메뉴 건너뛰기




Volumn 7, Issue MAY2016, 2016, Pages

Transgenic plant-produced hydrolytic enzymes and the potential of insect gut-derived hydrolases for biofuels

Author keywords

Biofuel; Cell wall degrading (CWD) enzyme; Enzyme targeting; Gene expression; Hydrolase; Insect cellulase; Lignocellulosic

Indexed keywords


EID: 84971432368     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2016.00675     Document Type: Review
Times cited : (19)

References (140)
  • 1
    • 43849113288 scopus 로고    scopus 로고
    • Production of a recombinant xylanase in plants and its potential for pulp biobleaching applications
    • Bae, H. J., Kim, H. J., and Kim, Y. S. (2008). Production of a recombinant xylanase in plants and its potential for pulp biobleaching applications. Bioresour. Technol. 99, 3513-3519. doi: 10.1016/j.biortech.2007.07.064
    • (2008) Bioresour. Technol , vol.99 , pp. 3513-3519
    • Bae, H.J.1    Kim, H.J.2    Kim, Y.S.3
  • 2
    • 84937022695 scopus 로고    scopus 로고
    • Insect phylogenomics
    • Behura, S. K. (2015). Insect phylogenomics. Insect Mol. Biol. 24, 403-411. doi: 10.1111/imb.12174
    • (2015) Insect Mol. Biol , vol.24 , pp. 403-411
    • Behura, S.K.1
  • 3
    • 84873119880 scopus 로고    scopus 로고
    • Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes
    • Bhalla, A., Bansal, N., Kumar, S., Bischoff, K. M., and Sani, R. K. (2013). Improved lignocellulose conversion to biofuels with thermophilic bacteria and thermostable enzymes. Bioresour. Technol. 128, 751-759. doi: 10.1016/j.biortech.2012.10.145
    • (2013) Bioresour. Technol , vol.128 , pp. 751-759
    • Bhalla, A.1    Bansal, N.2    Kumar, S.3    Bischoff, K.M.4    Sani, R.K.5
  • 4
    • 0034253208 scopus 로고    scopus 로고
    • Cellulases and related enzymes in biotechnology
    • Bhat, M. K. (2000). Cellulases and related enzymes in biotechnology. Biotechnol. Adv. 18, 355-383. doi: 10.1016/S0734-9750(00)00041-0
    • (2000) Biotechnol. Adv , vol.18 , pp. 355-383
    • Bhat, M.K.1
  • 5
    • 33749496498 scopus 로고    scopus 로고
    • Expression of biologically active Acidothermus cellulolyticus endoglucanase in transgenic maize plants
    • Biswas, G. C. G., Ransom, C., and Sticklen, M. (2006). Expression of biologically active Acidothermus cellulolyticus endoglucanase in transgenic maize plants. Plant Sci. 171, 617-623. doi: 10.1016/j.plantsci.2006.06.004
    • (2006) Plant Sci , vol.171 , pp. 617-623
    • Biswas, G.C.G.1    Ransom, C.2    Sticklen, M.3
  • 6
    • 77950985578 scopus 로고    scopus 로고
    • Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases
    • Borkhardt, B., Harholt, J., Ulvskov, P., Ahring, B. K., Jorgensen, B., and Brinch-Pedersen, H. (2010). Autohydrolysis of plant xylans by apoplastic expression of thermophilic bacterial endo-xylanases. Plant Biotechnol. J. 8, 363-374. doi: 10.1111/j.1467-7652.2010.00506.x
    • (2010) Plant Biotechnol. J , vol.8 , pp. 363-374
    • Borkhardt, B.1    Harholt, J.2    Ulvskov, P.3    Ahring, B.K.4    Jorgensen, B.5    Brinch-Pedersen, H.6
  • 7
    • 0003025148 scopus 로고
    • The effects of furfural on ethanol-production by Saccharomyces-cerevisiae in batch culture
    • Boyer, L. J., Vega, J. L., Klasson, K. T., Clausen, E. C., and Gaddy, J. L. (1992). The effects of furfural on ethanol-production by Saccharomyces-cerevisiae in batch culture. Biomass Bioenerg. 3, 41-48. doi: 10.1016/0961-9534(92)90018
    • (1992) Biomass Bioenerg , vol.3 , pp. 41-48
    • Boyer, L.J.1    Vega, J.L.2    Klasson, K.T.3    Clausen, E.C.4    Gaddy, J.L.5
  • 9
    • 84894028767 scopus 로고    scopus 로고
    • Symbiotic digestion of lignocellulose in termite guts
    • Brune, A. (2014). Symbiotic digestion of lignocellulose in termite guts. Nat. Rev. Microbiol. 12, 168-180. doi: 10.1038/nrmicro3182
    • (2014) Nat. Rev. Microbiol , vol.12 , pp. 168-180
    • Brune, A.1
  • 10
    • 78951478132 scopus 로고    scopus 로고
    • In planta expression of A. Cellulolyticus Cel5A endocellulase reduces cell wall recalcitrance in tobacco and maize
    • Brunecky, R., Selig, M. J., Vinzant, T. B., Himmel, M. E., Lee, D., Blaylock, M. J., et al. (2011). In planta expression of A. cellulolyticus Cel5A endocellulase reduces cell wall recalcitrance in tobacco and maize. Biotechnol. Biofuels 4, 1-11. doi: 10.1186/1754-6834-4-1
    • (2011) Biotechnol. Biofuels , vol.4 , pp. 1-11
    • Brunecky, R.1    Selig, M.J.2    Vinzant, T.B.3    Himmel, M.E.4    Lee, D.5    Blaylock, M.J.6
  • 11
    • 84928893009 scopus 로고    scopus 로고
    • Brachypodium distachyon and Setaria viridis: Model genetic systems for the grasses
    • Brutnell, T. P., Bennetzen, J. L., and Vogel, J. P. (2015). Brachypodium distachyon and Setaria viridis: model genetic systems for the grasses. Annu. Rev. Plant Biol. 66, 465-485. doi: 10.1146/annurev-arplant-042811-105528
    • (2015) Annu. Rev. Plant Biol , vol.66 , pp. 465-485
    • Brutnell, T.P.1    Bennetzen, J.L.2    Vogel, J.P.3
  • 13
    • 70349607350 scopus 로고    scopus 로고
    • Feruloylated arabinoxylans are oxidatively cross-linked by extracellular maize peroxidase but not by horseradish peroxidase
    • Burr, S. J., and Fry, S. C. (2009). Feruloylated arabinoxylans are oxidatively cross-linked by extracellular maize peroxidase but not by horseradish peroxidase. Mol. Plant 2, 883-892. doi: 10.1093/mp/ssp044
    • (2009) Mol. Plant , vol.2 , pp. 883-892
    • Burr, S.J.1    Fry, S.C.2
  • 14
    • 66449114749 scopus 로고    scopus 로고
    • Cellulosic biofuels
    • Carroll, A., and Somerville, C. (2009). Cellulosic biofuels. Annu. Rev. Plant Biol. 60, 165-182. doi: 10.1146/annurev.arplant.043008.092125
    • (2009) Annu. Rev. Plant Biol , vol.60 , pp. 165-182
    • Carroll, A.1    Somerville, C.2
  • 15
    • 84864802283 scopus 로고    scopus 로고
    • A novel exo-cellulase from white spotted longhorn beetle (Anoplophora malasiaca)
    • Chang, C. J., Wu, C. P., Lu, S. C., Chao, A. L., Ho, T. H., Yu, S. M., et al. (2012). A novel exo-cellulase from white spotted longhorn beetle (Anoplophora malasiaca). Insect Biochem. Mol. Bio. 42, 629-636. doi: 10.1016/j.ibmb.2012.05.002
    • (2012) Insect Biochem. Mol. Bio , vol.42 , pp. 629-636
    • Chang, C.J.1    Wu, C.P.2    Lu, S.C.3    Chao, A.L.4    Ho, T.H.5    Yu, S.M.6
  • 16
    • 83055181899 scopus 로고    scopus 로고
    • High level expression of Acidothermus cellulolyticus beta-1, 4-endoglucanase in transgenic rice enhances the hydrolysis of its straw by cultured cow gastric fluid
    • Chou, H. L., Dai, Z., Hsieh, C. W., and Ku, M. S. (2011). High level expression of Acidothermus cellulolyticus beta-1, 4-endoglucanase in transgenic rice enhances the hydrolysis of its straw by cultured cow gastric fluid. Biotechnol. Biofuels 4:58. doi: 10.1186/1754-6834-4-58
    • (2011) Biotechnol. Biofuels , vol.4 , pp. 58
    • Chou, H.L.1    Dai, Z.2    Hsieh, C.W.3    Ku, M.S.4
  • 17
    • 27644525170 scopus 로고    scopus 로고
    • Growth of the plant cell wall
    • Cosgrove, D. J. (2005). Growth of the plant cell wall. Nat. Rev. Mol. Cell Biol. 6, 850-861. doi: 10.1038/nrm1746
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 850-861
    • Cosgrove, D.J.1
  • 18
    • 0034127210 scopus 로고    scopus 로고
    • Expression of Acidothermus cellulolyticus endoglucanase E1 in transgenic tobacco: Biochemical characteristics and physiological effects
    • Dai, Z., Hooker, B. S., Anderson, D. B., and Thomas, S. R. (2000). Expression of Acidothermus cellulolyticus endoglucanase E1 in transgenic tobacco: biochemical characteristics and physiological effects. Transgenic Res. 9, 43-54. doi: 10.1023/A:1008922404834
