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Volumn 26, Issue 8, 2010, Pages 1385-1391

Production of a highly glucose tolerant β-glucosidase by Paecilomyces variotii MG3: Optimization of fermentation conditions using Plackett-Burman and Box-Behnken experimental designs

Author keywords

Glucosidase; Box Behnken design; Glucose tolerant; Paecilomyces variotii; Response surface methodology

Indexed keywords

BOX-BEHNKEN DESIGN; BOX-BEHNKEN EXPERIMENTAL DESIGN; CELLO-OLIGOSACCHARIDES; CELLOBIOSE; CELLULOSE DEGRADATION; CONCENTRATION OF; ENZYME PRODUCTION; GLUCOHYDROLASE; GLUCOSIDASE; GLYCOSIDIC BOND; INCUBATION PERIODS; INCUBATION TIME; PAECILOMYCES; PLACKETT-BURMAN; PLACKETT-BURMAN DESIGNS; RESPONSE SURFACE METHODOLOGY; SOLID-STATE FERMENTATION; STATISTICAL EXPERIMENTS;

EID: 77954459995     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-010-0311-0     Document Type: Article
Times cited : (38)

References (30)
  • 1
    • 0036323669 scopus 로고    scopus 로고
    • Optimization of thermostable lipase production from a thermophilic Geobacillus sp. using Box-Behnken experimental design
    • Abdel-Fattah YR (2002) Optimization of thermostable lipase production from a thermophilic Geobacillus sp. using Box-Behnken experimental design. Biotechnol Lett 24: 1217-1222.
    • (2002) Biotechnol Lett , vol.24 , pp. 1217-1222
    • Abdel-Fattah, Y.R.1
  • 2
    • 0037332961 scopus 로고    scopus 로고
    • Use of response surface methodology for selection of nutrient levels for culturing Paecilomyces variotii in eucalyptus hemicellulosic hydrolyzate
    • Almeida e Silva JB, Lima UA, Taqueda MES, Guaragna FG (2003) Use of response surface methodology for selection of nutrient levels for culturing Paecilomyces variotii in eucalyptus hemicellulosic hydrolyzate. Bioresour Technol 87: 45-50.
    • (2003) Bioresour Technol , vol.87 , pp. 45-50
    • Almeida e Silva, J.B.1    Lima, U.A.2    Taqueda, M.E.S.3    Guaragna, F.G.4
  • 3
    • 33846696107 scopus 로고    scopus 로고
    • Tannase production by Paecilomyces variotii
    • Battestin V, Macedo GA (2007) Tannase production by Paecilomyces variotii. Bioresour Technol 98: 1832-1837.
    • (2007) Bioresour Technol , vol.98 , pp. 1832-1837
    • Battestin, V.1    Macedo, G.A.2
  • 4
    • 0036448608 scopus 로고    scopus 로고
    • Microbial β-glucosidase: Cloning, properties and applications
    • Bhatia Y, Mishra S, Bisaria VS (2002) Microbial β-glucosidase: cloning, properties and applications. Crit Rev Biotechnol 22: 375-407.
    • (2002) Crit Rev Biotechnol , vol.22 , pp. 375-407
    • Bhatia, Y.1    Mishra, S.2    Bisaria, V.S.3
  • 5
    • 84946657020 scopus 로고
    • Some new three-level design for the study of quantitative variables
    • Box GEP, Behnken DW (1960) Some new three-level design for the study of quantitative variables. Technometrics 2: 455-475.
    • (1960) Technometrics , vol.2 , pp. 455-475
    • Box, G.E.P.1    Behnken, D.W.2
  • 6
    • 0025149227 scopus 로고
    • Comparison of the hydrolytic activity of commercial cellulase preparations
    • Breuil C, Chan M, Saddler JN (1990) Comparison of the hydrolytic activity of commercial cellulase preparations. Appl Microbiol Biotechnol 34: 31-35.
    • (1990) Appl Microbiol Biotechnol , vol.34 , pp. 31-35
    • Breuil, C.1    Chan, M.2    Saddler, J.N.3
  • 8
    • 0038342002 scopus 로고    scopus 로고
    • Oligosaccharide synthesis by the hyperthermostable β-glucosidase from Pyrococcus furiosus: Kinetics and modeling
    • Bruins ME, Strubel M, van Lieshout JFT, Janssen AEM, Boom RM (2003) Oligosaccharide synthesis by the hyperthermostable β-glucosidase from Pyrococcus furiosus: kinetics and modeling. Enzyme Microb Technol 33: 3-11.
    • (2003) Enzyme Microb Technol , vol.33 , pp. 3-11
    • Bruins, M.E.1    Strubel, M.2    van Lieshout, J.F.T.3    Janssen, A.E.M.4    Boom, R.M.5
  • 9
    • 0020720326 scopus 로고
    • The use of sugarcane stillage for single cell protein production
    • Cabib G, Silva HJ, Giulietti A (1983) The use of sugarcane stillage for single cell protein production. J Chem Technol Biotechnol 33: 21-28.
    • (1983) J Chem Technol Biotechnol , vol.33 , pp. 21-28
    • Cabib, G.1    Silva, H.J.2    Giulietti, A.3
  • 10
    • 31044441978 scopus 로고    scopus 로고
