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Volumn 2013, Issue , 2013, Pages

β -glucosidases from the fungus Trichoderma: An efficient cellulase machinery in biotechnological applications

Author keywords

[No Author keywords available]

Indexed keywords

BETA GLUCOSIDASE; BIOFUEL; CELLULASE; FUNGAL ENZYME;

EID: 84883184307     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/203735     Document Type: Article
Times cited : (82)

References (91)
  • 2
    • 0242405614 scopus 로고    scopus 로고
    • High-yield cellulase production by Trichoderma reesei ZU-02 on corn cob residue
    • 2-s2.0-0242405614 10.1016/S0960-8524(03)00195-0
    • Liming X., Xueliang S., High-yield cellulase production by Trichoderma reesei ZU-02 on corn cob residue. Bioresource Technology 2004 91 3 259 262 2-s2.0-0242405614 10.1016/S0960-8524(03)00195-0
    • (2004) Bioresource Technology , vol.91 , Issue.3 , pp. 259-262
    • Liming, X.1    Xueliang, S.2
  • 3
  • 4
    • 0025168749 scopus 로고
    • Molecular biology of cellulose degradation
    • 2-s2.0-0025168749
    • Béguin P., Molecular biology of cellulose degradation. Annual Review of Microbiology 1990 44 219 248 2-s2.0-0025168749
    • (1990) Annual Review of Microbiology , vol.44 , pp. 219-248
    • Béguin, P.1
  • 5
    • 0032838958 scopus 로고    scopus 로고
    • Purification and biochemical characteristics of β -D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus -SSBP
    • 2-s2.0-0032838958
    • Lin J., Pillay B., Singh S., Purification and biochemical characteristics of β -D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus -SSBP. Biotechnology and Applied Biochemistry 1999 30 1 81 87 2-s2.0-0032838958
    • (1999) Biotechnology and Applied Biochemistry , vol.30 , Issue.1 , pp. 81-87
    • Lin, J.1    Pillay, B.2    Singh, S.3
  • 6
    • 84966185447 scopus 로고
    • Synergism of cellulases from Trichoderma reesei in the degradation of cellulose
    • Henrissat B., Driguez H., Viet C., Synergism of cellulases from Trichoderma reesei in the degradation of cellulose. Biotechnology 1985 3 722 726
    • (1985) Biotechnology , vol.3 , pp. 722-726
    • Henrissat, B.1    Driguez, H.2    Viet, C.3
  • 7
    • 0014624087 scopus 로고
    • Purification and characterization of beta-glucosidase of Alcaligenes faecalis
    • 2-s2.0-0014624087
    • Han Y. W., Srinivasan V. R., Purification and characterization of beta-glucosidase of Alcaligenes faecalis. Journal of Bacteriology 1969 100 3 1355 1363 2-s2.0-0014624087
    • (1969) Journal of Bacteriology , vol.100 , Issue.3 , pp. 1355-1363
    • Han, Y.W.1    Srinivasan, V.R.2
  • 8
    • 0018082362 scopus 로고
    • Production, purification and partial characterization of 1,4- β -glucosidase enzymes from Sporotrichum pulverulentum
    • 2-s2.0-0018082362
    • Deshpande V., Eriksson K. E., Pettersson B., Production, purification and partial characterization of 1,4- β -glucosidase enzymes from Sporotrichum pulverulentum. European Journal of Biochemistry 1978 90 1 191 198 2-s2.0-0018082362
    • (1978) European Journal of Biochemistry , vol.90 , Issue.1 , pp. 191-198
    • Deshpande, V.1    Eriksson, K.E.2    Pettersson, B.3
  • 9
    • 0014040191 scopus 로고
    • Purification and characterization of yeast beta-glucosidases
    • 2-s2.0-0014040191
    • Fleming L. W., Duerksen J. D., Purification and characterization of yeast beta-glucosidases. Journal of Bacteriology 1967 93 1 135 141 2-s2.0-0014040191
    • (1967) Journal of Bacteriology , vol.93 , Issue.1 , pp. 135-141
    • Fleming, L.W.1    Duerksen, J.D.2
  • 10
    • 0041399496 scopus 로고
    • Almond-emulsin beta-D-glucosidase and beta-D-galactosidase
    • 2-s2.0-0041399496
    • Heyworth R., Walker P. G., Almond-emulsin beta-D-glucosidase and beta-D-galactosidase. The Biochemical Journal 1962 83 331 335 2-s2.0-0041399496
    • (1962) The Biochemical Journal , vol.83 , pp. 331-335
    • Heyworth, R.1    Walker, P.G.2
  • 11
    • 84883195418 scopus 로고    scopus 로고
    • Physico-kinetic and functional features of a novel β -glucosidase isolated from milk thistle (Silybum marianum Gaertn.) flower petals
    • 10.1007/s13562-013-0221-y
    • Mishra S. K., Sangwan N. S., Sangwan R. S., Physico-kinetic and functional features of a novel β -glucosidase isolated from milk thistle (Silybum marianum Gaertn.) flower petals. Journal of Plant Biochemistry and Biotechnology 2013 10.1007/s13562-013-0221-y
    • (2013) Journal of Plant Biochemistry and Biotechnology
    • Mishra, S.K.1    Sangwan, N.S.2    Sangwan, R.S.3
  • 12
    • 84876455651 scopus 로고    scopus 로고
    • Comparative physico-kinetic properties of a homogenous purified β -glucosidase from Withania somnifera leaf
    • Mishra S. K., Sangwan N. S., Sangwan R. S., Comparative physico-kinetic properties of a homogenous purified β -glucosidase from Withania somnifera leaf. Acta Physiologiae Plantarum 2013 35 1439 1451
    • (2013) Acta Physiologiae Plantarum , vol.35 , pp. 1439-1451
    • Mishra, S.K.1    Sangwan, N.S.2    Sangwan, R.S.3
  • 13
    • 84876368229 scopus 로고    scopus 로고
    • Purification and characterization of a gluconolactone inhibition-insensitive β -glucosidase from Andrographis paniculata nees. Leaf