    • (2000) Transgenic Res , vol.9 , pp. 43-54
    • Dai, Z.1    Hooker, B.S.2    Erson, D.B.3    Thomas, S.R.4
  • 19
    • 0032995899 scopus 로고    scopus 로고
    • Expression of Trichoderma reesei exo-cellobiohydrolase I in transgenic tobacco leaves and calli
    • Dai, Z., Hooker, B. S., Quesenberry, R. D., and Gao, J. (1999). Expression of Trichoderma reesei exo-cellobiohydrolase I in transgenic tobacco leaves and calli. Appl. Biochem. Biotechnol. 77-79, 689-699. doi: 10.1385/ABAB:79: 1-3:689
    • (1999) Appl. Biochem. Biotechnol , vol.77-79 , pp. 689-699
    • Dai, Z.1    Hooker, B.S.2    Quesenberry, R.D.3    Gao, J.4
  • 20
    • 27144454522 scopus 로고    scopus 로고
    • Optimization of Acidothermus cellulolyticus endoglucanase (E1) production in transgenic tobacco plants by transcriptional, post-transcription and post-translational modification
    • Dai, Z., Hooker, B. S., Quesenberry, R. D., and Thomas, S. R. (2005). Optimization of Acidothermus cellulolyticus endoglucanase (E1) production in transgenic tobacco plants by transcriptional, post-transcription and post-translational modification. Transgenic Res. 14, 627-643. doi: 10.1007/s11248-005-5695-5
    • (2005) Transgenic Res , vol.14 , pp. 627-643
    • Dai, Z.1    Hooker, B.S.2    Quesenberry, R.D.3    Thomas, S.R.4
  • 21
    • 0033781874 scopus 로고    scopus 로고
    • Improved plant-based production of E1 endoglucanase using potato: Expression optimization and tissue targeting
    • Dai, Z. Y., Hooker, B. S., Anderson, D. B., and Thomas, S. R. (2000). Improved plant-based production of E1 endoglucanase using potato: expression optimization and tissue targeting. Mol. Breeding 6, 277-285. doi: 10.1023/A:1009653011948
    • (2000) Mol. Breeding , vol.6 , pp. 277-285
    • Dai, Z.Y.1    Hooker, B.S.2    Erson, D.B.3    Thomas, S.R.4
  • 22
    • 78649796264 scopus 로고    scopus 로고
    • C4GEM, a genome-scale metabolic model to study C4 plant metabolism
    • Dal’Molin, C. G., Quek, L. E., Palfreyman, R. W., Brumbley, S. M., and Nielsen, L. K. (2010). C4GEM, a genome-scale metabolic model to study C4 plant metabolism. Plant Physiol. 154, 1871-1885. doi: 10.1104/pp.110.166488
    • (2010) Plant Physiol , vol.154 , pp. 1871-1885
    • Dal’Molin, C.G.1    Quek, L.E.2    Palfreyman, R.W.3    Brumbley, S.M.4    Nielsen, L.K.5
  • 23
    • 84955566497 scopus 로고    scopus 로고
    • Improving the utilization of lignocellulosic biomass by polysaccharide modification
    • Damm, T., Commandeur, U., Fischer, R., Usadel, B., and Klose, H. (2016). Improving the utilization of lignocellulosic biomass by polysaccharide modification. Process Biochem. 51, 288-296. doi: 10.1016/j.procbio.2015.12.003
    • (2016) Process Biochem , vol.51 , pp. 288-296
    • Damm, T.1    Commandeur, U.2    Fischer, R.3    Usadel, B.4    Klose, H.5
  • 24
    • 0001087630 scopus 로고
    • PH Gradients in Lepidopteran midgut
    • Dow, J. A. (1992). pH Gradients in Lepidopteran midgut. J. Exp. Biol. 172, 355-375.
    • (1992) J. Exp. Biol , vol.172 , pp. 355-375
    • Dow, J.A.1
  • 25
    • 77950984305 scopus 로고    scopus 로고
    • Production of multifunctional chimaeric enzymes in plants: A promising approach for degrading plant cell wall from within
    • Fan, Z., and Yuan, L. (2010). Production of multifunctional chimaeric enzymes in plants: a promising approach for degrading plant cell wall from within. Plant Biotechnol. J. 8, 308-315. doi: 10.1111/j.1467-7652.2009.00484.x
    • (2010) Plant Biotechnol. J , vol.8 , pp. 308-315
    • Fan, Z.1    Yuan, L.2
  • 26
    • 84856948838 scopus 로고    scopus 로고
    • GMP issues for recombinant plant-derived pharmaceutical proteins
    • Fischer, R., Schillberg, S., Hellwig, S., Twyman, R. M., and Drossard, J. (2012). GMP issues for recombinant plant-derived pharmaceutical proteins. Biotechnol. Adv. 30, 434-439. doi: 10.1016/j.biotechadv.2011.08.007
    • (2012) Biotechnol. Adv , vol.30 , pp. 434-439
    • Fischer, R.1    Schillberg, S.2    Hellwig, S.3    Twyman, R.M.4    Drossard, J.5
  • 29
    • 39149141561 scopus 로고    scopus 로고
    • Transgenics are imperative for biofuel crops
    • Gressel, J. (2008). Transgenics are imperative for biofuel crops. Plant Sci. 174, 246-263. doi: 10.1016/j.plantsci.2007.11.009
    • (2008) Plant Sci , vol.174 , pp. 246-263
    • Gressel, J.1
  • 30
    • 80052477745 scopus 로고    scopus 로고
    • Accumulation of recombinant cellobiohydrolase and endoglucanase in the leaves of mature transgenic sugar cane
    • Harrison, M. D., Geijskes, J., Coleman, H. D., Shand, K., Kinkema, M., Palupe, A., et al. (2011). Accumulation of recombinant cellobiohydrolase and endoglucanase in the leaves of mature transgenic sugar cane. Plant Biotechnol. J. 9, 884-896. doi: 10.1111/j.1467-7652.2011.00597.x
    • (2011) Plant Biotechnol. J , vol.9 , pp. 884-896
    • Harrison, M.D.1    Geijskes, J.2    Coleman, H.D.3    Shand, K.4    Kinkema, M.5    Palupe, A.6
  • 31
    • 84863496231 scopus 로고    scopus 로고
    • Butterfly genome reveals promiscuous exchange of mimicry adaptations among species
    • Heliconius Genome Consortium
    • Heliconius Genome Consortium (2012). Butterfly genome reveals promiscuous exchange of mimicry adaptations among species. Nature 487, 94-98. doi: 10.1038/nature11041
    • (2012) Nature , vol.487 , pp. 94-98
  • 32
    • 8344236780 scopus 로고    scopus 로고
    • Plant cell cultures for the production of recombinant proteins
    • Hellwig, S., Drossard, J., Twyman, R. M., and Fischer, R. (2004). Plant cell cultures for the production of recombinant proteins. Nat. Biotechnol. 22, 1415-1422. doi: 10.1038/nbt1027
    • (2004) Nat. Biotechnol , vol.22 , pp. 1415-1422
    • Hellwig, S.1    Drossard, J.2    Twyman, R.M.3    Fischer, R.4
  • 33
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991). A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280(Pt 2), 309-316. doi: 10.1042/bj2800309
    • (1991) Biochem. J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 34
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A. (1993). New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293(Pt 3), 781-788. doi: 10.1042/bj2930781
    • (1993) Biochem. J , vol.293 , Issue.3 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 35
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • Henrissat, B., and Bairoch, A. (1996). Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316(Pt 2), 695-696. doi: 10.1042/bj3160695
    • (1996) Biochem. J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 36
    • 0028891888 scopus 로고
    • A thermostable xylanase from Clostridium thermocellum expressed at high-levels in the apoplast of transgenic tobacco has no detrimental effects and is easily purified
    • Herbers, K., Wilke, I., and Sonnewald, U. (1995). A thermostable xylanase from Clostridium thermocellum expressed at high-levels in the apoplast of transgenic tobacco has no detrimental effects and is easily purified. Bio. Technol. 13, 63-66. doi: 10.1038/nbt0195-63
    • (1995) Bio. Technol , vol.13 , pp. 63-66
    • Herbers, K.1    Wilke, I.2    Sonnewald, U.3
  • 37
    • 77956037495 scopus 로고    scopus 로고
    • Purification and characterization of termite endogenous beta-1,4-endoglucanases produced in Aspergillus oryzae
    • Hirayama, K., Watanabe, H., Tokuda, G., Kitamoto, K., and Arioka, M. (2010). Purification and characterization of termite endogenous beta-1,4-endoglucanases produced in Aspergillus oryzae. Biosci. Biotechnol. Biochem. 74, 1680-1686. doi: 10.1271/bbb.100296
    • (2010) Biosci. Biotechnol. Biochem , vol.74 , pp. 1680-1686
    • Hirayama, K.1    Watanabe, H.2    Tokuda, G.3    Kitamoto, K.4    Arioka, M.5