    • Comparison between various commercial sources of almond β-glucosidase for the production of alkyl glucosides
    • Ducret A, Trani M, Lortie R (2006) Comparison between various commercial sources of almond β-glucosidase for the production of alkyl glucosides. J Mol Catal B: Enzyme 38: 91-94.
    • (2006) J Mol Catal B: Enzyme , vol.38 , pp. 91-94
    • Ducret, A.1    Trani, M.2    Lortie, R.3
  • 11
    • 66849128580 scopus 로고    scopus 로고
    • Response surface optimization of enzymatic hydrolysis of Cistus ladanifer and Cytisus striatus for bio-ethanol production
    • Ferreira S, Duarte AP, Ribeiro MHL, Queiroz JA, Domingues FC (2009) Response surface optimization of enzymatic hydrolysis of Cistus ladanifer and Cytisus striatus for bio-ethanol production. Biochem Eng J 45: 192-200.
    • (2009) Biochem Eng J , vol.45 , pp. 192-200
    • Ferreira, S.1    Duarte, A.P.2    Ribeiro, M.H.L.3    Queiroz, J.A.4    Domingues, F.C.5
  • 12
    • 0017394722 scopus 로고
    • Cellobiase from Trichoderma viride: Purification, properties, kinetics and mechanism
    • Gong CS, Ladisch MR, Tsao GT (1977) Cellobiase from Trichoderma viride: purification, properties, kinetics and mechanism. Biotechnol Bioeng 19: 959-981.
    • (1977) Biotechnol Bioeng , vol.19 , pp. 959-981
    • Gong, C.S.1    Ladisch, M.R.2    Tsao, G.T.3
  • 13
    • 0031552603 scopus 로고    scopus 로고
    • Enhancement of aromatic quality of Muscat wine by the use of immobilized β-glucosidase
    • Gueguen Y, Chemardin P, Pien S, Arnaud A, Galzy P (1997) Enhancement of aromatic quality of Muscat wine by the use of immobilized β-glucosidase. J Biotechnol 55: 151-156.
    • (1997) J Biotechnol , vol.55 , pp. 151-156
    • Gueguen, Y.1    Chemardin, P.2    Pien, S.3    Arnaud, A.4    Galzy, P.5
  • 14
    • 0344889065 scopus 로고    scopus 로고
    • Production of highly glucose tolerant extracellular β-glucosidase by three Aspergillus strains
    • Gunata Z, Vallier M (1999) Production of highly glucose tolerant extracellular β-glucosidase by three Aspergillus strains. Biotechnol Lett 21: 219-223.
    • (1999) Biotechnol Lett , vol.21 , pp. 219-223
    • Gunata, Z.1    Vallier, M.2
  • 15
    • 33846125000 scopus 로고    scopus 로고
    • Cloning and functional expression of thermostable β-glucosidase gene from Thermoascus auranticus
    • Hong J, Tamaki H, Kumagai H (2007) Cloning and functional expression of thermostable β-glucosidase gene from Thermoascus auranticus. Appl Microbiol Biotechnol 73: 1331-1339.
    • (2007) Appl Microbiol Biotechnol , vol.73 , pp. 1331-1339
    • Hong, J.1    Tamaki, H.2    Kumagai, H.3
  • 16
    • 67649403761 scopus 로고    scopus 로고
    • Characterization of a recombinant β-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus
    • Hong M, Kim Y, Park C, Lee J, Kim Y, Oh D (2009) Characterization of a recombinant β-glucosidase from the thermophilic bacterium Caldicellulosiruptor saccharolyticus. J Biosci Bioeng 108: 36-40.
    • (2009) J Biosci Bioeng , vol.108 , pp. 36-40
    • Hong, M.1    Kim, Y.2    Park, C.3    Lee, J.4    Kim, Y.5    Oh, D.6
  • 17
    • 0034775836 scopus 로고    scopus 로고
    • Production and characterization of β-glucosidase from different Aspergillus strains
    • Jäger S, Brumbauer A, Feher E, Rėczey K, Kiss L (2001) Production and characterization of β-glucosidase from different Aspergillus strains. World J Microbiol Biotechnol 17: 455-461.
    • (2001) World J Microbiol Biotechnol , vol.17 , pp. 455-461
    • Jäger, S.1    Brumbauer, A.2    Feher, E.3    Reczey, K.4    Kiss, L.5
  • 18
    • 0034695422 scopus 로고    scopus 로고
    • The tertiary structure at 1.59Å resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces variotii Bainer
    • Kumar PR, Eswaramoorthy S, Vithayathil PJ, Viswamitra MA (2000) The tertiary structure at 1. 59Å resolution and the proposed amino acid sequence of a family-11 xylanase from the thermophilic fungus Paecilomyces variotii Bainer. J Mol Biol 295: 581-593.
    • (2000) J Mol Biol , vol.295 , pp. 581-593
    • Kumar, P.R.1    Eswaramoorthy, S.2    Vithayathil, P.J.3    Viswamitra, M.A.4
  • 19
    • 32844467765 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable cellulase free xylanase from the newly isolated Paecilomyces thermophila