    • 10.1080/10826068.2012.759966
    • Mishra S. K., Sangwan N. S., Sangwan R. S., Purification and characterization of a gluconolactone inhibition-insensitive β -glucosidase from Andrographis paniculata nees. leaf. Preparative Biochemistry and Biotechnology 2013 43 5 481 499 10.1080/10826068.2012.759966
    • (2013) Preparative Biochemistry and Biotechnology , vol.43 , Issue.5 , pp. 481-499
    • Mishra, S.K.1    Sangwan, N.S.2    Sangwan, R.S.3
  • 14
    • 0031436636 scopus 로고    scopus 로고
    • Cytosolic pyridoxine- β -D-glucoside hydrolase from porcine jejunal mucosa. Purification, properties, and comparison with broad specificity β - glucosidase
    • 2-s2.0-0031436636 10.1074/jbc.272.51.32025
    • McMahon L. G., Nakano H., Levy M.-D., Gregory J. F. III, Cytosolic pyridoxine- β -D-glucoside hydrolase from porcine jejunal mucosa. Purification, properties, and comparison with broad specificity β-glucosidase. Journal of Biological Chemistry 1997 272 51 32025 32033 2-s2.0-0031436636 10.1074/jbc.272.51.32025
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.51 , pp. 32025-32033
    • McMahon, L.G.1    Nakano, H.2    Levy, M.-D.3    Gregory III, J.F.4
  • 15
    • 0025957467 scopus 로고
    • Enzyme production by recombinant Trichoderma reesei strains
    • 2-s2.0-0025957467 10.1016/0168-1656(91)90025-Q
    • Uusitalo J. M., Nevalainen K. M. H., Harkki A. M., Knowles J. K. C., Penttila M. E., Enzyme production by recombinant Trichoderma reesei strains. Journal of Biotechnology 1991 17 1 35 49 2-s2.0-0025957467 10.1016/0168-1656(91) 90025-Q
    • (1991) Journal of Biotechnology , vol.17 , Issue.1 , pp. 35-49
    • Uusitalo, J.M.1    Nevalainen, K.M.H.2    Harkki, A.M.3    Knowles, J.K.C.4    Penttila, M.E.5
  • 16
    • 0017618890 scopus 로고
    • β Glucosidase: Microbial production and effect on enzymatic hydrolysis of cellulose
    • 2-s2.0-0017618890
    • Steinberg D., Vijayakumar P., Reese E. T., β Glucosidase: microbial production and effect on enzymatic hydrolysis of cellulose. Canadian Journal of Microbiology 1977 23 2 139 147 2-s2.0-0017618890
    • (1977) Canadian Journal of Microbiology , vol.23 , Issue.2 , pp. 139-147
    • Steinberg, D.1    Vijayakumar, P.2    Reese, E.T.3
  • 17
    • 0001790276 scopus 로고
    • Enzymatic hydrolysis of cellulose: Is the current theory of the mechanism of hydrolysis valid?
    • Enari T. M., Niku-Paavola M. L., Enzymatic hydrolysis of cellulose: is the current theory of the mechanism of hydrolysis valid? Critical Reviews in Biotechnology 1987 5 67 87
    • (1987) Critical Reviews in Biotechnology , vol.5 , pp. 67-87
    • Enari, T.M.1    Niku-Paavola, M.L.2
  • 18
    • 0031059628 scopus 로고    scopus 로고
    • Subsite structure of the β -glucosidase from Aspergillus niger, evaluated by steady-state kinetics with cello-oligosaccharides as substrates
    • 2-s2.0-0031059628 10.1016/S0008-6215(96)00287-X
    • Yazaki T., Ohnishi M., Rokushika S., Okada G., Subsite structure of the β -glucosidase from Aspergillus niger, evaluated by steady-state kinetics with cello-oligosaccharides as substrates. Carbohydrate Research 1997 298 1-2 51 57 2-s2.0-0031059628 10.1016/S0008-6215(96)00287-X
    • (1997) Carbohydrate Research , vol.298 , Issue.1-2 , pp. 51-57
    • Yazaki, T.1    Ohnishi, M.2    Rokushika, S.3    Okada, G.4
  • 19
    • 84883174414 scopus 로고    scopus 로고
    • The biotechnological perspective of beta-glucosidases
    • 10.1038/npre.2010.4945.1
    • Khan I., Akhtar M. W., The biotechnological perspective of beta-glucosidases. Nature Preceedings 2010 10.1038/npre.2010.4945.1
    • (2010) Nature Preceedings
    • Khan, I.1    Akhtar, M.W.2
  • 20
    • 0027738757 scopus 로고
    • Release of active cytokinin by a β -glucosidase localized to the maize root meristem
    • 2-s2.0-0027738757
    • Brzobohaty B., Moore I., Kristoffersen P., Bako L., Campos N., Schell J., Palme K., Release of active cytokinin by a β -glucosidase localized to the maize root meristem. Science 1993 262 5136 1051 1054 2-s2.0-0027738757
    • (1993) Science , vol.262 , Issue.5136 , pp. 1051-1054
    • Brzobohaty, B.1    Moore, I.2    Kristoffersen, P.3    Bako, L.4    Campos, N.5    Schell, J.6    Palme, K.7
  • 23
    • 0020099053 scopus 로고
    • Fungal and other β -d-glucosidases - Their properties and applications
    • 2-s2.0-0020099053
    • Woodward J., Wiseman A., Fungal and other β -d-glucosidases-their properties and applications. Enzyme and Microbial Technology 1982 4 2 73 79 2-s2.0-0020099053
    • (1982) Enzyme and Microbial Technology , vol.4 , Issue.2 , pp. 73-79
    • Woodward, J.1    Wiseman, A.2
  • 25
    • 0025187770 scopus 로고
    • Thermostable fungal β -glucosidases
    • 2-s2.0-0025187770
    • Stutzenberger F., Thermostable fungal β -glucosidases. Letters in Applied Microbiology 1990 11 4 173 178 2-s2.0-0025187770
    • (1990) Letters in Applied Microbiology , vol.11 , Issue.4 , pp. 173-178
    • Stutzenberger, F.1
  • 26
    • 0036448608 scopus 로고    scopus 로고
    • Microbial β -glucosidases: Cloning, properties, and applications
    • 2-s2.0-0036448608 10.1080/07388550290789568
