메뉴 건너뛰기




Volumn 86, Issue 5, 2011, Pages 633-641

The quest for alternatives to microbial cellulase mix production: Corn stover-produced heterologous multi-cellulases readily deconstruct lignocellulosic biomass into fermentable sugars

Author keywords

1,4 cellobiohydrolases I; AFEX; Biofuels; CBH I; Cellobiase; Corn; E1; Endo cellulase; Fermentable sugar; Maize

Indexed keywords

AFEX; CBH I; CELLOBIASE; CELLOBIOHYDROLASES; CORN; E1; ENDO-CELLULASE; FERMENTABLE SUGARS; MAIZE;

EID: 79953673859     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.2584     Document Type: Article
Times cited : (23)

References (46)
  • 1
    • 0033924229 scopus 로고    scopus 로고
    • How the deposition of cellulose microfibrils builds cell wall architecture
    • Emons AM and Mulder BM, How the deposition of cellulose microfibrils builds cell wall architecture. Trends Plant Sci 5: 35-40 (2000).
    • (2000) Trends Plant Sci , vol.5 , pp. 35-40
    • Emons, A.M.1    Mulder, B.M.2
  • 3
    • 39449092009 scopus 로고    scopus 로고
    • Feedstock genetic engineering for biofuels
    • Sticklen M, Feedstock genetic engineering for biofuels. Crop Sci 47: 2238-2248 (2007).
    • (2007) Crop Sci , vol.47 , pp. 2238-2248
    • Sticklen, M.1
  • 4
    • 77954532784 scopus 로고    scopus 로고
    • Multifaceted characterization of cell wall decomposition products formed during ammonia fiber expansion (AFEX) and dilute acid based pretreatments
    • Chundawat SP, Vismeh R, Sharma LN, Humpula JF, da Costa Sousa L, Chambliss CK et al, Multifaceted characterization of cell wall decomposition products formed during ammonia fiber expansion (AFEX) and dilute acid based pretreatments. Bioresource Technol 101: 8429-8438 (2010).
    • (2010) Bioresource Technol , vol.101 , pp. 8429-8438
    • Chundawat, S.P.1    Vismeh, R.2    Sharma, L.N.3    Humpula, J.F.4    da Costa Sousa, L.5    Chambliss, C.K.6
  • 5
    • 13544271892 scopus 로고    scopus 로고
    • Enhanced production of cellobiohydrolases in Trichoderma reesei and evaluation of the new preparations in biofinishing of cotton
    • Miettinen-Oinonen A, Paloheimo M, Lantto R and Suominen P, Enhanced production of cellobiohydrolases in Trichoderma reesei and evaluation of the new preparations in biofinishing of cotton. J Biotechnol 116: 305-317 (2005).
    • (2005) J Biotechnol , vol.116 , pp. 305-317
    • Miettinen-Oinonen, A.1    Paloheimo, M.2    Lantto, R.3    Suominen, P.4
  • 6
    • 0030562068 scopus 로고    scopus 로고
    • A sequence analysis of the beta-glucosidase sub-family B
    • Rojas A and Romeu A, A sequence analysis of the beta-glucosidase sub-family B. FEBS Lett 378: 93-97 (1996).
    • (1996) FEBS Lett , vol.378 , pp. 93-97
    • Rojas, A.1    Romeu, A.2
  • 7
    • 8844286155 scopus 로고    scopus 로고
    • Expression in Trichoderma reesei and characterisation of a thermostable family 3 beta-glucosidase from the moderately thermophilic fungus Talaromyces emersonii
    • Murray P, Aro N, Collins C, Grassick A, Penttila M, Saloheimo M et al, Expression in Trichoderma reesei and characterisation of a thermostable family 3 beta-glucosidase from the moderately thermophilic fungus Talaromyces emersonii. Protein Expr Purif 38: 248-257 (2004).
    • (2004) Protein Expr Purif , vol.38 , pp. 248-257
    • Murray, P.1    Aro, N.2    Collins, C.3    Grassick, A.4    Penttila, M.5    Saloheimo, M.6
  • 8
    • 0026539878 scopus 로고
    • The bgl1 gene encoding extracellular beta-glucosidase from Trichoderma reesei is required for rapid induction of the cellulase complex
    • Fowler T and Brown RD Jr, The bgl1 gene encoding extracellular beta-glucosidase from Trichoderma reesei is required for rapid induction of the cellulase complex. Mol Microbiol 6: 3225-3235 (1992).