  • 38
    • 83055181533 scopus 로고    scopus 로고
    • Manipulating corn germplasm to increase recombinant protein accumulation
    • Hood, E. E., Devaiah, S. P., Fake, G., Egelkrout, E., Teoh, K. T., Requesens, D. V., et al. (2012). Manipulating corn germplasm to increase recombinant protein accumulation. Plant Biotechnol. J. 10, 20-30. doi: 10.1111/j.1467-7652.2011.00627.x
    • (2012) Plant Biotechnol. J , vol.10 , pp. 20-30
    • Hood, E.E.1    Devaiah, S.P.2    Fake, G.3    Egelkrout, E.4    Teoh, K.T.5    Requesens, D.V.6
  • 39
    • 35148831566 scopus 로고    scopus 로고
    • Subcellular targeting is a key condition for high-level accumulation of cellulase protein in transgenic maize seed
    • Hood, E. E., Love, R., Lane, J., Bray, J., Clough, R., Pappu, K., et al. (2007). Subcellular targeting is a key condition for high-level accumulation of cellulase protein in transgenic maize seed. Plant Biotechnol. J. 5, 709-719. doi: 10.1111/j.1467-7652.2007.00275.x
    • (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
  • 41
    • 29344448488 scopus 로고    scopus 로고
    • Dual targeting of xylanase to chloroplasts and peroxisomes as a means to increase protein accumulation in plant cells
    • Hyunjong, B., Lee, D. S., and Hwang, I. (2006). Dual targeting of xylanase to chloroplasts and peroxisomes as a means to increase protein accumulation in plant cells. J. Exper. Bot. 57, 161-169. doi: 10.1093/jxb/erj019
    • (2006) J. Exper. Bot , vol.57 , pp. 161-169
    • Hyunjong, B.1    Lee, D.S.2    Hwang, I.3
  • 42
    • 17044412101 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cellulase gene from a symbiotic protist of the lower termite, Coptotermes formosanus
    • Inoue, T., Moriya, S., Ohkuma, M., and Kudo, T. (2005). Molecular cloning and characterization of a cellulase gene from a symbiotic protist of the lower termite, Coptotermes formosanus. Gene 349, 67-75. doi: 10.1016/j.gene.2004.11.048
    • (2005) Gene , vol.349 , pp. 67-75
    • Inoue, T.1    Moriya, S.2    Ohkuma, M.3    Kudo, T.4
  • 43
    • 77649141259 scopus 로고    scopus 로고
    • Genome sequence of the pea aphid Acyrthosiphon pisum
    • International Aphid Genomics Consortium
    • International Aphid Genomics Consortium (2010). Genome sequence of the pea aphid Acyrthosiphon pisum. PLoS Biol. 8:e1000313. doi: 10.1371/journal.pbio.1000313
    • (2010) Plos Biol , vol.8
  • 44
    • 34447093550 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of maize
    • Ishida, Y., Hiei, Y., and Komari, T. (2007). Agrobacterium-mediated transformation of maize. Nature Protoc. 2, 1614-1621. doi: 10.1038/nprot.2007.241
    • (2007) Nature Protoc , vol.2 , pp. 1614-1621
    • Ishida, Y.1    Hiei, Y.2    Komari, T.3
  • 45
    • 13444283767 scopus 로고    scopus 로고
    • Rice Annotation Database (RAD): A contig-oriented database for map-based rice genomics
    • Ito, Y., Arikawa, K., Antonio, B. A., Ohta, I., Naito, S., Mukai, Y., et al. (2005). Rice Annotation Database (RAD): a contig-oriented database for map-based rice genomics. Nucleic Acids Res. 33, D651-D655. doi: 10.1093/nar/gki083
    • (2005) Nucleic Acids Res , vol.33
    • Ito, Y.1    Arikawa, K.2    Antonio, B.A.3    Ohta, I.4    Naito, S.5    Mukai, Y.6
  • 46
    • 0029866675 scopus 로고    scopus 로고
    • Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
    • Jensen, L. G., Olsen, O., Kops, O., Wolf, N., Thomsen, K. K., and von Wettstein, D. (1996). Transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination. Proc. Natl. Acad. Sci. U.S.A. 93, 3487-3491. doi: 10.1073/pnas.93.8.3487
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3487-3491
    • Jensen, L.G.1    Olsen, O.2    Kops, O.3    Wolf, N.4    Thomsen, K.K.5    Von Wettstein, D.6
  • 47
    • 0034897401 scopus 로고    scopus 로고
    • Gene tagging in rice: A high throughput system for functional genomics
    • Jeon, J. S., and An, G. H. (2001). Gene tagging in rice: a high throughput system for functional genomics. Plant Sci. 161, 211-219. doi: 10.1016/S0168-9452(01)00414-9
    • (2001) Plant Sci , vol.161 , pp. 211-219
    • Jeon, J.S.1    An, G.H.2
  • 48
    • 0037339657 scopus 로고    scopus 로고
    • Expression and import of an active cellulase from a thermophilic bacterium into the chloroplast both in vitro and in vivo
    • Jin, R., Richter, S., Zhong, R., and Lamppa, G. K. (2003). Expression and import of an active cellulase from a thermophilic bacterium into the chloroplast both in vitro and in vivo. Plant Mol. Biol. 51, 493-507. doi: 10.1023/A:1022354124741
    • (2003) Plant Mol. Biol , vol.51 , pp. 493-507
    • Jin, R.1    Richter, S.2    Zhong, R.3    Lamppa, G.K.4
  • 49
    • 80053240846 scopus 로고    scopus 로고
    • Effect of reduced ferulate-mediated lignin/arabinoxylan cross-linking in corn silage on feed intake, digestibility, and milk production
    • Jung, H. G., Mertens, D. R., and Phillips, R. L. (2011). Effect of reduced ferulate-mediated lignin/arabinoxylan cross-linking in corn silage on feed intake, digestibility, and milk production. J. Dairy Sci. 94, 5124-5137. doi: 10.3168/jds.2011-4495
    • (2011) J. Dairy Sci , vol.94 , pp. 5124-5137
    • Jung, H.G.1    Mertens, D.R.2    Phillips, R.L.3
  • 50
    • 77957308417 scopus 로고    scopus 로고
    • Expression of thermostable bacterial beta-glucosidase (BglB) in transgenic tobacco plants
    • Jung, S., Kim, S., Bae, H., Lim, H. S., and Bae, H. J. (2010). Expression of thermostable bacterial beta-glucosidase (BglB) in transgenic tobacco plants. Bioresour. Technol. 101, 7155-7161. doi: 10.1016/j.biortech.2010.03.140
    • (2010) Bioresour. Technol , vol.101 , pp. 7155-7161
    • Jung, S.1    Kim, S.2    Bae, H.3    Lim, H.S.4    Bae, H.J.5
  • 51
    • 84904728937 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens mediated transient expression of plant cell wall-degrading enzymes in detached sunflower leaves
    • Jung, S. K., Lindenmuth, B. E., McDonald, K. A., Hwang, H., Bui, M. Q., Falk, B. W., et al. (2014). Agrobacterium tumefaciens mediated transient expression of plant cell wall-degrading enzymes in detached sunflower leaves. Biotechnol. Prog. 30, 905-915. doi: 10.1002/btpr.1888
    • (2014) Biotechnol. Prog , vol.30 , pp. 905-915
    • Jung, S.K.1    Lindenmuth, B.E.2    McDonald, K.A.3    Hwang, H.4    Bui, M.Q.5    Falk, B.W.6
  • 52
    • 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., and Bae, H. J. (2013). Improved recombinant cellulase expression in chloroplast of tobacco through promoter engineering and 5’ amplification promoting sequence. Plant Mol. Biol. 83, 317-328. doi: 10.1007/s11103-013-0088-2
    • (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
  • 53
    • 0032724310 scopus 로고    scopus 로고
    • Expression of a bacterial endoglucanase gene in tobacco increases digestibility of its cell wall fibers
    • Kawazu, T., Sun, J. L., Shibata, M., Kimura, T., Sakka, K., and Ohmiya, K. (1999). Expression of a bacterial endoglucanase gene in tobacco increases digestibility of its cell wall fibers. J. Biosci. Bioeng. 88, 421-425. doi: 10.1016/S1389-1723(99)80220-5
    • (1999) J. Biosci. Bioeng , vol.88 , pp. 421-425
    • Kawazu, T.1    Sun, J.L.2    Shibata, M.3    Kimura, T.4    Sakka, K.5    Ohmiya, K.6
  • 54
    • 45849144011 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a glycosyl hydrolase family 9 cellulase distributed throughout the digestive tract of the cricket Teleogryllus emma
    • Kim, N., Choo, Y. M., Lee, K. S., Hong, S. J., Seol, K. Y., Je, Y. H., et al. (2008). Molecular cloning and characterization of a glycosyl hydrolase family 9 cellulase distributed throughout the digestive tract of the cricket Teleogryllus emma. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. 150, 368-376. doi: 10.1016/j.cbpb.2008.04.005