    • Bhatia Y., Mishra S., Bisaria V. S., Microbial β -glucosidases: cloning, properties, and applications. Critical Reviews in Biotechnology 2002 22 4 375 407 2-s2.0-0036448608 10.1080/07388550290789568
    • (2002) Critical Reviews in Biotechnology , vol.22 , Issue.4 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 28
    • 84880955007 scopus 로고    scopus 로고
    • Biochemical and proteomic characterization of a novel extracellular β -glucosidase from Trichoderma citrinoviride
    • 2-s2.0-84858608559 10.1007/s12033-012-9526-7
    • Chandra M., Kalra A., Sangwan N. S., Sangwan R. S., Biochemical and proteomic characterization of a novel extracellular β -glucosidase from Trichoderma citrinoviride. Molecular Biotechnology 2013 53 289 299 2-s2.0-84858608559 10.1007/s12033-012-9526-7
    • (2013) Molecular Biotechnology , vol.53 , pp. 289-299
    • Chandra, M.1    Kalra, A.2    Sangwan, N.S.3    Sangwan, R.S.4
  • 30
    • 24944435502 scopus 로고    scopus 로고
    • An oligonucleotide barcode for species identification in Trichoderma and Hypocrea
    • 2-s2.0-24944435502 10.1016/j.fgb.2005.06.007
    • Druzhinina I. S., Kopchinskiy A. G., Komoń M., Bissett J., Szakacs G., Kubicek C. P., An oligonucleotide barcode for species identification in Trichoderma and Hypocrea. Fungal Genetics and Biology 2005 42 10 813 828 2-s2.0-24944435502 10.1016/j.fgb.2005.06.007
    • (2005) Fungal Genetics and Biology , vol.42 , Issue.10 , pp. 813-828
    • Druzhinina, I.S.1    Kopchinskiy, A.G.2    Komoń, M.3    Bissett, J.4    Szakacs, G.5    Kubicek, C.P.6
  • 31
    • 24944431722 scopus 로고    scopus 로고
    • TrichoBLAST: A multilocus database for Trichoderma and Hypocrea identifications
    • 2-s2.0-24944431722
    • Kopchinskiy A., Komoń M., Kubicek C. P., Druzhinina I. S., TrichoBLAST: a multilocus database for Trichoderma and Hypocrea identifications. Mycological Research 2005 109 6 658 660 2-s2.0-24944431722
    • (2005) Mycological Research , vol.109 , Issue.6 , pp. 658-660
    • Kopchinskiy, A.1    Komoń, M.2    Kubicek, C.P.3    Druzhinina, I.S.4
  • 32
    • 53649100300 scopus 로고    scopus 로고
    • Fungal genus Hypocrea/ Trichoderma: From barcodes to biodiversity
    • 2-s2.0-53649100300 10.1631/jzus.B0860015
    • Kubicek C. P., Komon-Zelazowska M., Druzhinina I. S., Fungal genus Hypocrea/ Trichoderma: from barcodes to biodiversity. Journal of Zhejiang University 2008 9 10 753 763 2-s2.0-53649100300 10.1631/jzus.B0860015
    • (2008) Journal of Zhejiang University , vol.9 , Issue.10 , pp. 753-763
    • Kubicek, C.P.1    Komon-Zelazowska, M.2    Druzhinina, I.S.3
  • 34
    • 77955660664 scopus 로고    scopus 로고
    • Biology and biotechnology of Trichoderma
    • 2-s2.0-77955660664 10.1007/s00253-010-2632-1
    • Schmoll M., Schuster A., Biology and biotechnology of Trichoderma. Applied Microbiology and Biotechnology 2010 87 3 787 799 2-s2.0-77955660664 10.1007/s00253-010-2632-1
    • (2010) Applied Microbiology and Biotechnology , vol.87 , Issue.3 , pp. 787-799
    • Schmoll, M.1    Schuster, A.2
  • 35
    • 84868600048 scopus 로고    scopus 로고
    • Mutations in the substrate entrance region of β -glucosidase from Trichoderma reesei improve enzyme activity and thermostability
    • Lee H. L., Chang C. K., Jeng W. Y., Mutations in the substrate entrance region of β -glucosidase from Trichoderma reesei improve enzyme activity and thermostability. Protein Engineering, Design and Selection 2012 25 11 733 740
    • (2012) Protein Engineering, Design and Selection , vol.25 , Issue.11 , pp. 733-740
    • Lee, H.L.1    Chang, C.K.2    Jeng, W.Y.3
  • 36
    • 78649905870 scopus 로고    scopus 로고
    • Structural and functional analysis of three β -glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis
    • 2-s2.0-78649905870 10.1016/j.jsb.2010.07.008
    • Jeng W.-Y., Wang N.-C., Lin M.-H., Lin C.-T., Liaw Y.-C., Chang W.-J., Liu C.-I., Liang P.-H., Wang A. H.-J., Structural and functional analysis of three β -glucosidases from bacterium Clostridium cellulovorans, fungus Trichoderma reesei and termite Neotermes koshunensis. Journal of Structural Biology 2011 173 1 46 56 2-s2.0-78649905870 10.1016/j.jsb.2010.07.008
    • (2011) Journal of Structural Biology , vol.173 , Issue.1 , pp. 46-56
    • Jeng, W.-Y.1    Wang, N.-C.2    Lin, M.-H.3    Lin, C.-T.4    Liaw, Y.-C.5    Chang, W.-J.6    Liu, C.-I.7    Liang, P.-H.8    Wang, A.H.-J.9
  • 37
    • 84861163349 scopus 로고    scopus 로고
    • Overexpression of an exotic thermotolerant β -glucosidase in Trichoderma reesei and its significant increase in cellulolytic activity and saccharification of barley straw
    • Dashtban M., Qin W., Overexpression of an exotic thermotolerant β -glucosidase in Trichoderma reesei and its significant increase in cellulolytic activity and saccharification of barley straw. Microbial Cell Factories 2012 11 63 1 15
    • (2012) Microbial Cell Factories , vol.11 , Issue.63 , pp. 1-15
    • Dashtban, M.1    Qin, W.2
  • 39
    • 81255136050 scopus 로고    scopus 로고
    • Expression of a secretory β -glucosidase from Trichoderma reesei in Pichia pastoris and its characterization
    • 2-s2.0-81255136050 10.1007/s10529-011-0724-3