    • (1992) Mol Microbiol , vol.6 , pp. 3225-3235
    • Fowler, T.1    Brown Jr, R.D.2
  • 9
    • 35148831566 scopus 로고    scopus 로고
    • Subcellular targeting is a key condition for high-level accumulation of cellulase protein in transgenic maize seed
    • Hood EE, Love R, Lane J, Bray J, Clough R, Pappu K et al, Subcellular targeting is a key condition for high-level accumulation of cellulase protein in transgenic maize seed. Plant Biotechnol J 5: 709-719 (2007).
    • (2007) Plant Biotechnol J , vol.5 , pp. 709-719
    • Hood, E.E.1    Love, R.2    Lane, J.3    Bray, J.4    Clough, R.5    Pappu, K.6
  • 10
    • 77952744343 scopus 로고    scopus 로고
    • Genetic and biotechnological approaches for biofuel crop improvement
    • Vega-Sachez ME and Ronald PC, Genetic and biotechnological approaches for biofuel crop improvement. Current Opin Biotechnol 21: 218-224 (2010).
    • (2010) Current Opin Biotechnol , vol.21 , pp. 218-224
    • Vega-Sachez, M.E.1    Ronald, P.C.2
  • 11
    • 41049111196 scopus 로고    scopus 로고
    • High-throughput microplate technique for enzymatic hydrolysis of lignocellulosic biomass
    • Chundawat SP, Balan V and Dale BE, High-throughput microplate technique for enzymatic hydrolysis of lignocellulosic biomass. Biotechnol Bioeng 99: 1281-1294 (2008).
    • (2008) Biotechnol Bioeng , vol.99 , pp. 1281-1294
    • Chundawat, S.P.1    Balan, V.2    Dale, B.E.3
  • 12
    • 33846911472 scopus 로고    scopus 로고
    • Effect of particle size based separation of milled corn stover on AFEX pretreatment and enzymatic digestibility
    • Chundawat SP, Venkatesh B and Dale BE, Effect of particle size based separation of milled corn stover on AFEX pretreatment and enzymatic digestibility. Biotechnol Bioeng 96: 219-231 (2007).
    • (2007) Biotechnol Bioeng , vol.96 , pp. 219-231
    • Chundawat, S.P.1    Venkatesh, B.2    Dale, B.E.3
  • 13
    • 84970060363 scopus 로고
    • Ultra-Thermostable cellulases from acidothermus cellulolyticus: comparison of temperature optima with previously reported cellulases
    • Tucker MP, Mohagheghi A, Grohmann K and Himmel ME, Ultra-Thermostable cellulases from acidothermus cellulolyticus: comparison of temperature optima with previously reported cellulases. Nat Biotechnol 7: 817-820 (1989).
    • (1989) Nat Biotechnol , vol.7 , pp. 817-820
    • Tucker, M.P.1    Mohagheghi, A.2    Grohmann, K.3    Himmel, M.E.4
  • 14
    • 67449164820 scopus 로고    scopus 로고
    • Green tissue-specific production of a microbial endo-cellulase in maize (Zea mays L.) endoplasmic-reticulum and mitochondria converts cellulose into fermentable sugars
    • Mei C, Park SH, Sabzikar R, Qi C and Sticklen M, Green tissue-specific production of a microbial endo-cellulase in maize (Zea mays L.) endoplasmic-reticulum and mitochondria converts cellulose into fermentable sugars. J Chem Technol Biotechnol 84: 689-696 (2008).
    • (2008) J Chem Technol Biotechnol , vol.84 , pp. 689-696
    • Mei, C.1    Park, S.H.2    Sabzikar, R.3    Qi, C.4    Sticklen, M.5
  • 15
    • 0025376570 scopus 로고
    • Isolation of an efficient actin promoter for use in rice transformation
    • McElroy D, Zhang W, Cao J and Wu R, Isolation of an efficient actin promoter for use in rice transformation. Plant Cell 2: 163-171 (1990).
    • (1990) Plant Cell , vol.2 , pp. 163-171
    • McElroy, D.1    Zhang, W.2    Cao, J.3    Wu, R.4
  • 16
    • 0031468584 scopus 로고    scopus 로고
    • Cellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including the glycosylation pattern of the core protein
    • Klarskov K, Piens K, Stahlberg J, Hoj PB, Beeumen JV and Claeyssens M, Cellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including the glycosylation pattern of the core protein. Carbohydr Res 304: 143-154 (1997).
