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Volumn 14, Issue 4, 2009, Pages 457-466

Extracellular β-glucosidase production by a marine Aspergillus sydowii BTMFS 55 under solid state fermentation using statistical experimental design

Author keywords

glucosidase; Aspergillus sydowii; Plackett Burman; SSF; Wheat bran

Indexed keywords

ASPERGILLUS SYDOWII; EXTRACELLULAR; FUNGAL STRAINS; GENBANK; GLUCOSIDASE; GROWTH MEDIUM; HIGH AFFINITY; ION EXCHANGE CHROMATOGRAPHY; LOW CONCENTRATIONS; MEDIUM COMPONENTS; MOISTURE CONTENTS; MOLECULAR APPROACH; MONOMERIC PROTEINS; PLACKETT-BURMAN; RDNA SEQUENCE; RICE STRAWS; SACCHAROMYCES CEREVISIAE; SDS-PAGE; SEQUENTIAL OPTIMIZATION; SIGNIFICANT FACTORS; SOLID-STATE FERMENTATION; SSF; STATISTICAL EXPERIMENTAL DESIGN; WHEAT BRAN;

EID: 70349636182     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12257-008-0116-2     Document Type: Article
Times cited : (19)

References (50)
  • 1
    • 20444378957 scopus 로고    scopus 로고
    • Structural and biochemical studies of GH family 12 cellulases: Improved thermal stability and ligand complexes
    • Sandgrena, M., J. Stahlbergb, and C. Mitchinson (2005) Structural and biochemical studies of GH family 12 cellulases: Improved thermal stability and ligand complexes. Prog. Biophy. Mol. Biol. 89: 246-291.
    • (2005) Prog. Biophy. Mol. Biol. , vol.89 , pp. 246-291
    • Sandgrena, M.1    Stahlbergb, J.2    Mitchinson, C.3
  • 2
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-Gluco sidase from Aspergillus oryzae
    • Riou, C., J. M. Salmon, M. J. Vallier, Z. Gunata, and P. Barre (1998) Purification, characterization, and substrate specificity of a novel highly glucose-tolerant β-Gluco sidase from Aspergillus oryzae. Appl. Environ. Microbol. 64: 3607-3614.
    • (1998) Appl. Environ. Microbol. , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.M.2    Vallier, M.J.3    Gunata, Z.4    Barre, P.5
  • 3
    • 10044225564 scopus 로고    scopus 로고
    • Production of cellulases and hemicellulases by three Penicillium species: Effect of substrate and evaluation of cellulase adsorption by capillary electrophoresis
    • Jorgensen, H., A. Morkeberg, K. B. R. Krogh, and L. Olsson (2005) Production of cellulases and hemicellulases by three Penicillium species: Effect of substrate and evaluation of cellulase adsorption by capillary electrophoresis. Enz. Microb. Technol. 36: 42-48.
    • (2005) Enz. Microb. Technol. , vol.36 , pp. 42-48
    • Jorgensen, H.1    Morkeberg, A.2    Krogh, K.B.R.3    Olsson, L.4
  • 4
    • 0001035335 scopus 로고    scopus 로고
    • Harnessing marine microorganisms through solid state fermentation
    • Chandrasekaran, M (1996) Harnessing marine microorganisms through solid state fermentation. J. Scientific. Ind. Res. 55: 468-471.
    • (1996) J. Scientific. Ind. Res. , vol.55 , pp. 468-471
    • Chandrasekaran, M.1
  • 5
    • 28444460239 scopus 로고    scopus 로고
    • Substrate specificity and transglycosylation catalyzed by a thermostable β-glucosidase from marine hyperthermophile Thermotoga neapolitana
    • Park, T. H., K. W. Choi, C. S. Park, S. B. Lee, H. Y. Kang, K. J. Shon, J. S. Park, and J. Cha (2005) Substrate specificity and transglycosylation catalyzed by a thermostable β-glucosidase from marine hyperthermophile Thermotoga neapolitana. Appl. Microbiol. Biotechnol. 4: 411-422.