    • Chen P., Fu X., Ng T. B., Ye X.-Y., Expression of a secretory β -glucosidase from Trichoderma reesei in Pichia pastoris and its characterization. Biotechnology Letters 2011 33 12 2475 2479 2-s2.0-81255136050 10.1007/s10529-011-0724-3
    • (2011) Biotechnology Letters , vol.33 , Issue.12 , pp. 2475-2479
    • Chen, P.1    Fu, X.2    Ng, T.B.3    Ye, X.-Y.4
  • 40
    • 8844286155 scopus 로고    scopus 로고
    • Expression in Trichoderma reesei and characterisation of a thermostable family 3 β -glucosidase from the moderately thermophilic fungus Talaromyces emersonii
    • 2-s2.0-8844286155 10.1016/j.pep.2004.08.006
    • Murray P., Aro N., Collins C., Grassick A., Penttilä M., Saloheimo M., Tuohy M., Expression in Trichoderma reesei and characterisation of a thermostable family 3 β -glucosidase from the moderately thermophilic fungus Talaromyces emersonii. Protein Expression and Purification 2004 38 2 248 257 2-s2.0-8844286155 10.1016/j.pep.2004.08.006
    • (2004) Protein Expression and Purification , vol.38 , Issue.2 , pp. 248-257
    • Murray, P.1    Aro, N.2    Collins, C.3    Grassick, A.4    Penttilä, M.5    Saloheimo, M.6    Tuohy, M.7
  • 41
    • 0036729340 scopus 로고    scopus 로고
    • Enzymatic properties and intracellular localization of the novel Trichoderma reesei β -glucosidase BGLII (Cel1A)
    • 2-s2.0-0036729340 10.1128/AEM.68.9.4546-4553.2002
    • Saloheimo M., Kuja-Panula J., Ylösmäki E., Ward M., Penttilä M., Enzymatic properties and intracellular localization of the novel Trichoderma reesei β -glucosidase BGLII (Cel1A). Applied and Environmental Microbiology 2002 68 9 4546 4553 2-s2.0-0036729340 10.1128/AEM.68.9.4546-4553.2002
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.9 , pp. 4546-4553
    • Saloheimo, M.1    Kuja-Panula, J.2    Ylösmäki, E.3    Ward, M.4    Penttilä, M.5
  • 42
    • 0035460654 scopus 로고    scopus 로고
    • Purification and some properties of a β -glucosidase from Trichoderma harzianum type C-4
    • 2-s2.0-0035460654 10.1271/bbb.65.2028
    • Yun S.-I., Jeong C.-S., Chung D.-K., Choi H.-S., Purification and some properties of a β -glucosidase from Trichoderma harzianum type C-4. Bioscience, Biotechnology and Biochemistry 2001 65 9 2028 2032 2-s2.0-0035460654 10.1271/bbb.65.2028
    • (2001) Bioscience, Biotechnology and Biochemistry , vol.65 , Issue.9 , pp. 2028-2032
    • Yun, S.-I.1    Jeong, C.-S.2    Chung, D.-K.3    Choi, H.-S.4
  • 43
    • 0032937042 scopus 로고    scopus 로고
    • Molecular cloning and expression of the novel fungal β -glucosidase genes from Humicola grisea and Trichoderma reesei
    • 2-s2.0-0032937042
    • Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T., Molecular cloning and expression of the novel fungal β -glucosidase genes from Humicola grisea and Trichoderma reesei. Journal of Biochemistry 1999 125 4 728 736 2-s2.0-0032937042
    • (1999) Journal of Biochemistry , vol.125 , Issue.4 , pp. 728-736
    • Takashima, S.1    Nakamura, A.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 44
    • 0028055658 scopus 로고
    • Purification, characterization, and synergistic activity of a glucan 1,3-beta-glucosidase and an N-acetyl-beta-glucosaminidase from Trichoderma harzianum
    • 2-s2.0-0028055658
    • Lorito M., Hayes C. K., Di Pietro A., Woo S. L., Harman G. E., Purification, characterization, and synergistic activity of a glucan 1,3-beta-glucosidase and an N-acetyl-beta-glucosaminidase from Trichoderma harzianum. Phytopathology 1994 84 4 398 405 2-s2.0-0028055658
    • (1994) Phytopathology , vol.84 , Issue.4 , pp. 398-405
    • Lorito, M.1    Hayes, C.K.2    Di Pietro, A.3    Woo, S.L.4    Harman, G.E.5
  • 45
    • 0023273547 scopus 로고
    • Purification and characterization of a β -glucosidase from Trichoderma reesei
    • 2-s2.0-0023273547
    • Chirico W. J., Brown R. D. Jr., Purification and characterization of a β -glucosidase from Trichoderma reesei. European Journal of Biochemistry 1987 165 2 333 341 2-s2.0-0023273547
    • (1987) European Journal of Biochemistry , vol.165 , Issue.2 , pp. 333-341
    • Chirico, W.J.1    Brown Jr., R.D.2
  • 46
    • 0022425315 scopus 로고
    • The cellulase of Trichoderma viride. Purification, characterization and comparison of all detectable endoglucanases, exoglucanases and beta-glucosidases
    • 2-s2.0-0022425315
    • Beldman G., Searle-Van Leeuwen M. F., Rombouts F. M., Voragen F. G., The cellulase of Trichoderma viride. Purification, characterization and comparison of all detectable endoglucanases, exoglucanases and beta-glucosidases. European Journal of Biochemistry 1985 146 2 301 308 2-s2.0-0022425315
    • (1985) European Journal of Biochemistry , vol.146 , Issue.2 , pp. 301-308
    • Beldman, G.1    Searle-Van Leeuwen, M.F.2    Rombouts, F.M.3    Voragen, F.G.4
  • 47
    • 84883178098 scopus 로고    scopus 로고
    • http://www.cazy.org/
  • 48
    • 0033081517 scopus 로고    scopus 로고
    • Three-dimensional structure of a barley β -D-glucan exohydrolase, a family 3 glycosyl hydrolase
    • 2-s2.0-0033081517 10.1016/S0969-2126(99)80024-0
    • Varghese J. N., Hrmova M., Fincher G. B., Three-dimensional structure of a barley β -D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure 1999 7 2 179 190 2-s2.0-0033081517 10.1016/S0969-2126(99)80024-0