    • (1997) Carbohydr Res , vol.304 , pp. 143-154
    • Klarskov, K.1    Piens, K.2    Stahlberg, J.3    Hoj, P.B.4    Beeumen, J.V.5    Claeyssens, M.6
  • 17
    • 79953682613 scopus 로고    scopus 로고
    • Genetic transformation of tobacco with a beta-glucosidase gene to induce constitutive systemic acquired resistance against tobacco mosaic virus. PhD Dissertation Western Michigan University, Kalamazoo, MI
    • Yao JQ, Genetic transformation of tobacco with a beta-glucosidase gene to induce constitutive systemic acquired resistance against tobacco mosaic virus. PhD Dissertation Western Michigan University, Kalamazoo, MI (2004).
    • (2004)
    • Yao, J.Q.1
  • 18
    • 0025032040 scopus 로고
    • Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a beta-glucosidase
    • Lin LL, Rumbak E, Zappe H, Thomson JA and Woods DR, Cloning, sequencing and analysis of expression of a Butyrivibrio fibrisolvens gene encoding a beta-glucosidase. J Gen Microbiol 136: 1567-1576 (1990).
    • (1990) J Gen Microbiol , vol.136 , pp. 1567-1576
    • Lin, L.L.1    Rumbak, E.2    Zappe, H.3    Thomson, J.A.4    Woods, D.R.5
  • 19
    • 0342803566 scopus 로고    scopus 로고
    • pGreen: a versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation
    • Hellens RP, Edwards EA, Leyland NR, Bean S and Mullineaux PM, pGreen: a versatile and flexible binary Ti vector for Agrobacterium-mediated plant transformation. Plant Mol Biol 42: 819-832 (2000).
    • (2000) Plant Mol Biol , vol.42 , pp. 819-832
    • Hellens, R.P.1    Edwards, E.A.2    Leyland, N.R.3    Bean, S.4    Mullineaux, P.M.5
  • 20
    • 33749496498 scopus 로고    scopus 로고
    • Expression of biologically active Acidothermus cellulolyticus endoglucanase in transgenic maize plants
    • Biswas GCG, Ransom C and Sticklen M, Expression of biologically active Acidothermus cellulolyticus endoglucanase in transgenic maize plants. Plant Sci 171: 617-623 (2006).
    • (2006) Plant Sci , vol.171 , pp. 617-623
    • Biswas, G.C.G.1    Ransom, C.2    Sticklen, M.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254 (1976).
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 73749087300 scopus 로고    scopus 로고
    • Mixture optimization of six core glycosyl hydrolases for maximizing saccharification of ammonia fiber expansion (AFEX) pretreated corn stover
    • and, YEAR).
    • Gao D, Chundawat SP, Krishnan C, Balan V and Dale BE, Mixture optimization of six core glycosyl hydrolases for maximizing saccharification of ammonia fiber expansion (AFEX) pretreated corn stover. Bioresource Technol 101: 2770-2781 (YEAR).
    • Bioresource Technol , vol.101 , pp. 2770-2781
    • Gao, D.1    Chundawat, S.P.2    Krishnan, C.3    Balan, V.4    Dale, B.E.5
  • 23
    • 0345369649 scopus 로고    scopus 로고
    • production and distribution of endoglucanase, cellobiohydrolase, and beta -glucosidase components of the cellulolytic system of Volvariella volvacea, the edible straw mushroom
    • Cai YJ, Chapman SJ, Buswell JA and Chang S-T, production and distribution of endoglucanase, cellobiohydrolase, and beta -glucosidase components of the cellulolytic system of Volvariella volvacea, the edible straw mushroom. Appl Environ Microbiol 65: 553-559 (1999).
    • (1999) Appl Environ Microbiol , vol.65 , pp. 553-559
    • Cai, Y.J.1    Chapman, S.J.2    Buswell, J.A.3    Chang, S.-T.4
  • 24
    • 17844368369 scopus 로고    scopus 로고
    • Recombinant human acid beta-glucosidase stored in tobacco seed is stable, active and taken up by human fibroblasts
    • Reggi S, Marchetti S, Patti T, De Amicis F, Cariati R, Bembi B et al, Recombinant human acid beta-glucosidase stored in tobacco seed is stable, active and taken up by human fibroblasts. Plant Mol Biology 57: 101-113 (2005).