    • (2005) Appl. Microbiol. Biotechnol. , vol.4 , pp. 411-422
    • Park, T.H.1    Choi, K.W.2    Park, C.S.3    Lee, S.B.4    Kang, H.Y.5    Shon, K.J.6    Park, J.S.7    Cha, J.8
  • 6
    • 0030061364 scopus 로고    scopus 로고
    • Catalytical potency of β-Glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis
    • Fischer, L., R. Bromann, S. W. M. Kengen, W. M. dVos, and F. Wagner (1996) Catalytical potency of β-Glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis. Biotechnology 14: 88-91.
    • (1996) Biotechnology , vol.14 , pp. 88-91
    • Fischer, L.1    Bromann, R.2    Kengen, S.W.M.3    dVos, W.M.4    Wagner, F.5
  • 9
    • 0034790005 scopus 로고    scopus 로고
    • A novel alkaline endoglucanase from an alkaliphilic Bacillus isolate: Enzymatic properties, and nucleotide and deduced amino acid sequences
    • Endo, K., Y. Hakamada, S. Takizawa, H. Kubota, N. Sumitomo, T. Kobayashi, and S. Ito (2001) A novel alkaline endoglucanase from an alkaliphilic Bacillus isolate: Enzymatic properties, and nucleotide and deduced amino acid sequences. Appl. Microbiol. Biotechnol. 57: 109-116.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 109-116
    • Endo, K.1    Hakamada, Y.2    Takizawa, S.3    Kubota, H.4    Sumitomo, N.5    Kobayashi, T.6    Ito, S.7
  • 11
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • Plackett, R. L. and J. P. Burman (1946) The design of optimum multifactorial experiments. Biometrica 33: 305-325.
    • (1946) Biometrica , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 12
    • 0025209804 scopus 로고
    • Precipitation techniques
    • Englard, S. and S. Seifter (1990) Precipitation techniques. Meth. Enzymol. 182: 285-300.
    • (1990) Meth. Enzymol. , vol.182 , pp. 285-300
    • Englard, S.1    Seifter, S.2
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmlli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmlli, U.K.1
  • 14
    • 0035156434 scopus 로고    scopus 로고
    • Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus
    • Parry, N. J., D. E. Beever, E. Owen, I. Vandenberghe, J. Van Beeumen, and M. K. Bhat (2001) Biochemical characterization and mechanism of action of a thermostable β-glucosidase purified from Thermoascus aurantiacus. Biochem. J. 353: 117-127.
    • (2001) Biochem. J. , vol.353 , pp. 117-127
    • Parry, N.J.1    Beever, D.E.2    Owen, E.3    Vandenberghe, I.4    Van Beeumen, J.5    Bhat, M.K.6
  • 15
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver, H. and D. Burk (1934) The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56: 658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 16
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. (1953) The determination of enzyme inhibitor constants. Biochem. J. 55: 170-171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31: 426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 18
    • 24744470487 scopus 로고    scopus 로고
    • Fungal identification method based on DNA sequence analysis: Reassesment of the methods of the pharmaceutical society of japan and the japanese pharmacopoeia
    • Sugita, T. and A. Nishikawa (2003) Fungal identification method based on DNA sequence analysis: Reassesment of the methods of the pharmaceutical society of japan and the japanese pharmacopoeia. J. Health Sci. 49: 531-533.
    • (2003) J. Health Sci. , vol.49 , pp. 531-533
    • Sugita, T.1    Nishikawa, A.2
  • 19
    • 0142106009 scopus 로고    scopus 로고
    • Optimization of submerged culture conditions for mycelial growth and exobiopolymer production by Auricularia polytricha (wood ears fungus) using the methods of uniform design and regression analysis
    • Xu, C. P. and J. W. Yun (2003) Optimization of submerged culture conditions for mycelial growth and exobiopolymer production by Auricularia polytricha (wood ears fungus) using the methods of uniform design and regression analysis. Biotechnol. Appl. Biochem. 38: 193-199.
