Rico, A.2    Rencoret, J.3    Kalum, L.4    Lund, H.5    Romero, J.6    Del Rio, J.C.7    Martinez, A.T.8    Gutierrez, A.9
  • 22
    • 33748567153 scopus 로고    scopus 로고
    • Production of multiple xylanolytic and cellulolytic enzymes by thermophilic fungus Myceliophthora sp IMI 387099
    • Badhan AK, Chadha BS, Kaur J, Saini HS, Bhat MK. 2007. Production of multiple xylanolytic and cellulolytic enzymes by thermophilic fungus Myceliophthora sp. IMI 387099. Bioresour. Technol. 98:504 -510.
    • (2007) Bioresour. Technol. , vol.98 , pp. 504-510
    • Badhan, A.K.1    Chadha, B.S.2    Kaur, J.3    Saini, H.S.4    Bhat, M.K.5
  • 23
    • 0001583695 scopus 로고
    • Sporotrichum thermophile growth, cellulose degradation, and cellulase activity
    • Bhat KM, Maheshwari R. 1987. Sporotrichum thermophile growth, cellulose degradation, and cellulase activity. Appl. Environ. Microbiol. 53: 2175-2182.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2175-2182
    • Bhat, K.M.1    Maheshwari, R.2
  • 24
    • 0025134717 scopus 로고
    • Purification and properties of an extracellular endoglucanase from Myceliophthora thermophila D-14 (ATCC 48104)
    • Roy SK, Dey SK, Raha SK, Chakrabarty SL. 1990. Purification and properties of an extracellular endoglucanase from Myceliophthora thermophila D-14 (ATCC 48104). J. Gen. Microbiol. 136:1967-1971.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1967-1971
    • Roy, S.K.1    Dey, S.K.2    Raha, S.K.3    Chakrabarty, S.L.4
  • 28
    • 0001945906 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL. 1956. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31:3.
    • (1956) Anal. Chem. , vol.31 , pp. 3
    • Miller, G.L.1
  • 29
    • 34250417397 scopus 로고
    • Revision of thermophilic Sporotrichum species: Chrysosporium thermophilum (Apinis) comb. nov. and Chrysosporium fergusii spec. nov. equal status conidialis of Corynascus thermophilus Fergus and (Sinden) comb. nov
    • von Klopotek A. 1974. Revision of thermophilic Sporotrichum species: Chrysosporium thermophilum (Apinis) comb. nov. and Chrysosporium fergusii spec. nov. equal status conidialis of Corynascus thermophilus Fergus and (Sinden) comb. nov. Arch. Microbiol. 98:365-369.
    • (1974) Arch. Microbiol. , vol.98 , pp. 365-369
    • Von Klopotek, A.1
  • 30
    • 0017310749 scopus 로고
    • Thielavia heterothallica spec. nov., die perfekte Form von Chrysosporium thermophilum
    • Von Klopotek A. 1976. Thielavia heterothallica spec. nov., die perfekte Form von Chrysosporium thermophilum. Arch. Microbiol. 107:223.
    • (1976) Arch. Microbiol. , vol.107 , pp. 223
    • Von Klopotek, A.1
  • 33
    • 0017694236 scopus 로고
    • Preparation of mutants of Trichoderma reesei with enhanced cellulase production
    • Montenecourt BS, Eveleigh DE. 1977. Preparation of mutants of Trichoderma reesei with enhanced cellulase production. Appl. Environ. Microbiol. 34:777-782.
    • (1977) Appl. Environ. Microbiol. , vol.34 , pp. 777-782
    • Montenecourt, B.S.1    Eveleigh, D.E.2
  • 34
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries RP, Visser J. 2001. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. Rev. 65:497-522.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 497-522
    • De Vries, R.P.1    Visser, J.2
  • 36
    • 33751040643 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable intracellular betaxylosidase from the thermophilic fungus Sporotrichum thermophile
    • Katapodis P, Nerinckx W, Claeyssens M, Christakopoulos P. 2006. Purification and characterization of a thermostable intracellular betaxylosidase from the thermophilic fungus Sporotrichum thermophile. Proc. Biochem. 41:7.
    • (2006) Proc. Biochem. , vol.41 , pp. 7
    • Katapodis, P.1    Nerinckx, W.2    Claeyssens, M.3    Christakopoulos, P.4
  • 38
    • 49349086760 scopus 로고    scopus 로고
    • Heterologous expression of Aspergillus niger β-D-xylosidase (XlnD): characterization on lignocellulosic substrates
    • Selig MJ, Knoshaug EP, Decker SR, Baker JO, Himmel ME, Adney WS. 2008. Heterologous expression of Aspergillus niger β-D-xylosidase (XlnD): characterization on lignocellulosic substrates. Appl. Biochem. Biotechnol. 146:57- 68.
    • (2008) Appl. Biochem. Biotechnol. , vol.146 , pp. 57-68
    • Selig, M.J.1    Knoshaug, E.P.2    Decker, S.R.3    Baker, J.O.4    Himmel, M.E.5    Adney, W.S.6
  • 39
    • 0030934768 scopus 로고    scopus 로고
    • β-Xylosidase activity, encoded by xlnD, is essential for complete hydrolysis of xylan by Aspergillus niger but not for induction of the xylanolytic enzyme spectrum
    • van Peij NN, Brinkmann J, Vrsanska M, Visser J, de Graaff LH. 1997. β-Xylosidase activity, encoded by xlnD, is essential for complete hydrolysis of xylan by Aspergillus niger but not for induction of the xylanolytic enzyme spectrum. Eur. J. Biochem. 245:164 -173.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 164-173
    • Van Peij, N.N.1    Brinkmann, J.2    Vrsanska, M.3    Visser, J.4    De Graaff, L.H.5
  • 40
    • 72449210541 scopus 로고    scopus 로고
    • Isolation and properties of extracellular β-xylosidases from fungi Aspergillus japonicus and Trichoderma reesei
    • Semenova MV, Drachevskaya MI, Sinitsyna OA, Gusakov AV, Sinitsyn AP. 2009. Isolation and properties of extracellular β-xylosidases from fungi Aspergillus japonicus and Trichoderma reesei. Biochem. Biokhim. 74:1002-1008.
    • (2009) Biochem. Biokhim. , vol.74 , pp. 1002-1008
    • Semenova, M.V.1    Drachevskaya, M.I.2    Sinitsyna, O.A.3    Gusakov, A.V.4    Sinitsyn, A.P.5
  • 41
    • 80855143728 scopus 로고    scopus 로고
    • Engineering lower inhibitor affinities in β-D-xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145
    • Jordan DB, Wagschal K, Fan Z, Yuan L, Braker JD, Heng C. 2011. Engineering lower inhibitor affinities in β-D-xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145. J. Ind. Microbiol. Biotechnol. 38:1821-1835.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1821-1835
    • Jordan, D.B.1    Wagschal, K.2    Fan, Z.3    Yuan, L.4    Braker, J.D.5    Heng, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.