    • (2008) Comp. Biochem. Physiol. B, Biochem. Mol. Biol , vol.150 , pp. 368-376
    • Kim, N.1    Choo, Y.M.2    Lee, K.S.3    Hong, S.J.4    Seol, K.Y.5    Je, Y.H.6
  • 55
    • 0038151901 scopus 로고    scopus 로고
    • Molecular breeding of transgenic rice expressing a xylanase domain of the xynA gene from Clostridium thermocellum
    • Kimura, T., Mizutani, T., Tanaka, T., Koyama, T., Sakka, K., and Ohmiya, K. (2003). Molecular breeding of transgenic rice expressing a xylanase domain of the xynA gene from Clostridium thermocellum. Appl. Microbiol. Biotechnol. 62, 374-379. doi: 10.1007/s00253-003-1301-z
    • (2003) Appl. Microbiol. Biotechnol , vol.62 , pp. 374-379
    • Kimura, T.1    Mizutani, T.2    Tanaka, T.3    Koyama, T.4    Sakka, K.5    Ohmiya, K.6
  • 56
    • 84857441283 scopus 로고    scopus 로고
    • The challenge of enzyme cost in the production of lignocellulosic biofuels
    • Klein-Marcuschamer, D., Oleskowicz-Popiel, P., Simmons, B. A., and Blanch, H. W. (2012). The challenge of enzyme cost in the production of lignocellulosic biofuels. Biotechnol. Bioeng. 109, 1083-1087. doi: 10.1002/bit.24370
    • (2012) Biotechnol. Bioeng , vol.109 , pp. 1083-1087
    • Klein-Marcuschamer, D.1    Oleskowicz-Popiel, P.2    Simmons, B.A.3    Blanch, H.W.4
  • 57
    • 84876077030 scopus 로고    scopus 로고
    • Ethanol inducible expression of a mesophilic cellulase avoids adverse effects on plant development
    • Klose, H., Gunl, M., Usadel, B., Fischer, R., and Commandeur, U. (2013). Ethanol inducible expression of a mesophilic cellulase avoids adverse effects on plant development. Biotechnol. Biofuels 6:53. doi: 10.1186/1754-6834-6-53
    • (2013) Biotechnol. Biofuels , vol.6 , pp. 53
    • Klose, H.1    Gunl, M.2    Usadel, B.3    Fischer, R.4    Commandeur, U.5
  • 58
    • 84924082254 scopus 로고    scopus 로고
    • Cell wall modification in tobacco by differential targeting of recombinant endoglucanase from Trichoderma reesei
    • Klose, H., Gunl, M., Usadel, B., Fischer, R., and Commandeur, U. (2015). Cell wall modification in tobacco by differential targeting of recombinant endoglucanase from Trichoderma reesei. BMC Plant Biol. 15:54. doi: 10.1186/s12870-015-0443-3
    • (2015) BMC Plant Biol , vol.15 , pp. 54
    • Klose, H.1    Gunl, M.2    Usadel, B.3    Fischer, R.4    Commandeur, U.5
  • 59
    • 84865340615 scopus 로고    scopus 로고
    • Hyperthermophilic endoglucanase for in planta lignocellulose conversion
    • Klose, H., Röder, J., Girfoglio, M., Fischer, R., and Commandeur, U. (2012). Hyperthermophilic endoglucanase for in planta lignocellulose conversion. Biotechnol. Biofuels 5:63. doi: 10.1186/1754-6834-5-63
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 63
    • Klose, H.1    Röder, J.2    Girfoglio, M.3    Fischer, R.4    Commandeur, U.5
  • 60
    • 84055221845 scopus 로고    scopus 로고
    • Synergistic interactions in cellulose hydrolysis
    • Kostylev, M., and Wilson, D. (2012). Synergistic interactions in cellulose hydrolysis. Biofuels 3, 61-70. doi: 10.4155/bfs.11.150
    • (2012) Biofuels , vol.3 , pp. 61-70
    • Kostylev, M.1    Wilson, D.2
  • 61
    • 84988877013 scopus 로고    scopus 로고
    • Challenges and advances in the heterologous expression of cellulolytic enzymes: A review. Biotechnol
    • Lambertz, C., Garvey, M., Klinger, J., Heesel, D., Klose, H., Fischer, R., et al. (2014). Challenges and advances in the heterologous expression of cellulolytic enzymes: a review. Biotechnol. Biofuels 7, 135-150. doi: 10.1186/s13068-014-0135-5
    • (2014) Biofuels , vol.7 , pp. 135-150
    • Lambertz, C.1    Garvey, M.2    Klinger, J.3    Heesel, D.4    Klose, H.5    Fischer, R.6
  • 62
    • 84865467444 scopus 로고    scopus 로고
    • Synergistic effects of 2A-mediated polyproteins on the production of lignocelluloses degradation enzymes in tobacco plants
    • Lee, D. S., Lee, K. H., Jung, S., Jo, E. J., Han, K. H., and Bae, H. J. (2012). Synergistic effects of 2A-mediated polyproteins on the production of lignocelluloses degradation enzymes in tobacco plants. J. Exp. Bot. 63, 4797-4810. doi: 10.1093/jxb/ers159
    • (2012) J. Exp. Bot , vol.63 , pp. 4797-4810
    • Lee, D.S.1    Lee, K.H.2    Jung, S.3    Jo, E.J.4    Han, K.H.5    Bae, H.J.6
  • 63
    • 4444293375 scopus 로고    scopus 로고
    • H., et al. (2004). cDNA cloning, expression, and enzymatic activity of a cellulase from the mulberry longicorn beetle, Apriona germari
    • Lee, S. J., Kim, S. R., Yoon, H. J., Kim, I., Lee, K. S., Je, Y. H., et al. (2004). cDNA cloning, expression, and enzymatic activity of a cellulase from the mulberry longicorn beetle, Apriona germari. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 139, 107-116. doi: 10.1016/j.cbpc.2004.06.015
    • Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.139 , pp. 107-116
    • Lee, S.J.1    Kim, S.R.2    Yoon, H.J.3    Kim, I.4    Lee, K.S.5    Je, Y.6
  • 64
    • 20044384694 scopus 로고    scopus 로고
    • A novel cellulase gene from the mulberry longicorn beetle, Apriona germari: Gene structure, expression, and enzymatic activity
    • Lee, S. J., Lee, K. S., Kim, S. R., Gui, Z. Z., Kim, Y. S., Yoon, H. J., et al. (2005). A novel cellulase gene from the mulberry longicorn beetle, Apriona germari: gene structure, expression, and enzymatic activity. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 140, 551-560. doi: 10.1016/j.cbpc.2004.12.003
    • (2005) Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.140 , pp. 551-560
    • Lee, S.J.1    Lee, K.S.2    Kim, S.R.3    Gui, Z.Z.4    Kim, Y.S.5    Yoon, H.J.6
  • 65
    • 79451472642 scopus 로고    scopus 로고
    • High throughput Agrobacterium-mediated switchgrass transformation
    • Li, R. Y., and Qu, R. D. (2011). High throughput Agrobacterium-mediated switchgrass transformation. Biomass. Bioenerg. 35, 1046-1054. doi: 10.1016/j.biombioe.2010.11.025
    • (2011) Biomass. Bioenerg , vol.35 , pp. 1046-1054
    • Li, R.Y.1    Qu, R.D.2
  • 66
    • 84862829528 scopus 로고    scopus 로고
    • Highly efficient sorghum transformation
    • Liu, G., and Godwin, I. D. (2012). Highly efficient sorghum transformation. Plant Cell Rep. 31, 999-1007. doi: 10.1007/s00299-011-1218-4
    • (2012) Plant Cell Rep , vol.31 , pp. 999-1007
    • Liu, G.1    Godwin, I.D.2
  • 67
    • 79251624712 scopus 로고    scopus 로고
    • Microbiome of fungus-growing termites: A new reservoir for lignocellulase genes
    • Liu, N., Yan, X., Zhang, M., Xie, L., Wang, Q., Huang, Y., et al. (2011). Microbiome of fungus-growing termites: a new reservoir for lignocellulase genes. Appl. Environ. Microbiol. 77, 48-56. doi: 10.1128/AEM.01521-10
    • (2011) Appl. Environ. Microbiol , vol.77 , pp. 48-56
    • Liu, N.1    Yan, X.2    Zhang, M.3    Xie, L.4    Wang, Q.5    Huang, Y.6
  • 68
    • 84886092842 scopus 로고    scopus 로고
    • Advanced genetic tools for plant biotechnology. Nat
    • Liu, W. S., Yuan, J. S., and Stewart, C. N. Jr. (2014). Advanced genetic tools for plant biotechnology. Nat. Rev. Genet. 15, 781-973. doi: 10.1038/nrg3583
    • (2014) Rev. Genet , vol.15 , pp. 781-973
    • Liu, W.S.1    Yuan, J.S.2    Stewart, C.N.3
  • 69
  • 71
    • 79960468065 scopus 로고    scopus 로고
    • In planta differential targeting analysis of Thermotoga maritima Cel5A and CBM6-engineered Cel5A for autohydrolysis
    • Mahadevan, S. A., Wi, S. G., Kim, Y. O., Lee, K. H., and Bae, H. J. (2011). In planta differential targeting analysis of Thermotoga maritima Cel5A and CBM6-engineered Cel5A for autohydrolysis. Transgenic Res. 20, 877-886. doi: 10.1007/s11248-010-9464-8