    • (1999) Structure , vol.7 , Issue.2 , pp. 179-190
    • Varghese, J.N.1    Hrmova, M.2    Fincher, G.B.3
  • 50
    • 0035314098 scopus 로고    scopus 로고
    • Mechanisms of glycosyl transferases and hydrolases
    • 2-s2.0-0035314098 10.1016/S0144-8617(00)00249-6
    • Withers S. G., Mechanisms of glycosyl transferases and hydrolases. Carbohydrate Polymers 2001 44 4 325 337 2-s2.0-0035314098 10.1016/S0144-8617(00) 00249-6
    • (2001) Carbohydrate Polymers , vol.44 , Issue.4 , pp. 325-337
    • Withers, S.G.1
  • 51
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • 2-s2.0-0030733350 10.1016/S0959-440X(97)80072-3
    • Henrissat B., Davies G., Structural and sequence-based classification of glycoside hydrolases. Current Opinion in Structural Biology 1997 7 5 637 644 2-s2.0-0030733350 10.1016/S0959-440X(97)80072-3
    • (1997) Current Opinion in Structural Biology , vol.7 , Issue.5 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 52
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β -glucosidase from Aspergillus oryzae
    • 2-s2.0-0031685554
    • Riou C., Salmon J.-M., Vallier M.-J., Günata Z., Barre P., Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β -glucosidase from Aspergillus oryzae. Applied and Environmental Microbiology 1998 64 10 3607 3614 2-s2.0-0031685554
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.10 , pp. 3607-3614
    • Riou, C.1    Salmon, J.-M.2    Vallier, M.-J.3    Günata, Z.4    Barre, P.5
  • 53
    • 84946481369 scopus 로고    scopus 로고
    • β -Glucosidases from filamentous fungi: Properties, structure, and applications
    • CRC Taylor and Francis group
    • Eyzaguirre J., Hidalgo M., Leschot A., β -Glucosidases from filamentous fungi: properties, structure, and applications. Handbook of Carbohydrate Engineering 2005 CRC Taylor and Francis group
    • (2005) Handbook of Carbohydrate Engineering
    • Eyzaguirre, J.1    Hidalgo, M.2    Leschot, A.3
  • 54
    • 0028171629 scopus 로고
    • Characterisation of a β -D-glucosidase from the anaerobic rumen fungus Neocallimastix frontalis with particular reference to attack on cello-oligosaccharides
    • 2-s2.0-0028171629 10.1016/0168-1656(94)90129-5
    • Wilson C. A., McCrae S. I., Wood T. M., Characterisation of a β -D-glucosidase from the anaerobic rumen fungus Neocallimastix frontalis with particular reference to attack on cello-oligosaccharides. Journal of Biotechnology 1994 37 3 217 227 2-s2.0-0028171629 10.1016/0168-1656(94)90129-5
    • (1994) Journal of Biotechnology , vol.37 , Issue.3 , pp. 217-227
    • Wilson, C.A.1    McCrae, S.I.2    Wood, T.M.3
  • 55
    • 0021925730 scopus 로고
    • Extracellular enzymes of Phytophthora infestans: Endo-cellulase, β -glucosidases, and 1,3- β -glucanases
    • 2-s2.0-0021925730
    • Bodenmann J., Heiniger U., Hohl H. R., Extracellular enzymes of Phytophthora infestans: endo-cellulase, β -glucosidases, and 1,3- β -glucanases. Canadian Journal of Microbiology 1985 31 1 75 82 2-s2.0-0021925730
    • (1985) Canadian Journal of Microbiology , vol.31 , Issue.1 , pp. 75-82
    • Bodenmann, J.1    Heiniger, U.2    Hohl, H.R.3
  • 56
    • 0017816271 scopus 로고
    • Purification and properties of an induced β -D-glucosidase from Stachybotrys atra
    • 2-s2.0-0017816271
    • De Gussem R. L., Aerts G. M., Claeyssens M., De Bruyne C. K., Purification and properties of an induced β -D-glucosidase from Stachybotrys atra. Biochimica et Biophysica Acta 1978 525 1 142 153 2-s2.0-0017816271
    • (1978) Biochimica et Biophysica Acta , vol.525 , Issue.1 , pp. 142-153
    • De Gussem, R.L.1    Aerts, G.M.2    Claeyssens, M.3    De Bruyne, C.K.4
  • 57
    • 85007860310 scopus 로고
    • High recovery purification and some properties of a β -glucosidase from Aspergillus niger
    • Unno T., Ide K., Yazaki T., High recovery purification and some properties of a β -glucosidase from Aspergillus niger. Bioscience Biotechnology and Biochemistry 1993 57 2172 2173
    • (1993) Bioscience Biotechnology and Biochemistry , vol.57 , pp. 2172-2173
    • Unno, T.1    Ide, K.2    Yazaki, T.3
  • 58
    • 85004246138 scopus 로고
    • Purification and properties of two β -glucosidases from Penicillium herquei Banier and Sartory
    • Funaguma T., Hara A., Purification and properties of two β -glucosidases from Penicillium herquei Banier and Sartory. Agricultural and Biological Chemistry 1988 52 749 755
    • (1988) Agricultural and Biological Chemistry , vol.52 , pp. 749-755
    • Funaguma, T.1    Hara, A.2
  • 59
    • 0020400010 scopus 로고
    • Purification and some properties of the extracellular β -d-glucosidase of the cellulolytic fungus Trichoderma koningii
    • 2-s2.0-0020400010
    • Wood T. M., McCrae S. I., Purification and some properties of the extracellular β -d-glucosidase of the cellulolytic fungus Trichoderma koningii. Journal of General Microbiology 1982 128 12 2973 2982 2-s2.0-0020400010
    • (1982) Journal of General Microbiology , vol.128 , Issue.12 , pp. 2973-2982
    • Wood, T.M.1    McCrae, S.I.2
  • 60
    • 0015816336 scopus 로고
    • Glycoprotein enzymes secreted by Aspergillus fumigatus. Purification and properties of β glucosidase
    • 2-s2.0-0015816336