    • Li L, Tian H, Cheng Y, Jiang Z, Yang S (2006) Purification and characterization of a thermostable cellulase free xylanase from the newly isolated Paecilomyces thermophila. Enzyme Microb Technol 38: 780-787.
    • (2006) Enzyme Microb Technol , vol.38 , pp. 780-787
    • Li, L.1    Tian, H.2    Cheng, Y.3    Jiang, Z.4    Yang, S.5
  • 20
    • 0001131698 scopus 로고
    • The design of optimum multifactorial experiments
    • Plackett RL, Burman JP (1946) The design of optimum multifactorial experiments. Biometrika 33: 305-325.
    • (1946) Biometrika , vol.33 , pp. 305-325
    • Plackett, R.L.1    Burman, J.P.2
  • 22
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization and substrate specificity of a novel highly glucose tolerant β-glucosidase from Aspergillus oryzae
    • Riou C, Salmon JM, Vallier M, Gunata Z, Barre P (1998) Purification, characterization and substrate specificity of a novel highly glucose tolerant β-glucosidase from Aspergillus oryzae. Appl Environ Microbiol 64: 3607-3614.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.M.2    Vallier, M.3    Gunata, Z.4    Barre, P.5
  • 24
    • 0002341771 scopus 로고    scopus 로고
    • Experimental design for improvement of fermentation
    • 2nd edn., A. L. Demain and J. E. Davies (Eds.), Washington, DC: ASM press
    • Strobel RJ, Sullivan GR (1999) Experimental design for improvement of fermentation. In: Demain AL, Davies JE (eds) Manual of industrial microbiology and biotechnology, 2nd edn. ASM press, Washington, DC, pp 80-93.
    • (1999) Manual of Industrial Microbiology and Biotechnology , pp. 80-93
    • Strobel, R.J.1    Sullivan, G.R.2
  • 25
    • 0034041751 scopus 로고    scopus 로고
    • Solid-state fermentation with Aspergillus niger for cellobiase production
    • Tsao GT, Xia L, Cao N, Gong CS (2000) Solid-state fermentation with Aspergillus niger for cellobiase production. Appl Biochem Biotechnol 84-86: 743-749.
    • (2000) Appl Biochem Biotechnol , vol.84-86 , pp. 743-749
    • Tsao, G.T.1    Xia, L.2    Cao, N.3    Gong, C.S.4
  • 26
    • 34247375264 scopus 로고    scopus 로고
    • A novel variant of Thermotoga neapolitana β-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation
    • Turner P, Svensson D, Adlercreutz P, Karlsson EN (2007) A novel variant of Thermotoga neapolitana β-glucosidase B is an efficient catalyst for the synthesis of alkyl glucosides by transglycosylation. J Biotechnol 130: 67-74.
    • (2007) J Biotechnol , vol.130 , pp. 67-74
    • Turner, P.1    Svensson, D.2    Adlercreutz, P.3    Karlsson, E.N.4
  • 27
    • 0034319166 scopus 로고    scopus 로고
    • Experimental design for media development: Statistical design or global random search?
    • Weuster-Botz D (2000) Experimental design for media development: statistical design or global random search? J Biosci Bioeng 90: 473-483.
    • (2000) J Biosci Bioeng , vol.90 , pp. 473-483
    • Weuster-Botz, D.1
  • 28
    • 33746960265 scopus 로고    scopus 로고
    • High level of xylanase production by the thermophilic Paecilomyces thermophila J18 on wheat straw in solid state fermentation
    • Yang SQ, Yan QJ, Jiang ZQ, Li LT, Tian HM, Wang YZ (2006) High level of xylanase production by the thermophilic Paecilomyces thermophila J18 on wheat straw in solid state fermentation. Bioresour Technol 97: 1794-1800.
    • (2006) Bioresour Technol , vol.97 , pp. 1794-1800
    • Yang, S.Q.1    Yan, Q.J.2    Jiang, Z.Q.3    Li, L.T.4    Tian, H.M.5    Wang, Y.Z.6
  • 29
    • 7644238142 scopus 로고    scopus 로고
    • β-Glucosidase-activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose
    • Zanoelo FF, Polizeli MLTM, Terenzi HF, Jorge JA (2004) β-Glucosidase-activity from the thermophilic fungus Scytalidium thermophilum is stimulated by glucose and xylose. FEMS Microbiol Lett 240: 137-143.
    • (2004) FEMS Microbiol Lett , vol.240 , pp. 137-143
    • Zanoelo, F.F.1    Polizeli, M.L.T.M.2    Terenzi, H.F.3    Jorge, J.A.4
  • 30
    • 33751092533 scopus 로고    scopus 로고
    • Purification and characterization of piceid-β-D-glucosidase from Aspergillus oryzae
    • Zhang C, Li D, Yu H, Zang B, Jin F (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    Zang, B.4    Jin, F.5


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