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Volumn 40, Issue 4, 2007, Pages 637-644

Isolation, purification and characterisation of an endoglucanase and β-glucosidase from an anaerobic sulphidogenic bioreactor

Author keywords

Glucosidase; Anaerobic sludge digestion; Endoglucanase; Purification

Indexed keywords

ACETONE PRECIPITATION; ANAEROBIC SLUDGE DIGESTION; ENDOGLUCANASE; GLUCOSIDASE;

EID: 33847311694     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.05.020     Document Type: Article
Times cited : (27)

References (33)
  • 3
    • 0032204689 scopus 로고    scopus 로고
    • Mechanism of cellulose action in textile processes
    • Cavaco-Paulo A. Mechanism of cellulose action in textile processes. Carbohydrate Polym 37 (1998) 273-277
    • (1998) Carbohydrate Polym , vol.37 , pp. 273-277
    • Cavaco-Paulo, A.1
  • 5
    • 0034922896 scopus 로고    scopus 로고
    • Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration
    • Zaldivar J., Nielsen J., and Olsson L. Fuel ethanol production from lignocellulose: a challenge for metabolic engineering and process integration. Appl Microbiol Biotechnol 56 (2001) 17-34
    • (2001) Appl Microbiol Biotechnol , vol.56 , pp. 17-34
    • Zaldivar, J.1    Nielsen, J.2    Olsson, L.3
  • 6
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degrading enzymes and their potential industrial applications
    • Bhat M.K., and Bhat S. Cellulose degrading enzymes and their potential industrial applications. Biotechnol Adv 15 (1997) 583-620
    • (1997) Biotechnol Adv , vol.15 , pp. 583-620
    • Bhat, M.K.1    Bhat, S.2
  • 8
    • 33847291050 scopus 로고    scopus 로고
    • Specific sulphur metabolites stimulate β-glucosidase activity in an anaerobic sulphidogenic bioreactor
    • Ngesi N., Pletschke B.I., Rose P.D., and Whiteley C.G. Specific sulphur metabolites stimulate β-glucosidase activity in an anaerobic sulphidogenic bioreactor. Biotechnol Lett 31 (2002) 419-424
    • (2002) Biotechnol Lett , vol.31 , pp. 419-424
    • Ngesi, N.1    Pletschke, B.I.2    Rose, P.D.3    Whiteley, C.G.4
  • 9
    • 0037008352 scopus 로고    scopus 로고
    • The enzymology of sludge solubilisation utilising sulphate reducing systems: identification of ATP-sulphurylase
    • Pletschke B.I., Rose P.D., and Whiteley C.G. The enzymology of sludge solubilisation utilising sulphate reducing systems: identification of ATP-sulphurylase. Enzyme Microbiol Technol 31 (2002) 329-336
    • (2002) Enzyme Microbiol Technol , vol.31 , pp. 329-336
    • Pletschke, B.I.1    Rose, P.D.2    Whiteley, C.G.3
  • 10
    • 0141794140 scopus 로고    scopus 로고
    • Co-digestion of primary sewage sludge and industrial wastewater under anaerobic sulphate reducing conditions: enzymatic profiles in a reciprocating sludge bed reactor
    • Enongene G., Pletschke B.I., Rose P.D., Whittington-Jones K., and Whiteley C.G. Co-digestion of primary sewage sludge and industrial wastewater under anaerobic sulphate reducing conditions: enzymatic profiles in a reciprocating sludge bed reactor. Water Sci Technol 48 4 (2003) 129-138
    • (2003) Water Sci Technol , vol.48 , Issue.4 , pp. 129-138
    • Enongene, G.1    Pletschke, B.I.2    Rose, P.D.3    Whittington-Jones, K.4    Whiteley, C.G.5
  • 12
    • 0012896349 scopus 로고
    • Cellulases from Eupenicillium javanicum
    • Colowick S.P., and Kaplan N.O. Cellulases from Eupenicillium javanicum. Meth Enzymol 160 (1988) 253-289
    • (1988) Meth Enzymol , vol.160 , pp. 253-289
    • Colowick, S.P.1    Kaplan, N.O.2
  • 13
    • 0035078267 scopus 로고    scopus 로고
    • Improved method for the fluorimetric detection of β-d-galactosidase in water
    • Hattenberger M., Mascher F., Kalcher K., and Marth E. Improved method for the fluorimetric detection of β-d-galactosidase in water. Int J Hyg Environ Health 203 (2001) 281-287
    • (2001) Int J Hyg Environ Health , vol.203 , pp. 281-287