    • Rudick M. J., Elbein A. D., Glycoprotein enzymes secreted by Aspergillus fumigatus. Purification and properties of β glucosidase. Journal of Biological Chemistry 1973 248 18 6506 6513 2-s2.0-0015816336
    • (1973) Journal of Biological Chemistry , vol.248 , Issue.18 , pp. 6506-6513
    • Rudick, M.J.1    Elbein, A.D.2
  • 61
    • 0023421236 scopus 로고
    • Purification and partial characterization of a cellodextrin glucohydrolase (β -glucosidase) from Trichoderma reesei strain QM9414
    • 2-s2.0-0023421236
    • Schmid G., Wandrey C., Purification and partial characterization of a cellodextrin glucohydrolase (β -glucosidase) from Trichoderma reesei strain QM9414. Biotechnology and Bioengineering 1987 30 4 571 585 2-s2.0-0023421236
    • (1987) Biotechnology and Bioengineering , vol.30 , Issue.4 , pp. 571-585
    • Schmid, G.1    Wandrey, C.2
  • 62
    • 0019841342 scopus 로고
    • The cellulolytic system of Talaromyces emersonii. Purification and characterization of the extracellular and intracellular β -glucosidases
    • 2-s2.0-0019841342
    • McHale A., Coughlan M. P., The cellulolytic system of Talaromyces emersonii. Purification and characterization of the extracellular and intracellular β -glucosidases. Biochimica et Biophysica Acta 1981 662 1 152 159 2-s2.0-0019841342
    • (1981) Biochimica et Biophysica Acta , vol.662 , Issue.1 , pp. 152-159
    • McHale, A.1    Coughlan, M.P.2
  • 63
    • 84860491834 scopus 로고
    • Relationship between carbohydrate moiety and thermostability of β -glucosidase from Mucor miehei YH-10
    • Yoshioka H., Hayashida S., Relationship between carbohydrate moiety and thermostability of β -glucosidase from Mucor miehei YH-10. Agricultural and Biological Chemistry 1981 45 571 577
    • (1981) Agricultural and Biological Chemistry , vol.45 , pp. 571-577
    • Yoshioka, H.1    Hayashida, S.2
  • 64
    • 0032176017 scopus 로고    scopus 로고
    • Purification and characterization of extracellular and cell wall bound β -glucosidases from Aspergillus kawachii
    • 2-s2.0-0032176017
    • Iwashita K., Todoroki K., Kimura H., Shimoi H., Ito K., Purification and characterization of extracellular and cell wall bound β -glucosidases from Aspergillus kawachii. Bioscience, Biotechnology and Biochemistry 1998 62 10 1938 1946 2-s2.0-0032176017
    • (1998) Bioscience, Biotechnology and Biochemistry , vol.62 , Issue.10 , pp. 1938-1946
    • Iwashita, K.1    Todoroki, K.2    Kimura, H.3    Shimoi, H.4    Ito, K.5
  • 65
    • 0000091593 scopus 로고
    • Nojirimycin and d-glucono-1,5-lactone as inhibitors of carbohydrases
    • 2-s2.0-0000091593
    • Reese E. T., Parrish F. W., Ettlinger M., Nojirimycin and d-glucono-1,5-lactone as inhibitors of carbohydrases. Carbohydrate Research 1971 18 3 381 388 2-s2.0-0000091593
    • (1971) Carbohydrate Research , vol.18 , Issue.3 , pp. 381-388
    • Reese, E.T.1    Parrish, F.W.2    Ettlinger, M.3
  • 66
    • 0026206044 scopus 로고
    • Purification and characterization of an extracellular β -glucosidase from the rumen fungus Neocallimastix frontalis EB188
    • 2-s2.0-0026206044 10.1016/0141-0229(91)90075-L
    • Li X., Calza R. E., Purification and characterization of an extracellular β -glucosidase from the rumen fungus Neocallimastix frontalis EB188. Enzyme and Microbial Technology 1991 13 8 622 628 2-s2.0-0026206044 10.1016/0141-0229(91)90075-L
    • (1991) Enzyme and Microbial Technology , vol.13 , Issue.8 , pp. 622-628
    • Li, X.1    Calza, R.E.2
  • 67
    • 0041084347 scopus 로고
    • Mechanism for β -glucosidase release into cellulose-grown Trichoderma reesei culture supernatants
    • 2-s2.0-0041084347
    • Jackson M. A., Talburt D. E., Mechanism for β -glucosidase release into cellulose-grown Trichoderma reesei culture supernatants. Experimental Mycology 1988 12 2 203 216 2-s2.0-0041084347
    • (1988) Experimental Mycology , vol.12 , Issue.2 , pp. 203-216
    • Jackson, M.A.1    Talburt, D.E.2
  • 68
    • 0020415037 scopus 로고
    • Localization and release mechanism of cellulases in Trichoderma reesei QM 9414
    • Nanda M., Bisaria V. S., Ghose T. K., Localization and release mechanism of cellulases in Trichoderma reesei QM 9414. Canadian Journal of Microbiology 1982 4 10 633 638
    • (1982) Canadian Journal of Microbiology , vol.4 , Issue.10 , pp. 633-638
    • Nanda, M.1    Bisaria, V.S.2    Ghose, T.K.3
  • 69
    • 0023269485 scopus 로고
    • Involvement of a conidial endoglucanase and a plasma-membrane-bound β -glucosidase in the induction of endoglucanase synthesis by cellulose in Trichoderma reesei
    • 2-s2.0-0023269485
    • Kubicek C. P., Involvement of a conidial endoglucanase and a plasma-membrane-bound β -glucosidase in the induction of endoglucanase synthesis by cellulose in Trichoderma reesei. Journal of General Microbiology 1987 133 6 1481 1487 2-s2.0-0023269485
    • (1987) Journal of General Microbiology , vol.133 , Issue.6 , pp. 1481-1487
    • Kubicek, C.P.1
  • 70
    • 0018980548 scopus 로고
    • Partial purification and characterization of a new intracellular beta-glucosidase of Trichoderma reesei
    • 2-s2.0-0018980548