    • (2011) Transgenic Res , vol.20 , pp. 877-886
    • Mahadevan, S.A.1    Wi, S.G.2    Kim, Y.O.3    Lee, K.H.4    Bae, H.J.5
  • 72
    • 51349085542 scopus 로고    scopus 로고
    • Site-directed mutagenesis and CBM engineering of Cel5A (Thermotoga maritima)
    • Mahadevan, S. A., Wi, S. G., Lee, D. S., and Bae, H. J. (2008). Site-directed mutagenesis and CBM engineering of Cel5A (Thermotoga maritima). FEMS Microbiol. Lett. 287, 205-211. doi: 10.1111/j.1574-6968.2008.01324.x
    • (2008) FEMS Microbiol. Lett , vol.287 , pp. 205-211
    • Mahadevan, S.A.1    Wi, S.G.2    Lee, D.S.3    Bae, H.J.4
  • 73
    • 8644230008 scopus 로고    scopus 로고
    • Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis
    • Marana, S. R., Andrade, E. H., Ferreira, C., and Terra, W. R. (2004). Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis. Eur. J. Biochem. 271, 4169-4177. doi: 10.1111/j.1432-1033.2004.04354.x
    • (2004) Eur. J. Biochem , vol.271 , pp. 4169-4177
    • Marana, S.R.1    Rade, E.H.2    Ferreira, C.3    Terra, W.R.4
  • 75
    • 84859726707 scopus 로고    scopus 로고
    • Identification and characterization of a new xylanase from Gram-positive bacteria isolated from termite gut (Reticulitermes santonensis)
    • Mattéotti, C., Bauwens, J., Brasseur, C., Tarayre, C., Thonart, P., Destain, J., et al. (2012). Identification and characterization of a new xylanase from Gram-positive bacteria isolated from termite gut (Reticulitermes santonensis). Protein Expr. Purif. 83, 117-127. doi: 10.1016/j.pep.2012.03.009
    • (2012) Protein Expr. Purif , vol.83 , pp. 117-127
    • Mattéotti, C.1    Bauwens, J.2    Brasseur, C.3    Tarayre, C.4    Thonart, P.5    Destain, J.6
  • 76
    • 78650217378 scopus 로고    scopus 로고
    • Characterization of a new beta-glucosidase/beta-xylosidase from the gut microbiota of the termite (Reticulitermes santonensis)
    • Mattéotti, C., Haubruge, E., Thonart, P., Francis, F., De Pauw, E., Portetelle, D., et al. (2011). Characterization of a new beta-glucosidase/beta-xylosidase from the gut microbiota of the termite (Reticulitermes santonensis). FEMS Microbiol. Lett. 314, 147-157. doi: 10.1111/j.1574-6968.2010.02161.x
    • (2011) FEMS Microbiol. Lett , vol.314 , pp. 147-157
    • Mattéotti, C.1    Haubruge, E.2    Thonart, P.3    Francis, F.4    De Pauw, E.5    Portetelle, D.6
  • 77
    • 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., and Cowan, D. A. (2014). Recombinant hyperthermophilic enzyme expression in plants: a novel approach for lignocellulose digestion. Trends Biotechnol. 32, 281-289. doi: 10.1016/j.tibtech.2014.03.003
    • (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
  • 78
    • 84909606775 scopus 로고    scopus 로고
    • Phylogenomics resolves the timing and pattern of insect evolution
    • Misof, B., Liu, S. L., Meusemann, K., Peters, R. S., Donath, A., Mayer, C., et al. (2014). Phylogenomics resolves the timing and pattern of insect evolution. Science 346, 763-767. doi: 10.1126/science.1257570
    • (2014) Science , vol.346 , pp. 763-767
    • Misof, B.1    Liu, S.L.2    Meusemann, K.3    Peters, R.S.4    Donath, A.5    Mayer, C.6
  • 79
    • 79958822686 scopus 로고    scopus 로고
    • The grass leaf developmental gradient as a platform for a systems understanding of the anatomical specialization of C-4 leaves
    • Nelson, T. (2011). The grass leaf developmental gradient as a platform for a systems understanding of the anatomical specialization of C-4 leaves. J. Exp. Bot. 62, 3039-3048. doi: 10.1093/jxb/err072
    • (2011) J. Exp. Bot , vol.62 , pp. 3039-3048
    • Nelson, T.1
  • 80
    • 84882692475 scopus 로고    scopus 로고
    • Lignocellulose-degrading enzymes from termites and their symbiotic microbiota
    • Ni, J. F., and Tokuda, G. (2013). Lignocellulose-degrading enzymes from termites and their symbiotic microbiota. Biotechnol. Adv. 31, 838-850. doi: 10.1016/j.biotechadv.2013.04.005
    • (2013) Biotechnol. Adv , vol.31 , pp. 838-850
    • Ni, J.F.1    Tokuda, G.2
  • 81
    • 36849085009 scopus 로고    scopus 로고
    • Heterologous expression and enzymatic characterization of beta-glucosidase from the drywood-eating termite, Neotermes koshunensis
    • Ni, J. F., Tokuda, G., Takehara, M., and Watanabe, H. (2007). Heterologous expression and enzymatic characterization of beta-glucosidase from the drywood-eating termite, Neotermes koshunensis. Appl. Entomol. Zool. 42, 457-463. doi: 10.1303/aez.2007.457
    • (2007) Appl. Entomol. Zool , vol.42 , pp. 457-463
    • Ni, J.F.1    Tokuda, G.2    Takehara, M.3    Watanabe, H.4
  • 82
    • 84865140768 scopus 로고    scopus 로고
    • Enhanced saccharification of rice straw by overexpression of rice exo-glucanase
    • Nigorikawa, M., Watanabe, A., Furukawa, K., Sonoki, T., and Ito, Y. (2012). Enhanced saccharification of rice straw by overexpression of rice exo-glucanase. Rice 5:14. doi: 10.1186/1939-8433-5-14
    • (2012) Rice , vol.5 , pp. 14
    • Nigorikawa, M.1    Watanabe, A.2    Furukawa, K.3    Sonoki, T.4    Ito, Y.5
  • 83
    • 0037364788 scopus 로고    scopus 로고
    • Termite symbiotic systems: Efficient bio-recycling of lignocellulose
    • Ohkuma, M. (2003). Termite symbiotic systems: efficient bio-recycling of lignocellulose. Appl. Microbiol. Biotechnol. 61, 1-9. doi: 10.1007/s00253-002-1189-z
    • (2003) Appl. Microbiol. Biotechnol , vol.61 , pp. 1-9
    • Ohkuma, M.1
  • 85
    • 35848947524 scopus 로고    scopus 로고
    • Enhanced conversion of plant biomass into glucose using transgenic rice-produced endoglucanase for cellulosic ethanol
    • Oraby, H., Venkatesh, B., Dale, B., Ahmad, R., Ransom, C., Oehmke, J., et al. (2007). Enhanced conversion of plant biomass into glucose using transgenic rice-produced endoglucanase for cellulosic ethanol. Transgenic Res. 16, 739-749. doi: 10.1007/s11248-006-9064-9
    • (2007) Transgenic Res , vol.16 , pp. 739-749
    • Oraby, H.1    Venkatesh, B.2    Dale, B.3    Ahmad, R.4    Ransom, C.5    Oehmke, J.6
  • 86
    • 0033997338 scopus 로고    scopus 로고
    • Transgenic barley expressing a fungal xylanase gene in the endosperm of the developing grains
    • Patel, M., Johnson, J. S., Brettell, R. I. S., Jacobsen, J., and Xue, G. P. (2000). Transgenic barley expressing a fungal xylanase gene in the endosperm of the developing grains. Mol. Breed. 6, 113-123. doi: 10.1023/A:1009640427515
    • (2000) Mol. Breed , vol.6 , pp. 113-123
    • Patel, M.1    Johnson, J.S.2    Brettell, R.I.S.3    Jacobsen, J.4    Xue, G.P.5
  • 87
    • 39449119156 scopus 로고    scopus 로고
    • Heterologous Acidothermus cellulolyticus 1,4-beta-endoglucanase E1 produced within the corn biomass converts corn stover into glucose
    • Ransom, C., Balan, V., Biswas, G., Dale, B., Crockett, E., and Sticklen, M. (2007). Heterologous Acidothermus cellulolyticus 1,4-beta-endoglucanase E1 produced within the corn biomass converts corn stover into glucose. Appl. Biochem. Biotechnol. 137-140, 207-219. doi: 10.1007/s12010-007-9053-3
    • (2007) Appl. Biochem. Biotechnol , vol.137-140 , pp. 207-219
    • Ransom, C.1    Balan, V.2    Biswas, G.3    Dale, B.4    Crockett, E.5    Sticklen, M.6
  • 88
    • 76549243087 scopus 로고
    • The biological degradation of soluble cellulose derivatives and Its relationship to the mechanism of cellulose hydrolysis
    • Reese, E. T., Siu, R. G. H., and Levinson, H. S. (1950). The biological degradation of soluble cellulose derivatives and Its relationship to the mechanism of cellulose hydrolysis. J. Bacteriol. 59, 485-497.