    • (2003) Biotechnol. Appl. Biochem. , vol.38 , pp. 193-199
    • Xu, C.P.1    Yun, J.W.2
  • 21
    • 0020099053 scopus 로고
    • Fungal and other β-glucosidases-their properties and applications
    • Woodward, J. and A. Wiseman (1982) Fungal and other β-glucosidases-their properties and applications. Enz. Microb. Technol. 4: 73-79.
    • (1982) Enz. Microb. Technol. , vol.4 , pp. 73-79
    • Woodward, J.1    Wiseman, A.2
  • 22
    • 84987406038 scopus 로고
    • Purification and properties of two β-glucosidases isolated from Aspergillus niger
    • Witte, K. and A. Wartenberg (1989) Purification and properties of two β-glucosidases isolated from Aspergillus niger. Acta. Biotechnol. 9: 179-190.
    • (1989) Acta. Biotechnol. , vol.9 , pp. 179-190
    • Witte, K.1    Wartenberg, A.2
  • 23
    • 0031301864 scopus 로고    scopus 로고
    • Purification and some properties of β-glucosidase from Aspergillus niger IBT-90
    • Galas, E. and I. Romanowska (1997) Purification and some properties of β-glucosidase from Aspergillus niger IBT-90. Acta. Microbiol. Pol. 46: 241-252.
    • (1997) Acta. Microbiol. Pol. , vol.46 , pp. 241-252
    • Galas, E.1    Romanowska, I.2
  • 24
    • 0000822014 scopus 로고    scopus 로고
    • Purification and characterization of a glucose-tolerant β-glucosidase from Aspergillus niger CCRC 31494
    • Yan, T. R. and C. L. Lin (1997) Purification and characterization of a glucose-tolerant β-glucosidase from Aspergillus niger CCRC 31494. Biosci. Biotechnol. Biochem. 61: 965-970.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 965-970
    • Yan, T.R.1    Lin, C.L.2
  • 25
    • 0026941151 scopus 로고
    • Purification and characterization of two extracellular β-glucosidases from Aspergillus nidulans
    • Kwon, K. S., H. G. Kang, and Y. C. Hah (1992) Purification and characterization of two extracellular β-glucosidases from Aspergillus nidulans. FEMS Microbiol. Lett. 97: 149-153.
    • (1992) FEMS Microbiol. Lett. , vol.97 , pp. 149-153
    • Kwon, K.S.1    Kang, H.G.2    Hah, Y.C.3
  • 26
    • 0029786225 scopus 로고    scopus 로고
    • Production, purification, and characterization of a highly glucose-tolerant novel β-glucosidase from Candida peltata
    • Saha, B. C., and R. J. Bothast (1996) Production, purification, and characterization of a highly glucose-tolerant novel β-glucosidase from Candida peltata. Appl. Environ. Biotechnol. 62: 3165-3170.
    • (1996) Appl. Environ. Biotechnol. , vol.62 , pp. 3165-3170
    • Saha, B.C.1    Bothast, R.J.2
  • 27
    • 33750987679 scopus 로고    scopus 로고
    • Characterization of a novel β-glucosidase from a Stachybotrys strain
    • Amouri, B. and A. Gargouri (2006) Characterization of a novel β-glucosidase from a Stachybotrys strain. Biochem. Eng. J. 32: 191-197.
    • (2006) Biochem. Eng. J. , vol.32 , pp. 191-197
    • Amouri, B.1    Gargouri, A.2
  • 28
    • 29144432094 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a recombinant β-glucosidase from Volvariella volvacea
    • Li, X., J. Pei, G. Wu, and W. Shao (2005) Expression, purification, and characterization of a recombinant β-glucosidase from Volvariella volvacea. Biotech. Lett. 27: 1369-1373.