    • (2005) Plant Mol Biology , vol.57 , pp. 101-113
    • Reggi, S.1    Marchetti, S.2    Patti, T.3    De Amicis, F.4    Cariati, R.5    Bembi, B.6
  • 25
    • 33644919973 scopus 로고    scopus 로고
    • Ectopic over-expression of the maize beta-glucosidase Zm-p60.1 perturbs cytokinin homeostasis in transgenic tobacco
    • Kiran NS, Polanska L, Fohlerova R, Mazura P, Valkova M, Smeral M et al, Ectopic over-expression of the maize beta-glucosidase Zm-p60.1 perturbs cytokinin homeostasis in transgenic tobacco. J Exp Bot 57: 985-996 (2006).
    • (2006) J Exp Bot , vol.57 , pp. 985-996
    • Kiran, N.S.1    Polanska, L.2    Fohlerova, R.3    Mazura, P.4    Valkova, M.5    Smeral, M.6
  • 26
    • 0029740205 scopus 로고    scopus 로고
    • Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose
    • Sakon J, Adney WS, Himmel ME, Thomas SR and Karplus PA, Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose. Biochemistry 35: 10648-10660 (1996).
    • (1996) Biochemistry , vol.35 , pp. 10648-10660
    • Sakon, J.1    Adney, W.S.2    Himmel, M.E.3    Thomas, S.R.4    Karplus, P.A.5
  • 27
    • 0031578802 scopus 로고    scopus 로고
    • Comparative analysis of BiP gene expression in maize endosperm
    • Wrobel RL, GR OB and Boston RS, Comparative analysis of BiP gene expression in maize endosperm. Gene 204: 105-113 (1997).
    • (1997) Gene , vol.204 , pp. 105-113
    • Wrobel, R.L.1    Gr, O.B.2    Boston, R.S.3
  • 28
    • 67650739677 scopus 로고    scopus 로고
    • Expediting the biofuels agenda via genetic manipulations of cellulosic bioenergy crops
    • Sticklen MB, Expediting the biofuels agenda via genetic manipulations of cellulosic bioenergy crops. Biofuels, Bioprod Biorefining 3: 448-455 (2009).
    • (2009) Biofuels, Bioprod Biorefining , vol.3 , pp. 448-455
    • Sticklen, M.B.1
  • 29
    • 22444438991 scopus 로고    scopus 로고
    • BiP and zein binding domains within the delta zein protein
    • Randall JJ, Sutton DW, Hanson SF and Kemp JD, BiP and zein binding domains within the delta zein protein. Planta 221: 656-666 (2005).
    • (2005) Planta , vol.221 , pp. 656-666
    • Randall, J.J.1    Sutton, D.W.2    Hanson, S.F.3    Kemp, J.D.4
  • 30
    • 47349122440 scopus 로고    scopus 로고
    • A novel function for the cellulose binding module of cellobiohydrolase I
    • Wang L, Zhang Y and Gao P, A novel function for the cellulose binding module of cellobiohydrolase I. Sci China 51: 620-629 (2008).
    • (2008) Sci China , vol.51 , pp. 620-629
    • Wang, L.1    Zhang, Y.2    Gao, P.3
  • 31
    • 0025118121 scopus 로고
    • Studies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I
    • Claeyssens M, van Tilbeurgh H, Kamerling JP, Berg J, Vrsanska M and Biely P, Studies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I. Biochem J 270: 251-256 (1990).
    • (1990) Biochem J , vol.270 , pp. 251-256
    • Claeyssens, M.1    van Tilbeurgh, H.2    Kamerling, J.P.3    Berg, J.4    Vrsanska, M.5    Biely, P.6
  • 32
    • 0024035173 scopus 로고
    • Genetic improvement of Trichoderma reesei for large scale cellulase production
    • Durand H, Clanet M and Tiraby G, Genetic improvement of Trichoderma reesei for large scale cellulase production. Enzyme Microb Technol 10: 341-346 (1988).
    • (1988) Enzyme Microb Technol , vol.10 , pp. 341-346
    • Durand, H.1    Clanet, M.2    Tiraby, G.3
  • 33
    • 0010029569 scopus 로고
    • Exoglucanases from Zea mays L. seedlings: their role in β-D-glucan hydrolysis and their potential role in extension growth
    • Huber DJ and Nevins DJ, Exoglucanases from Zea mays L. seedlings: their role in β-D-glucan hydrolysis and their potential role in extension growth. Planta 155: 467-472 (1982).