    • (1950) J. Bacteriol , vol.59 , pp. 485-497
    • Reese, E.T.1    Siu, R.G.H.2    Levinson, H.S.3
  • 89
    • 19944434180 scopus 로고    scopus 로고
    • Comparative genome sequencing of Drosophila pseudoobscura: Chromosomal, gene, and cis-element evolution
    • Richards, S., Liu, Y., Bettencourt, B. R., Hradecky, P., Letovsky, S., Nielsen, R., et al. (2005). Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution. Genome Res. 15, 1-18. doi: 10.1101/gr.3059305
    • (2005) Genome Res , vol.15 , pp. 1-18
    • Richards, S.1    Liu, Y.2    Bettencourt, B.R.3    Hradecky, P.4    Letovsky, S.5    Nielsen, R.6
  • 91
    • 0037623814 scopus 로고    scopus 로고
    • Hemicellulose bioconversion
    • Saha, B. C. (2003). Hemicellulose bioconversion. J. Ind. Microbiol. Biotechnol. 30, 279-291. doi: 10.1007/s10295-003-0049-x
    • (2003) J. Ind. Microbiol. Biotechnol , vol.30 , pp. 279-291
    • Saha, B.C.1
  • 92
    • 77549084364 scopus 로고    scopus 로고
    • Brown midrib mutations and their importance to the utilization of maize, sorghum, and pearl millet lignocellulosic tissues
    • Sattler, S. E., Funnell-Harris, D. L., and Pedersen, J. F. (2010). Brown midrib mutations and their importance to the utilization of maize, sorghum, and pearl millet lignocellulosic tissues. Plant Sci. 178, 229-238. doi: 10.1016/j.plantsci.2010.01.001
    • (2010) Plant Sci , vol.178 , pp. 229-238
    • Sattler, S.E.1    Funnell-Harris, D.L.2    Pedersen, J.F.3
  • 93
    • 77954657091 scopus 로고    scopus 로고
    • Functional and translational analyses of a beta-glucosidase gene (Glycosyl hydrolase family 1) isolated from the gut of the lower termite Reticulitermes flavipes
    • Scharf, M. E., Kovaleva, E. S., Jadhao, S., Campbell, J. H., Buchman, G. W., and Boucias, D. G. (2010). Functional and translational analyses of a beta-glucosidase gene (glycosyl hydrolase family 1) isolated from the gut of the lower termite Reticulitermes flavipes. Insect Biochem. Mol. Biol. 40, 611-620. doi: 10.1016/j.ibmb.2010.06.002
    • (2010) Insect Biochem. Mol. Biol , vol.40 , pp. 611-620
    • Scharf, M.E.1    Kovaleva, E.S.2    Jadhao, S.3    Campbell, J.H.4    Buchman, G.W.5    Boucias, D.G.6
  • 94
    • 77950423986 scopus 로고    scopus 로고
    • Hemicelluloses
    • Scheller, H. V., and Ulvskov, P. (2010). Hemicelluloses. Annu. Rev. Plant Biol. 61, 263-289. doi: 10.1146/annurev-arplant-042809-112315
    • (2010) Annu. Rev. Plant Biol , vol.61 , pp. 263-289
    • Scheller, H.V.1    Ulvskov, P.2
  • 95
    • 0025790139 scopus 로고
    • A steroid-inducible gene expression system for plant cells
    • Schena, M., Lloyd, A. M., and Davis, R. W. (1991). A steroid-inducible gene expression system for plant cells. Proc. Natl. Acad. Sci. U.S.A. 88, 10421-10425. doi: 10.1073/pnas.88.23.10421
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10421-10425
    • Schena, M.1    Lloyd, A.M.2    Davis, R.W.3
  • 96
    • 84888808374 scopus 로고    scopus 로고
    • Endogenous cellulase enzymes in the stick insect (Phasmatodea) gut
    • Shelomi, M., Watanabe, H., and Arakawa, G. (2014). Endogenous cellulase enzymes in the stick insect (Phasmatodea) gut. J. Insect Physiol. 60, 25-30. doi: 10.1016/j.jinsphys.2013.10.007
    • (2014) J. Insect Physiol , vol.60 , pp. 25-30
    • Shelomi, M.1    Watanabe, H.2    Arakawa, G.3
  • 97
    • 84869476196 scopus 로고    scopus 로고
    • Engineering a thermoregulated intein-modified xylanase into maize for consolidated lignocellulosic biomass processing. Nat
    • Shen, B., Sun, X., Zuo, X., Shilling, T., Apgar, J., Ross, M., et al. (2012). Engineering a thermoregulated intein-modified xylanase into maize for consolidated lignocellulosic biomass processing. Nat. Biotechnol. 30, 1131-1136. doi: 10.1038/nbt.2402
    • (2012) Biotechnol , vol.30 , pp. 1131-1136
    • Shen, B.1    Sun, X.2    Zuo, X.3    Shilling, T.4    Apgar, J.5    Ross, M.6
  • 98
    • 84891516541 scopus 로고    scopus 로고
    • A genomics approach to deciphering lignin biosynthesis in switchgrass
    • Shen, H., Mazarei, M., Hisano, H., Escamilla-Trevino, L., Fu, C., Pu, Y., Rudis, M. R., et al. (2013). A genomics approach to deciphering lignin biosynthesis in switchgrass. Plant Cell 25, 4342-4361. doi: 10.1105/tpc.113.118828
    • (2013) Plant Cell , vol.25 , pp. 4342-4361
    • Shen, H.1    Mazarei, M.2    Hisano, H.3    Escamilla-Trevino, L.4    Fu, C.5    Pu, Y.6    Rudis, M.R.7
  • 99
    • 78650547542 scopus 로고    scopus 로고
    • Comparison of insect gut cellulose and xylanase activity across different insect species with distinct food sources
    • Shi, W. B., Ding, S. Y., and Yuan, J. S. (2011). Comparison of insect gut cellulose and xylanase activity across different insect species with distinct food sources. Bioenerg Res. 4, 1-10. doi: 10.1007/s12155-010-9096-0
    • (2011) Bioenerg Res , vol.4 , pp. 1-10
    • Shi, W.B.1    Ding, S.Y.2    Yuan, J.S.3
  • 100
    • 84873494410 scopus 로고    scopus 로고
    • Comparative genomic analysis of the microbiome [corrected] of herbivorous insects reveals eco-environmental adaptations: Biotechnology applications
    • Shi, W., Xie, S., Chen, X., Sun, S., Zhou, X., Liu, L., et al. (2013). Comparative genomic analysis of the microbiome [corrected] of herbivorous insects reveals eco-environmental adaptations: biotechnology applications. PLoS Genet. 9:e1003131. doi: 10.1371/journal.pgen.1003131
    • (2013) Plos Genet , vol.9
    • Shi, W.1    Xie, S.2    Chen, X.3    Sun, S.4    Zhou, X.5    Liu, L.6
  • 101
    • 84907876881 scopus 로고    scopus 로고
    • Expression of an endoglucanase from Tribolium castaneum (TcEG1) in Saccharomyces cerevisiae
    • Shirley, D., Oppert, C., Reynolds, T. B., Miracle, B., Oppert, B., Klingeman, W. E., et al. (2014). Expression of an endoglucanase from Tribolium castaneum (TcEG1) in Saccharomyces cerevisiae. Insect Sci. 21, 609-618. doi: 10.1111/1744-7917.12069
    • (2014) Insect Sci , vol.21 , pp. 609-618
    • Shirley, D.1    Oppert, C.2    Reynolds, T.B.3    Miracle, B.4    Oppert, B.5    Klingeman, W.E.6
  • 102
    • 0026448126 scopus 로고
    • Cellulose digestion in termites and cockroaches - What role do symbionts play?
    • Slaytor, M. (1992). Cellulose digestion in termites and cockroaches - What role do symbionts play? Comp. Biochem. Phys. B 103, 775-784. doi: 10.1016/0305-0491(92)90194-V
    • (1992) Comp. Biochem. Phys. B , vol.103 , pp. 775-784
    • Slaytor, M.1
  • 103
    • 34247138742 scopus 로고    scopus 로고
    • Expression and characterization of Acidothermus cellulolyticus E1 endoglucanase in transgenic duckweed Lemna minor 8627
    • Sun, Y., Cheng, J. J., Himmel, M. E., Skory, C. D., Adney, W. S., Thomas, S. R., et al. (2007). Expression and characterization of Acidothermus cellulolyticus E1 endoglucanase in transgenic duckweed Lemna minor 8627. Bioresour. Technol. 98, 2866-2872. doi: 10.1016/j.biortech.2006.09.055
    • (2007) Bioresour. Technol , vol.98 , pp. 2866-2872
    • Sun, Y.1    Cheng, J.J.2    Himmel, M.E.3    Skory, C.D.4    Adney, W.S.5    Thomas, S.R.6
  • 104
    • 47049123955 scopus 로고    scopus 로고
    • Heterologous expression of glycosyl hydrolases in planta: A new departure for biofuels
    • Taylor, L. E. II, Dai, Z., Decker, S. R., Brunecky, R., Adney, W. S., Ding, S. Y., et al. (2008). Heterologous expression of glycosyl hydrolases in planta: a new departure for biofuels. Trends Biotechnol. 26, 413-424. doi: 10.1016/j.tibtech.2008.05.002
    • (2008) Trends Biotechnol , vol.26 , pp. 413-424
    • Taylor, L.1    Dai, Z.2    Decker, S.R.3    Brunecky, R.4    Adney, W.S.5    Ding, S.Y.6
  • 105
    • 77949300418 scopus 로고    scopus 로고
    • Heterologous expression and characterization of an endoglucanase from a symbiotic protist of the lower termite, Reticulitermes speratus
    • Todaka, N., Lopez, C. M., Inoue, T., Saita, K., Maruyama, J., Arioka, M., et al. (2010). Heterologous expression and characterization of an endoglucanase from a symbiotic protist of the lower termite, Reticulitermes speratus. Appl. Microbiol. Biotechnol. 160, 1168-1178. doi: 10.1007/s12010-009-8626-8
    • (2010) Appl. Microbiol. Biotechnol , vol.160 , pp. 1168-1178
    • Todaka, N.1    Lopez, C.M.2    Inoue, T.3    Saita, K.4    Maruyama, J.5    Arioka, M.6
  • 106
    • 36549000535 scopus 로고    scopus 로고
    • Hidden cellulases in termites: Revision of an old hypothesis. Biol
    • Tokuda, G., and Watanabe, H. (2007). Hidden cellulases in termites: revision of an old hypothesis. Biol. Lett. 3, 336-339. doi: 10.1098/rsbl.2007.0073
    • (2007) Lett , vol.3 , pp. 336-339
    • Tokuda, G.1    Watanabe, H.2
  • 108
    • 79952575277 scopus 로고    scopus 로고
    • Heterologous expression and characterization of a glucose-stimulated beta-glucosidase from the termite Neotermes koshunensis in Aspergillus oryzae
    • Uchima, C. A., Tokuda, G., Watanabe, H., Kitamoto, K., and Arioka, M. (2011). Heterologous expression and characterization of a glucose-stimulated beta-glucosidase from the termite Neotermes koshunensis in Aspergillus oryzae. Appl. Microbiol. Biotechnol. 89, 1761-1771. doi: 10.1007/s00253-010-2963-y
    • (2011) Appl. Microbiol. Biotechnol , vol.89 , pp. 1761-1771
    • Uchima, C.A.1    Tokuda, G.2    Watanabe, H.3    Kitamoto, K.4    Arioka, M.5
  • 109
    • 84864095436 scopus 로고    scopus 로고
    • Heterologous expression in Pichia pastoris and characterization of an endogenous thermostable and high-glucose-tolerant beta-glucosidase from the termite Nasutitermes takasagoensis
    • Uchima, C. A., Tokuda, G., Watanabe, H., Kitamoto, K., and Arioka, M. (2012). Heterologous expression in Pichia pastoris and characterization of an endogenous thermostable and high-glucose-tolerant beta-glucosidase from the termite Nasutitermes takasagoensis. Appl. Environ. Microbiol. 78, 4288-4293. doi: 10.1128/AEM.07718-11