    • (2005) Biotech. Lett. , vol.27 , pp. 1369-1373
    • Li, X.1    Pei, J.2    Wu, G.3    Shao, W.4
  • 29
    • 0032854876 scopus 로고    scopus 로고
    • Kinetic study of the cellobiase activity of Trichoderma reesei cellulase complex at high substrate concentrations
    • Cascalheira, J. F. and J. A. Queiroz (1999) Kinetic study of the cellobiase activity of Trichoderma reesei cellulase complex at high substrate concentrations. Biotech. Lett. 21: 651-655.
    • (1999) Biotech. Lett. , vol.21 , pp. 651-655
    • Cascalheira, J.F.1    Queiroz, J.A.2
  • 30
    • 33751092533 scopus 로고    scopus 로고
    • Purification and characterization of piceid-β-D-glucosidase from Aspergillus oryzae
    • Zhang, C., D. Li, H. Yu, B. Zhang, and F. Jin (2007) Purification and characterization of piceid-β-D-glucosidase from Aspergillus oryzae. Proc. Biochem. 42: 83-88.
    • (2007) Proc. Biochem. , vol.42 , pp. 83-88
    • Zhang, C.1    Li, D.2    Yu, H.3    Zhang, B.4    Jin, F.5
  • 31
    • 0037298812 scopus 로고    scopus 로고
    • Purification and characterization of two intracellular β-glucosidases from the Neurospora crassa mutant cell-1
    • Yazdi, M. T., A. A. Khosravi, M. Nemati, and N. D. V. Motlagh (2003) Purification and characterization of two intracellular β-glucosidases from the Neurospora crassa mutant cell-1. W. J. Microbiol. Biotechnol. 19: 79-84.
    • (2003) W. J. Microbiol. Biotechnol. , vol.19 , pp. 79-84
    • Yazdi, M.T.1    Khosravi, A.A.2    Nemati, M.3    Motlagh, N.D.V.4
  • 32
    • 0030063753 scopus 로고    scopus 로고
    • Production of cellulases by Aspergillus fumigatus and characterization of one β-glucosidase
    • Ximenes, E. A., C. R. Felix, and C. J. Ulhoa (1996) Production of cellulases by Aspergillus fumigatus and characterization of one β-glucosidase. Curr. Microbiol. 32: 119-123.
    • (1996) Curr. Microbiol. , vol.32 , pp. 119-123
    • Ximenes, E.A.1    Felix, C.R.2    Ulhoa, C.J.3
  • 33
    • 0035091719 scopus 로고    scopus 로고
    • β-Glucosidase multiplicity from Aspergillus tubingensis CBS 643.92: Purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition, and acid tolerance
    • Decker, C. H., J. Visser, and P. Schreier (2001) β-Glucosidase multiplicity from Aspergillus tubingensis CBS 643.92: Purification and characterization of four β-glucosidases and their differentiation with respect to substrate specificity, glucose inhibition, and acid tolerance. Appl. Microbiol. Biotechnol. 55: 157-163
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 157-163
    • Decker, C.H.1    Visser, J.2    Schreier, P.3
  • 34
    • 0028108213 scopus 로고
    • Purification and characterization of an extracellular β-glucosidase with transglycosylation and exo-glucosidase activities from Fusarium oxysporum
    • Christakopoulos, P., P. W. Goodenough, D. Kekos, B. J. Macris, M. Claeyssens, and M. K. Bhat (1994) Purification and characterization of an extracellular β-glucosidase with transglycosylation and exo-glucosidase activities from Fusarium oxysporum. Eur. J. Biochem. 224: 379-385.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 379-385
    • Christakopoulos, P.1    Goodenough, P.W.2    Kekos, D.3    Macris, B.J.4    Claeyssens, M.5    Bhat, M.K.6
  • 35
    • 0023946361 scopus 로고
    • Stability and substrate specificity of a β-glucosidase from the thermophilic bacterium Tp8 cloned into Escherichia coli
    • Plant, A. R., J. E. Oliver, M. L. Patchett, R. M. Daniel, and H. W. Morgan (1988) Stability and substrate specificity of a β-glucosidase from the thermophilic bacterium Tp8 cloned into Escherichia coli. Arch. Biochem. Biophys. 262: 181-188.