    • (1982) Planta , vol.155 , pp. 467-472
    • Huber, D.J.1    Nevins, D.J.2
  • 34
    • 0012093419 scopus 로고
    • Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings
    • Hatfield R and Nevis DJ, Purification and properties of an endoglucanase isolated from the cell walls of Zea mays seedlings. Carbohydr Res 148: 265-278 (1986).
    • (1986) Carbohydr Res , vol.148 , pp. 265-278
    • Hatfield, R.1    Nevis, D.J.2
  • 37
    • 0036006037 scopus 로고    scopus 로고
    • Plant expansins are a complex multigene family with an ancient evolutionary origin
    • Li Y, Darley CP, Ongaro V, Fleming A, Schipper O, Baldauf SL et al, Plant expansins are a complex multigene family with an ancient evolutionary origin. Plant Physiol 128: 854-864 (2002).
    • (2002) Plant Physiol , vol.128 , pp. 854-864
    • Li, Y.1    Darley, C.P.2    Ongaro, V.3    Fleming, A.4    Schipper, O.5    Baldauf, S.L.6
  • 39
    • 48549100257 scopus 로고    scopus 로고
    • Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization
    • Brotman Y, Briff E, Viterbo A and Chet I, Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization. Plant Physiology 147: 779-789 (2008).
    • (2008) Plant Physiology , vol.147 , pp. 779-789
    • Brotman, Y.1    Briff, E.2    Viterbo, A.3    Chet, I.4
  • 40
    • 0036046037 scopus 로고    scopus 로고
    • Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials
    • Saloheimo M, Paloheimo M, Hakola S, Pere J, Swanson B, Nyyssonen E et al, Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur J Biochem/FEBS 269: 4202-4211 (2002).
    • (2002) Eur J Biochem/FEBS , vol.269 , pp. 4202-4211
    • Saloheimo, M.1    Paloheimo, M.2    Hakola, S.3    Pere, J.4    Swanson, B.5    Nyyssonen, E.6
  • 41
    • 3142757398 scopus 로고    scopus 로고
    • Cellulosomes: plant-cell-wall-degrading enzyme complexes
    • Doi RH and Kosugi A, Cellulosomes: plant-cell-wall-degrading enzyme complexes. Nat Rev Microbiol 2: 541-551 (2004).
    • (2004) Nat Rev Microbiol , vol.2 , pp. 541-551
    • Doi, R.H.1    Kosugi, A.2
  • 42
    • 0031831457 scopus 로고    scopus 로고
    • Intramolecular synergism in an engineered exo-endo-1,4-beta-glucanase fusion protein
    • Riedel K and Bronnenmeier K, Intramolecular synergism in an engineered exo-endo-1, 4-beta-glucanase fusion protein. Mol Microbiol 28: 767-775 (1998).
    • (1998) Mol Microbiol , vol.28 , pp. 767-775
    • Riedel, K.1    Bronnenmeier, K.2
  • 43
    • 77950993161 scopus 로고    scopus 로고
    • Chloroplast-derived enzyme cocktails hydrolyse lignocellulosic biomass and release fermentable sugars
    • Verma D, Kanagaraj A, Jin S, Singh ND, Kolattukudy PE and Daniell H, Chloroplast-derived enzyme cocktails hydrolyse lignocellulosic biomass and release fermentable sugars. Plant Biotechnol J 8: 332-350 (2010).
    • (2010) Plant Biotechnol J , vol.8 , pp. 332-350
    • Verma, D.1    Kanagaraj, A.2    Jin, S.3    Singh, N.D.4    Kolattukudy, P.E.5    Daniell, H.6
  • 45
    • 79953692767 scopus 로고    scopus 로고
    • Is Large-scale Production of Biofuel Possible? Bioscience
    • Sticklen M, Is Large-scale Production of Biofuel Possible? Bioscience (2010).
    • (2010)
    • Sticklen, M.1
  • 46
    • 0031468584 scopus 로고    scopus 로고
    • Cellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including the glycosylation pattern of the core protein
    • Klarskov K, Piens K, Stahlberg J, Høj PB, Van Beeumen J and Claeyssens M, Cellobiohydrolase I from Trichoderma reesei: identification of an active-site nucleophile and additional information on sequence including the glycosylation pattern of the core protein. Carbohydr Res 304: 143-154 (1997).
    • (1997) Carbohydr Res , vol.304 , pp. 143-154
    • Klarskov, K.1    Piens, K.2    Stahlberg, J.3    Høj, P.B.4    Van Beeumen, J.5    Claeyssens, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.