    • (2012) Appl. Environ. Microbiol , vol.78 , pp. 4288-4293
    • Uchima, C.A.1    Tokuda, G.2    Watanabe, H.3    Kitamoto, K.4    Arioka, M.5
  • 110
    • 84870757305 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of an endogenous endoglucanase belonging to GHF45 from the western corn rootworm, Diabrotica virgifera virgifera
    • Valencia, A., Alves, A. P., and Siegfried, B. D. (2013). Molecular cloning and functional characterization of an endogenous endoglucanase belonging to GHF45 from the western corn rootworm, Diabrotica virgifera virgifera. Gene 513, 260-267. doi: 10.1016/j.gene.2012.10.046
    • (2013) Gene , vol.513 , pp. 260-267
    • Valencia, A.1    Alves, A.P.2    Siegfried, B.D.3
  • 111
    • 76749150030 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the model grass Brachypodium distachyon
    • Vogel, J. P., Garvin, D. F., Mockler, T. C., Schmutz, J., Rokhsar, D., Bevan, M. W., et al. (2010). Genome sequencing and analysis of the model grass Brachypodium distachyon. Nature 463, 763-768. doi: 10.1038/nature08747
    • (2010) Nature , vol.463 , pp. 763-768
    • Vogel, J.P.1    Garvin, D.F.2    Mockler, T.C.3    Schmutz, J.4    Rokhsar, D.5    Bevan, M.W.6
  • 112
    • 68749109670 scopus 로고    scopus 로고
    • Development of SSR markers and analysis of diversity in Turkish populations of Brachypodium distachyon
    • Vogel, J. P., Tuna, M., Budak, H., Huo, N. X., Gu, Y. Q., and Steinwand, M. A. (2009). Development of SSR markers and analysis of diversity in Turkish populations of Brachypodium distachyon. BMC Plant Biol. 9:88. doi: 10.1186/1471-2229-9-88
    • (2009) BMC Plant Biol , vol.9 , pp. 88
    • Vogel, J.P.1    Tuna, M.2    Budak, H.3    Huo, N.X.4    Gu, Y.Q.5    Steinwand, M.A.6
  • 113
    • 84867206640 scopus 로고    scopus 로고
    • Characterization of a novel thermostable beta-glucosidase from a metagenomic library of termite gut
    • Wang, Q., Qian, C., Zhang, X. Z., Liu, N., Yan, X., and Zhou, Z. (2012). Characterization of a novel thermostable beta-glucosidase from a metagenomic library of termite gut. Enzyme Microb. Technol. 51, 319-324. doi: 10.1016/j.enzmictec.2012.07.015
    • (2012) Enzyme Microb. Technol , vol.51 , pp. 319-324
    • Wang, Q.1    Qian, C.2    Zhang, X.Z.3    Liu, N.4    Yan, X.5    Zhou, Z.6
  • 114
    • 0032560853 scopus 로고    scopus 로고
    • A cellulase gene of termite origin
    • Watanabe, H., Noda, H., Tokuda, G., and Lo, N. (1998). A cellulase gene of termite origin. Nature 394, 330-331. doi: 10.1038/28527
    • (1998) Nature , vol.394 , pp. 330-331
    • Watanabe, H.1    Noda, H.2    Tokuda, G.3    Lo, N.4
  • 115
    • 0034844001 scopus 로고    scopus 로고
    • Animal cellulases
    • Watanabe, H., and Tokuda, G. (2001). Animal cellulases. Cell. Mol. Life Sci. 58, 1167-1178. doi: 10.1007/PL00000931
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 1167-1178
    • Watanabe, H.1    Tokuda, G.2
  • 116
    • 77449097393 scopus 로고    scopus 로고
    • Cellulolytic systems in insects
    • Watanabe, H., and Tokuda, G. (2010). Cellulolytic systems in insects. Annu. Rev. Entomol. 55, 609-632. doi: 10.1146/annurev-ento-112408-085319
    • (2010) Annu. Rev. Entomol , vol.55 , pp. 609-632
    • Watanabe, H.1    Tokuda, G.2
  • 117
    • 33748894362 scopus 로고    scopus 로고
    • Molecular cloning, expression, and enzymatic activity of a novel endogenous cellulase from the mulberry longicorn beetle, Apriona germari
    • Wei, Y. D., Lee, K. S., Gui, Z. Z., Yoon, H. J., Kim, I., Zhang, G. Z., et al. (2006). Molecular cloning, expression, and enzymatic activity of a novel endogenous cellulase from the mulberry longicorn beetle, Apriona germari. Comp. Biochem Physiol. B Biochem. Mol. Biol. 145, 220-229. doi: 10.1016/j.cbpb.2006.07.007
    • (2006) Comp. Biochem Physiol. B Biochem. Mol. Biol , vol.145 , pp. 220-229
    • Wei, Y.D.1    Lee, K.S.2    Gui, Z.Z.3    Yoon, H.J.4    Kim, I.5    Zhang, G.Z.6
  • 118
    • 33750460281 scopus 로고    scopus 로고
    • Insights into social insects from the genome of the honeybee Apis mellifera
    • Weinstock, G. M., Robinson, G. E., Gibbs, R. A., Worley, K. C., Evans, J. D., Maleszka, R., et al. (2006). Insights into social insects from the genome of the honeybee Apis mellifera. Nature 443, 931-949. doi: 10.1038/nature05260
    • (2006) Nature , vol.443 , pp. 931-949
    • Weinstock, G.M.1    Robinson, G.E.2    Gibbs, R.A.3    Worley, K.C.4    Evans, J.D.5    Maleszka, R.6
  • 119
    • 84873305404 scopus 로고    scopus 로고
    • Effects of an exogenous xylanase gene expression on the growth of transgenic rice and the expression level of endogenous xylanase inhibitor gene RIXI
    • Weng, X., Huang, Y., Hou, C., and Jiang, D. (2013). Effects of an exogenous xylanase gene expression on the growth of transgenic rice and the expression level of endogenous xylanase inhibitor gene RIXI. J. Sci. Food. Agric. 93, 173-179. doi: 10.1002/jsfa.5746
    • (2013) J. Sci. Food. Agric , vol.93 , pp. 173-179
    • Weng, X.1    Huang, Y.2    Hou, C.3    Jiang, D.4
  • 120
    • 74549184089 scopus 로고    scopus 로고
    • Functional and evolutionary insights from the genomes of three parasitoid Nasonia species
    • Werren, J. H., Richards, S., Desjardins, C. A., Niehuis, O., Gadau, J., Colbourne, J. K., et al. (2010). Functional and evolutionary insights from the genomes of three parasitoid Nasonia species. Science 327, 343-348. doi: 10.1126/science.1178028
    • (2010) Science , vol.327 , pp. 343-348
    • Werren, J.H.1    Richards, S.2    Desjardins, C.A.3    Niehuis, O.4    Gadau, J.5    Colbourne, J.K.6
  • 121
    • 78651440931 scopus 로고    scopus 로고
    • Identification, cloning, and expression of a GHF9 cellulase from Tribolium castaneum (Coleoptera: Tenebrionidae)
    • Willis, J. D., Oppert, B., Oppert, C., Klingeman, W. E., and Jurat-Fuentes, J. L. (2011). Identification, cloning, and expression of a GHF9 cellulase from Tribolium castaneum (Coleoptera: Tenebrionidae). J. Insect Physiol. 57, 300-306. doi: 10.1016/j.jinsphys.2010.11.019
    • (2011) J. Insect Physiol , vol.57 , pp. 300-306
    • Willis, J.D.1    Oppert, B.2    Oppert, C.3    Klingeman, W.E.4    Jurat-Fuentes, J.L.5
  • 122
    • 77954171659 scopus 로고    scopus 로고
    • Methods for discovery and characterization of cellulolytic enzymes from insects
    • Willis, J. D., Oppert, C., and Jurat-Fuentes, J. L. (2010). Methods for discovery and characterization of cellulolytic enzymes from insects. Insect Sci. 17, 184-198. doi: 10.1111/j.1744-7917.2010.01322.x
    • (2010) Insect Sci , vol.17 , pp. 184-198
    • Willis, J.D.1    Oppert, C.2    Jurat-Fuentes, J.L.3
  • 123
    • 84971094179 scopus 로고
    • Comparative digestibility and anatomy of some sympatric C-3 and C-4 arid zone grasses
    • Wilson, J. R., and Hacker, J. B. (1987). Comparative digestibility and anatomy of some sympatric C-3 and C-4 arid zone grasses. Aust. J. Agr. Res. 38, 287-295. doi: 10.1071/AR9870287
    • (1987) Aust. J. Agr. Res , vol.38 , pp. 287-295
    • Wilson, J.R.1    Hacker, J.B.2
  • 124
    • 84868547280 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an endogenous digestive beta-glucosidase from the midgut of the fungus-growing termite Macrotermes barneyi
    • Wu, Y., Chi, S., Yun, C., Shen, Y., Tokuda, G., and Ni, J. (2012). Molecular cloning and characterization of an endogenous digestive beta-glucosidase from the midgut of the fungus-growing termite Macrotermes barneyi. Insect Mol. Biol. 21, 604-614. doi: 10.1111/j.1365-2583.2012.01164.x
    • (2012) Insect Mol. Biol , vol.21 , pp. 604-614
    • Wu, Y.1    Chi, S.2    Yun, C.3    Shen, Y.4    Tokuda, G.5    Ni, J.6
  • 125
    • 33947157565 scopus 로고    scopus 로고
    • What is (And is not) vital to advancing cellulosic ethanol
    • Wyman, C. E. (2007). What is (and is not) vital to advancing cellulosic ethanol. Trends Biotechnol. 25, 153-157. doi: 10.1016/j.tibtech.2007.02.009
    • (2007) Trends Biotechnol , vol.25 , pp. 153-157
    • Wyman, C.E.1
  • 126
    • 84871407705 scopus 로고    scopus 로고
    • CDNA cloning, expression, and enzymatic activity of a novel endogenous cellulase from the beetle Batocera horsfieldi
    • Xia, D., Wei, Y., Zhang, G., Zhao, Q., Zhang, Y., Xiang, Z., et al. (2013). cDNA cloning, expression, and enzymatic activity of a novel endogenous cellulase from the beetle Batocera horsfieldi. Gene 514, 62-68. doi: 10.1016/j.gene.2012.08.044
    • Gene , vol.514 , pp. 62-68
    • Xia, D.1    Wei, Y.2    Zhang, G.3    Zhao, Q.4    Zhang, Y.5
  • 127
    • 10844228836 scopus 로고    scopus 로고
    • Microplate-based filter paper assay to measure total cellulase activity
    • Xiao, Z. Z., Storms, R., and Tsang, A. (2004). Microplate-based filter paper assay to measure total cellulase activity. Biotechnol. Bioeng. 88, 832-837. doi: 10.1002/bit.20286
    • (2004) Biotechnol. Bioeng , vol.88 , pp. 832-837
    • Xiao, Z.Z.1    Storms, R.2    Tsang, A.3
  • 128
    • 0042128623 scopus 로고    scopus 로고
    • Selectable marker-free transgenic barley producing a high level of cellulose (1,4-beta-glucanase) in developing grains
    • Xue, G. P., Patel, M., Johnson, J. S., Smyth, D. J., and Vickers, C. E. (2003). Selectable marker-free transgenic barley producing a high level of cellulose (1,4-beta-glucanase) in developing grains. Plant Cell Rep. 21, 1088-1094. doi: 10.1007/s00299-003-0627-4
    • (2003) Plant Cell Rep , vol.21 , pp. 1088-1094
    • Xue, G.P.1    Patel, M.2    Johnson, J.S.3    Smyth, D.J.4    Vickers, C.E.5
  • 129
    • 33847710688 scopus 로고    scopus 로고
    • Expression of xylanase with high specific activity from Streptomyces olivaceoviridis A1 in transgenic potato plants (Solanum tuberosum L.)