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 181-188
    • Plant, A.R.1    Oliver, J.E.2    Patchett, M.L.3    Daniel, R.M.4    Morgan, H.W.5
  • 36
    • 33646190494 scopus 로고    scopus 로고
    • Purification and characterisation of an intracellular enzyme with β-glucosidase and β-galactosidase activity from the thermophilic fungus Talaromyces thermophilus CBS 236.58
    • Nakkharat, P. and D. Haltrich (2006) Purification and characterisation of an intracellular enzyme with β-glucosidase and β-galactosidase activity from the thermophilic fungus Talaromyces thermophilus CBS 236.58. J. Biotech. 123: 304-313
    • (2006) J. Biotech. , vol.123 , pp. 304-313
    • Nakkharat, P.1    Haltrich, D.2
  • 37
    • 0028786543 scopus 로고
    • Purification and characterization of an intracellular β-glucosidases from Botrytis cinerea
    • Gueguen, Y., P. Chemardin, A. Arnaud, and P. Galzy (1995) Purification and characterization of an intracellular β-glucosidases from Botrytis cinerea. Enz. Microb. Technol. 17: 900-906.
    • (1995) Enz. Microb. Technol. , vol.17 , pp. 900-906
    • Gueguen, Y.1    Chemardin, P.2    Arnaud, A.3    Galzy, P.4
  • 38
    • 0343052683 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular β-glucosidase from the filamentous fungus Acremonium persicinum and its probable role in β-glucan degradation
    • Pitson, S. M., R. J. Seviour, and B. M. McDougall (1997) Purification and characterization of an extracellular β-glucosidase from the filamentous fungus Acremonium persicinum and its probable role in β-glucan degradation. Enz. Microb. Technol. 21: 182-190
    • (1997) Enz. Microb. Technol. , vol.21 , pp. 182-190
    • Pitson, S.M.1    Seviour, R.J.2    McDougall, B.M.3
  • 39
    • 0032838958 scopus 로고    scopus 로고
    • Purification and biochemical characteristics of β-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus -SSBP
    • Lin, J., B. Pillay, and S. Singh (1999) Purification and biochemical characteristics of β-D-glucosidase from a thermophilic fungus, Thermomyces lanuginosus -SSBP. Biotechnol. Appl. Biochem. 30: 81-87.
    • (1999) Biotechnol. Appl. Biochem. , vol.30 , pp. 81-87
    • Lin, J.1    Pillay, B.2    Singh, S.3
  • 40
    • 0029122231 scopus 로고
    • Purification and characterization of a cellulose-binding β-gluco-sidase from cellulose-degrading cultures of Phanerochaete chrysosporium
    • Lymer, E. S. and V. Renganathan (1995) Purification and characterization of a cellulose-binding β-gluco-sidase from cellulose-degrading cultures of Phanerochaete chrysosporium. Appl. Environ. Microbiol. 61: 2976-2980.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2976-2980
    • Lymer, E.S.1    Renganathan, V.2
  • 41
    • 0005812912 scopus 로고
    • Isolation of Streptomyces sp. producing glucose-tolerant β-glucosidases and properties of the enzymes
    • Ozaki, H. and K. Yamada (1992) Isolation of Streptomyces sp. producing glucose-tolerant β-glucosidases and properties of the enzymes. Agric. Biol. Chem. 55: 979-987.
    • (1992) Agric. Biol. Chem. , vol.55 , pp. 979-987
    • Ozaki, H.1    Yamada, K.2
  • 42
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen, S. W. M., E. J. Luesink, A. J. M. Stams, and A. J. B. Zehnder (1993) Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 213: 305-312.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.M.1    Luesink, E.J.2    Stams, A.J.M.3    Zehnder, A.J.B.4
  • 43
    • 26844444325 scopus 로고    scopus 로고
    • Dilute acid pretreatment, enzymatic saccharification and fermentation of wheat straw to ethanol
    • Saha, B. C., L. B. Iten, M. A. Cotta, and Y. V. Wu (2005) Dilute acid pretreatment, enzymatic saccharification and fermentation of wheat straw to ethanol. Proc. Biochem. 40: 3693-3700.