    • Inglin M., Feinberg B. A., Loewenberg J. R., Partial purification and characterization of a new intracellular beta-glucosidase of Trichoderma reesei. Biochemical Journal 1980 185 2 515 519 2-s2.0-0018980548
    • (1980) Biochemical Journal , vol.185 , Issue.2 , pp. 515-519
    • Inglin, M.1    Feinberg, B.A.2    Loewenberg, J.R.3
  • 71
    • 0019098120 scopus 로고
    • The adaptability, purification and properties of exo-beta 1,3-glucanase from the fungus Trichoderma reesei
    • 2-s2.0-0019098120
    • Bamforth C. W., The adaptability, purification and properties of exo-beta 1,3-glucanase from the fungus Trichoderma reesei. Biochemical Journal 1980 191 3 863 866 2-s2.0-0019098120
    • (1980) Biochemical Journal , vol.191 , Issue.3 , pp. 863-866
    • Bamforth, C.W.1
  • 72
    • 44149103853 scopus 로고    scopus 로고
    • Trichoderma atroviride mutants with enhanced production of cellulase and β -glucosidase on pretreated willow
    • 2-s2.0-44149103853 10.1016/j.enzmictec.2008.02.006
    • Kovács K., Megyeri L., Szakacs G., Kubicek C. P., Galbe M., Zacchi G., Trichoderma atroviride mutants with enhanced production of cellulase and β -glucosidase on pretreated willow. Enzyme and Microbial Technology 2008 43 1 48 55 2-s2.0-44149103853 10.1016/j.enzmictec.2008.02.006
    • (2008) Enzyme and Microbial Technology , vol.43 , Issue.1 , pp. 48-55
    • Kovács, K.1    Megyeri, L.2    Szakacs, G.3    Kubicek, C.P.4    Galbe, M.5    Zacchi, G.6
  • 73
    • 0016638184 scopus 로고
    • Enzymatic studies on a cellulase system of Trichoderma viride - II. Purification and properties of two cellulases
    • 2-s2.0-0016638184
    • Okada G., Enzymatic studies on a cellulase system of Trichoderma viride-II. Purification and properties of two cellulases. Journal of Biochemistry 1975 77 1 33 42 2-s2.0-0016638184
    • (1975) Journal of Biochemistry , vol.77 , Issue.1 , pp. 33-42
    • Okada, G.1
  • 74
    • 67049087954 scopus 로고    scopus 로고
    • Application of Trichoderma reesei cellulase and xylanase promoters through homologous recombination for enhanced production of extracellular β -glucosidase i
    • 2-s2.0-67049087954 10.1271/bbb.80852
    • Rahman Z., Shida Y., Furukawa T., Suzuki Y., Okada H., Ogasawara W., Morikawa Y., Application of Trichoderma reesei cellulase and xylanase promoters through homologous recombination for enhanced production of extracellular β -glucosidase i. Bioscience, Biotechnology and Biochemistry 2009 73 5 1083 1089 2-s2.0-67049087954 10.1271/bbb.80852
    • (2009) Bioscience, Biotechnology and Biochemistry , vol.73 , Issue.5 , pp. 1083-1089
    • Rahman, Z.1    Shida, Y.2    Furukawa, T.3    Suzuki, Y.4    Okada, H.5    Ogasawara, W.6    Morikawa, Y.7
  • 75
    • 67650469491 scopus 로고    scopus 로고
    • Genetic modification of carbon catabolite repression in Trichoderma reesei for improved protein production
    • 2-s2.0-67650469491 10.1128/AEM.00282-09
    • Nakari-Setälä T., Paloheimo M., Kallio J., Vehmaanperä J., Penttilä M., Saloheimo M., Genetic modification of carbon catabolite repression in Trichoderma reesei for improved protein production. Applied and Environmental Microbiology 2009 75 14 4853 4860 2-s2.0-67650469491 10.1128/AEM.00282-09
    • (2009) Applied and Environmental Microbiology , vol.75 , Issue.14 , pp. 4853-4860
    • Nakari-Setälä, T.1    Paloheimo, M.2    Kallio, J.3    Vehmaanperä, J.4    Penttilä, M.5    Saloheimo, M.6
  • 76
    • 77952993064 scopus 로고    scopus 로고
    • Determination of product inhibition of CBH1, CBH2, and EG1 using a novel cellulase activity assay
    • 2-s2.0-77952993064 10.1007/s12010-009-8796-4
    • Du F., Wolger E., Wallace L., Liu A., Kaper T., Kelemen B., Determination of product inhibition of CBH1, CBH2, and EG1 using a novel cellulase activity assay. Applied Biochemistry and Biotechnology 2010 161 313 317 2-s2.0-77952993064 10.1007/s12010-009-8796-4
    • (2010) Applied Biochemistry and Biotechnology , vol.161 , pp. 313-317
    • Du, F.1    Wolger, E.2    Wallace, L.3    Liu, A.4    Kaper, T.5    Kelemen, B.6
  • 77
    • 34249809704 scopus 로고    scopus 로고
    • Optimization of enzyme complexes for lignocellulose hydrolysis
    • 2-s2.0-34249809704 10.1002/bit.21238
    • Berlin A., Maximenko V., Gilkes N., Saddler J., Optimization of enzyme complexes for lignocellulose hydrolysis. Biotechnology and Bioengineering 2007 97 2 287 296 2-s2.0-34249809704 10.1002/bit.21238
    • (2007) Biotechnology and Bioengineering , vol.97 , Issue.2 , pp. 287-296
    • Berlin, A.1    Maximenko, V.2    Gilkes, N.3    Saddler, J.4
  • 78
    • 36549070666 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of maize straw polysaccharides for the production of reducing sugars
    • 2-s2.0-36549070666 10.1016/j.carbpol.2007.06.011
    • Chen M., Zhao J., Xia L., Enzymatic hydrolysis of maize straw polysaccharides for the production of reducing sugars. Carbohydrate Polymers 2008 71 3 411 415 2-s2.0-36549070666 10.1016/j.carbpol.2007.06.011
    • (2008) Carbohydrate Polymers , vol.71 , Issue.3 , pp. 411-415
    • Chen, M.1    Zhao, J.2    Xia, L.3
  • 79
    • 56249108086 scopus 로고    scopus 로고
    • Development of a mutant of Trichoderma citrinoviride for enhanced production of cellulases
    • 2-s2.0-56249108086 10.1016/j.biortech.2008.09.011