    • Yang, P. L., Wang, Y. R., Bai, Y. G., Meng, K., Luo, H. Y., Yuan, T. Z., et al. (2007). Expression of xylanase with high specific activity from Streptomyces olivaceoviridis A1 in transgenic potato plants (Solanum tuberosum L.). Biotechnol. Lett. 29, 659-667. doi: 10.1007/s10529-006-9280-7
    • (2007) Biotechnol. Lett , vol.29 , pp. 659-667
    • Yang, P.L.1    Wang, Y.R.2    Bai, Y.G.3    Meng, K.4    Luo, H.Y.5    Yuan, T.Z.6
  • 130
    • 70349869654 scopus 로고    scopus 로고
    • Effect of particle size on the rate of enzymatic hydrolysis of cellulose
    • Yeh, A. I., Huang, Y. C., and Chen, S. H. (2010). Effect of particle size on the rate of enzymatic hydrolysis of cellulose. Carbohyd. Polym. 79, 192-199. doi: 10.1016/j.carbpol.2009.07.049
    • (2010) Carbohyd. Polym , vol.79 , pp. 192-199
    • Yeh, A.I.1    Huang, Y.C.2    Chen, S.H.3
  • 131
    • 34548396828 scopus 로고    scopus 로고
    • Expression of thermostable microbial cellulases in the chloroplasts of nicotine-free tobacco
    • Yu, L. X., Gray, B. N., Rutzke, C. J., Walker, L. P., Wilson, D. B., and Hanson, M. R. (2007). Expression of thermostable microbial cellulases in the chloroplasts of nicotine-free tobacco. J. Biotechnol. 131, 362-369. doi: 10.1016/j.jbiotec.2007.07.942
    • (2007) J. Biotechnol , vol.131 , pp. 362-369
    • Yu, L.X.1    Gray, B.N.2    Rutzke, C.J.3    Walker, L.P.4    Wilson, D.B.5    Hanson, M.R.6
  • 132
    • 84855193675 scopus 로고    scopus 로고
    • Functional analyses of the digestive beta-glucosidase of Formosan subterranean termites (Coptotermes formosanus)
    • Zhang A. B., and Lax, A. R. (2012). Functional analyses of the digestive beta-glucosidase of Formosan subterranean termites (Coptotermes formosanus). J. Insect Physiol. 58, 205-210. doi: 10.1016/j.jinsphys.2011.11.014
    • (2012) J. Insect Physiol , vol.58 , pp. 205-210
    • Zhang, A.B.1    Lax, A.R.2
  • 133
    • 79952196194 scopus 로고    scopus 로고
    • Characterization of a new endogenous endo-beta-1,4-glucanase of Formosan subterranean termite (Coptotermes formosanus)
    • Zhang, D., Lax, A. R., Bland, J. M., and Allen, A. B. (2011). Characterization of a new endogenous endo-beta-1,4-glucanase of Formosan subterranean termite (Coptotermes formosanus). Insect Biochem. Mol. Biol. 41, 211-218. doi:10.1016/j.ibmb.2010.12.006
    • (2011) Insect Biochem. Mol. Biol , vol.41 , pp. 211-218
    • Zhang, D.1    Lax, A.R.2    Bland, J.M.3    Allen, A.B.4
  • 134
    • 83655172643 scopus 로고    scopus 로고
    • Removal of the fermentation inhibitor, Furfural, using activated carbon in cellulosic-ethanol production
    • Zhang, K., Agrawal, M., Harper, J., Chen, R., and Koros, W. J. (2011). Removal of the fermentation inhibitor, Furfural, using activated carbon in cellulosic-ethanol production. Ind. Eng. Chem. Res. 50, 14055-14060. doi: 10.1021/ie2013983
    • (2011) Ind. Eng. Chem. Res , vol.50 , pp. 14055-14060
    • Zhang, K.1    Agrawal, M.2    Harper, J.3    Chen, R.4    Koros, W.J.5
  • 135
    • 84862782197 scopus 로고    scopus 로고
    • Expression of an Acidothermus cellulolyticus endoglucanase in transgenic rice seeds. ProteinExpr
    • Zhang, Q., Zhang, W., Lin, C. Y., Xu, X. L., and Shen, Z. C. (2012). Expression of an Acidothermus cellulolyticus endoglucanase in transgenic rice seeds. ProteinExpr. Purif. 82, 279-283. doi: 10.1016/j.pep.2012.01.011
    • (2012) Purif , vol.82 , pp. 279-283
    • Zhang, Q.1    Zhang, W.2    Lin, C.Y.3    Xu, X.L.4    Shen, Z.C.5
  • 136
    • 84925414041 scopus 로고    scopus 로고
    • Production of biofuels and biochemicals by in vitro synthetic biosystems: Opportunities and challenges
    • Zhang, Y. H. P. (2015). Production of biofuels and biochemicals by in vitro synthetic biosystems: opportunities and challenges. Biotechnol. Adv. 33, 1467-1483. doi: 10.1016/j.biotechadv.2014.10.009
    • (2015) Biotechnol. Adv , vol.33 , pp. 1467-1483
    • Zhang, Y.H.P.1
  • 137
    • 77954659025 scopus 로고    scopus 로고
    • Production and characterization of a recombinant beta-1,4-endoglucanase (Glycohydrolase family 9) from the termite Reticulitermes flavipes
    • Zhou, X., Kovaleva, E. S., Wu-Scharf, D., Campbell, J. H., Buchman, G. W., Boucias, D. G., et al. (2010). Production and characterization of a recombinant beta-1,4-endoglucanase (glycohydrolase family 9) from the termite Reticulitermes flavipes. Arch. Insect Biochem. Physiol. 74, 147-162. doi: 10.1002/arch.20368
    • (2010) Arch. Insect Biochem. Physiol , vol.74 , pp. 147-162
    • Zhou, X.1    Kovaleva, E.S.2    Wu-Scharf, D.3    Campbell, J.H.4    Buchman, G.W.5    Boucias, D.G.6
  • 138
    • 0035705385 scopus 로고    scopus 로고
    • Dramatic effects of truncation and sub-cellular targeting on the accumulation of recombinant microbial cellulase in tobacco
    • Ziegelhoffer, T., Raasch, J. A., and Austin-Phillips, S. (2001). Dramatic effects of truncation and sub-cellular targeting on the accumulation of recombinant microbial cellulase in tobacco. Mol. Breeding 8, 147-158. doi: 10.1023/A:1013338312948
    • (2001) Mol. Breeding , vol.8 , pp. 147-158
    • Ziegelhoffer, T.1    Raasch, J.A.2    Austin-Phillips, S.3
  • 139
    • 0032866269 scopus 로고    scopus 로고
    • Expression of bacterial cellulase genes in transgenic alfalfa (Medicago sativa L.), potato (Solanum tuberosum L.) and tobacco (Nicotiana tabacum L.)
    • Ziegelhoffer, T., Will, J., and Austin-Phillips, S. (1999). Expression of bacterial cellulase genes in transgenic alfalfa (Medicago sativa L.), potato (Solanum tuberosum L.) and tobacco (Nicotiana tabacum L.). Mol. Breeding 5, 309-318. doi: 10.1023/A:1009646830403
    • (1999) Mol. Breeding , vol.5 , pp. 309-318
    • Ziegelhoffer, T.1    Will, J.2    Austin-Phillips, S.3
  • 140
    • 0033996431 scopus 로고    scopus 로고
    • Accumulation of a thermostable endo-1,4-beta-D-glucanase in the apoplast of Arabidopsis thaliana leaves
    • Ziegler, M. T., Thomas, S. R., and Danna, K. J. (2000). Accumulation of a thermostable endo-1,4-beta-D-glucanase in the apoplast of Arabidopsis thaliana leaves. Mol Breeding 6, 37-46. doi:10.1023/A:1009667524690
    • (2000) Mol Breeding , vol.6 , pp. 37-46
    • Ziegler, M.T.1    Thomas, S.R.2    Danna, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.