    • (2005) Proc. Biochem. , vol.40 , pp. 3693-3700
    • Saha, B.C.1    Iten, L.B.2    Cotta, M.A.3    Wu, Y.V.4
  • 44
    • 0023247915 scopus 로고
    • Acid and enzymatic saccharification of agricultural mixed polymers for alcohol production
    • Tewari, H. K., S. S. Marwaha, J. F. Kennedy, and L. Singh (1987) Acid and enzymatic saccharification of agricultural mixed polymers for alcohol production. British Polym. J. 19: 425-428.
    • (1987) British Polym. J. , vol.19 , pp. 425-428
    • Tewari, H.K.1    Marwaha, S.S.2    Kennedy, J.F.3    Singh, L.4
  • 45
    • 4344594391 scopus 로고    scopus 로고
    • Ethanol from lignocellulosic materials by a simultaneous saccharification and fermentation process (SFS) with Kluyveromyces marxianus CECT 10875
    • Ballesteros, M., J. M. Oliva, M. J. Negro, P. Manzanares, and I. Ballesteros (2004) Ethanol from lignocellulosic materials by a simultaneous saccharification and fermentation process (SFS) with Kluyveromyces marxianus CECT 10875. Proc. Biochem. 39: 1843-1848.
    • (2004) Proc. Biochem. , vol.39 , pp. 1843-1848
    • Ballesteros, M.1    Oliva, J.M.2    Negro, M.J.3    Manzanares, P.4    Ballesteros, I.5
  • 46
    • 3042843745 scopus 로고    scopus 로고
    • Fermentation of enzymatic hydrolysate of sunflower hulls for ethanol production and its scale-up
    • Sharma, S. K., K. L. Kalra, and G. S. Kocher (2004) Fermentation of enzymatic hydrolysate of sunflower hulls for ethanol production and its scale-up. Biomass Bioenerg. 27: 399-402.
    • (2004) Biomass Bioenerg. , vol.27 , pp. 399-402
    • Sharma, S.K.1    Kalra, K.L.2    Kocher, G.S.3
  • 47
    • 33947531303 scopus 로고    scopus 로고
    • Improvement of ethanol yield from raw corn flour by Rhizopus sp. W
    • Wang, L. S., X. Y. Ge, and W. G. Zhang (2007) Improvement of ethanol yield from raw corn flour by Rhizopus sp. W. J. Microbiol. Biotechnol. 23: 461-465.
    • (2007) J. Microbiol. Biotechnol. , vol.23 , pp. 461-465
    • Wang, L.S.1    Ge, X.Y.2    Zhang, W.G.3
  • 48
    • 0032212838 scopus 로고    scopus 로고
    • Simultaneous saccharification fermentation of pretreated sugar cane leaves to ethanol
    • Hari Krishna, S., K. Prasanthi, G. V. Chowdary, and C. Ayyanna (1998) Simultaneous saccharification fermentation of pretreated sugar cane leaves to ethanol. Proc. Biochem. 33: 825-830.
    • (1998) Proc. Biochem. , vol.33 , pp. 825-830
    • Hari Krishna, S.1    Prasanthi, K.2    Chowdary, G.V.3    Ayyanna, C.4
  • 50
    • 0037036694 scopus 로고    scopus 로고
    • Bioconversion of water-hyacinth hemicellulose acid hydrolysate to motor fuel ethanol by xylose-fermenting yeast
    • Nigam, J. N. (2007) Bioconversion of water-hyacinth hemicellulose acid hydrolysate to motor fuel ethanol by xylose-fermenting yeast. J. Biotech. 97: 107-116.
    • (2007) J. Biotech. , vol.97 , pp. 107-116
    • Nigam, J.N.1


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