    • Chandra M., Kalra A., Sangwan N. S., Gaurav S. S., Darokar M. P., Sangwan R. S., Development of a mutant of Trichoderma citrinoviride for enhanced production of cellulases. Bioresource Technology 2009 100 4 1659 1662 2-s2.0-56249108086 10.1016/j.biortech.2008.09.011
    • (2009) Bioresource Technology , vol.100 , Issue.4 , pp. 1659-1662
    • Chandra, M.1    Kalra, A.2    Sangwan, N.S.3    Gaurav, S.S.4    Darokar, M.P.5    Sangwan, R.S.6
  • 80
  • 81
    • 0024352613 scopus 로고
    • Regulatory aspects of cellulase biosynthesis and secretion
    • 2-s2.0-0024352613
    • Bisaria V. S., Mishra S., Regulatory aspects of cellulase biosynthesis and secretion. Critical reviews in biotechnology 1989 9 2 61 103 2-s2.0-0024352613
    • (1989) Critical Reviews in Biotechnology , vol.9 , Issue.2 , pp. 61-103
    • Bisaria, V.S.1    Mishra, S.2
  • 83
    • 0025236339 scopus 로고
    • Therapeutic response to intravenous infusions of glucocerebrosidase in patients with Gauchers disease
    • Barton N. W., Furbish F. S., Murray G. T., Therapeutic response to intravenous infusions of glucocerebrosidase in patients with Gauchers disease. Proceedings of the National Academy of Sciences USA 1990 87 1913 1916
    • (1990) Proceedings of the National Academy of Sciences USA , vol.87 , pp. 1913-1916
    • Barton, N.W.1    Furbish, F.S.2    Murray, G.T.3
  • 84
    • 84870952001 scopus 로고    scopus 로고
    • Role and significance of beta glucosidases in the hydrolysis of cellulose for bioethanol production
    • 10.1016/j.biortech.2012.09.012
    • Singhania R. R., Patel A. K., Sukumaran R. K., Role and significance of beta glucosidases in the hydrolysis of cellulose for bioethanol production. Bioresource Technology 2013 127 500 507 10.1016/j.biortech.2012.09.012
    • (2013) Bioresource Technology , vol.127 , pp. 500-507
    • Singhania, R.R.1    Patel, A.K.2    Sukumaran, R.K.3
  • 85
    • 22544449588 scopus 로고    scopus 로고
    • Production of cellulase/ β -glucosidase by the mixed fungi culture Trichoderma reesei and Aspergillus phoenicis on dairy manure
    • 2-s2.0-22544449588 10.1016/j.procbio.2005.03.044
    • Wen Z., Liao W., Chen S., Production of cellulase/ β -glucosidase by the mixed fungi culture Trichoderma reesei and Aspergillus phoenicis on dairy manure. Process Biochemistry 2005 40 9 3087 3094 2-s2.0-22544449588 10.1016/j.procbio.2005.03.044
    • (2005) Process Biochemistry , vol.40 , Issue.9 , pp. 3087-3094
    • Wen, Z.1    Liao, W.2    Chen, S.3
  • 86
    • 70350774098 scopus 로고    scopus 로고
    • Enzymatic hydrolysis and simultaneous saccharification and fermentation of steam-pretreated spruce using crude Trichoderma reesei and Trichoderma atroviride enzymes
    • 2-s2.0-70350774098 10.1016/j.procbio.2009.07.006
    • Kovács K., Szakács G., Zacchi G., Enzymatic hydrolysis and simultaneous saccharification and fermentation of steam-pretreated spruce using crude Trichoderma reesei and Trichoderma atroviride enzymes. Process Biochemistry 2009 44 12 1323 1329 2-s2.0-70350774098 10.1016/j.procbio.2009.07. 006
    • (2009) Process Biochemistry , vol.44 , Issue.12 , pp. 1323-1329
    • Kovács, K.1    Szakács, G.2    Zacchi, G.3
  • 87
    • 63049127683 scopus 로고    scopus 로고
    • Cellulase production by six Trichoderma spp. Fermented on medicinal plant processings
    • 2-s2.0-63049127683 10.1007/s10295-009-0544-9
    • Chandra M., Kalra A., Sharma P. K., Sangwan R. S., Cellulase production by six Trichoderma spp. fermented on medicinal plant processings. Journal of Industrial Microbiology and Biotechnology 2009 36 4 605 609 2-s2.0-63049127683 10.1007/s10295-009-0544-9
    • (2009) Journal of Industrial Microbiology and Biotechnology , vol.36 , Issue.4 , pp. 605-609
    • Chandra, M.1    Kalra, A.2    Sharma, P.K.3    Sangwan, R.S.4
  • 88
    • 77951024585 scopus 로고    scopus 로고
    • Optimization of cellulases production by Trichoderma citrinoviride on marc of Artemisia annua and its application for bioconversion process
    • 2-s2.0-77951024585 10.1016/j.biombioe.2010.01.024
    • Chandra M., Kalra A., Sharma P. K., Kumar H., Sangwan R. S., Optimization of cellulases production by Trichoderma citrinoviride on marc of Artemisia annua and its application for bioconversion process. Biomass and Bioenergy 2010 34 5 805 811 2-s2.0-77951024585 10.1016/j.biombioe.2010.01.024
    • (2010) Biomass and Bioenergy , vol.34 , Issue.5 , pp. 805-811
    • Chandra, M.1    Kalra, A.2    Sharma, P.K.3    Kumar, H.4    Sangwan, R.S.5
  • 89
    • 0000729326 scopus 로고
    • Enhanced production of cellulase, hemicellulase, and β -Glucosidase by Trichoderma reesei (Rut C-30)
    • Tangnu S. K., Blanch H. W., Wilke C. R., Enhanced production of cellulase, hemicellulase, and β -Glucosidase by Trichoderma reesei (Rut C-30). Biotechnology and Bioengineering 1981 23 1837 1849
    • (1981) Biotechnology and Bioengineering , vol.23 , pp. 1837-1849
    • Tangnu, S.K.1    Blanch, H.W.2    Wilke, C.R.3
  • 90
    • 84883160194 scopus 로고    scopus 로고
    • http://www.genencor.com/
  • 91
    • 84883201508 scopus 로고    scopus 로고
    • http://www.novozymes.com/


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