    • Hattenberger, M.1    Mascher, F.2    Kalcher, K.3    Marth, E.4
  • 14
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver H., and Burk D. The determination of enzyme dissociation constants. J Am Chem Soc 56 (1934) 658-666
    • (1934) J Am Chem Soc , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 15
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden A. A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem J 137 (1974) 143-144
    • (1974) Biochem J , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 16
    • 33847316698 scopus 로고    scopus 로고
    • Lilley ID, Wentzel MC, Loewenthal RE, Marais GVR. Acid fermentation of primary sludge at 20 °C. Research Report W64. Civil Engineering Department, University of Cape Town; 1990. p. 87.
  • 17
    • 0033843651 scopus 로고    scopus 로고
    • A fast and simple turbidmetric method for the determination of sulfate in sulfate-reducing bacteria cultures
    • Kolmert A., Wikstrom P., and Hallberg K.B. A fast and simple turbidmetric method for the determination of sulfate in sulfate-reducing bacteria cultures. J Microbiol Meth 41 (2000) 179-184
    • (2000) J Microbiol Meth , vol.41 , pp. 179-184
    • Kolmert, A.1    Wikstrom, P.2    Hallberg, K.B.3
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal Biochem 72 (1976) 248-251
    • (1976) Anal Biochem , vol.72 , pp. 248-251
    • Bradford, M.M.1
  • 19
    • 62249137520 scopus 로고
    • The estimation of carbohydrates in the plant extract by anthrone
    • Yemm E.W.W., and Willis A.J. The estimation of carbohydrates in the plant extract by anthrone. Biochem J 57 (1954) 508-514
    • (1954) Biochem J , vol.57 , pp. 508-514
    • Yemm, E.W.W.1    Willis, A.J.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of a bacteriophage
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of a bacteriophage. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0031127852 scopus 로고    scopus 로고
    • Site of secretion and properties of endogenous endo-β-1,4-glucanase components from Reticulitermes speratus (Kolbe), a Japanese subterranean termite
    • Watanabe H., Nakamura M., Tokuda G., Yamaoka I., Scrivener A.M., and Noda H. Site of secretion and properties of endogenous endo-β-1,4-glucanase components from Reticulitermes speratus (Kolbe), a Japanese subterranean termite. Insect Biochem Mol Biol 27 (1997) 305-313
    • (1997) Insect Biochem Mol Biol , vol.27 , pp. 305-313
    • Watanabe, H.1    Nakamura, M.2    Tokuda, G.3    Yamaoka, I.4    Scrivener, A.M.5    Noda, H.6
  • 23
    • 0028946812 scopus 로고
    • Purification and characterisation of a protease-resistant cellulase from Aspergillus niger
    • Akiba S., Kimura Y., Yamamoto K., and Kumagai H. Purification and characterisation of a protease-resistant cellulase from Aspergillus niger. J Ferment Bioeng 79 (1995) 125-130
    • (1995) J Ferment Bioeng , vol.79 , pp. 125-130
    • Akiba, S.1    Kimura, Y.2    Yamamoto, K.3    Kumagai, H.4
  • 24
    • 0032813273 scopus 로고    scopus 로고
    • Molecular cloning and expression of an endo-β-1,4-d-glucanase I (avicelase I) gene from Bacillus cellulolyticus K-12 and characterisation of the recombinant enzyme
    • Lee T.-K., and Kim C.-H. Molecular cloning and expression of an endo-β-1,4-d-glucanase I (avicelase I) gene from Bacillus cellulolyticus K-12 and characterisation of the recombinant enzyme. Appl Biochem Biotechnol 80 (1999) 121-125
    • (1999) Appl Biochem Biotechnol , vol.80 , pp. 121-125
    • Lee, T.-K.1    Kim, C.-H.2
  • 26
    • 0032839883 scopus 로고    scopus 로고
    • Heavy metal effects on β-glucosidase activity influenced by pH and buffer systems
    • Geiger G., Furrer G., Funk F., Brandl H., and Schulin R. Heavy metal effects on β-glucosidase activity influenced by pH and buffer systems. J Enzyme Inhib 14 5 (1999) 365-379
    • (1999) J Enzyme Inhib , vol.14 , Issue.5 , pp. 365-379
    • Geiger, G.1    Furrer, G.2    Funk, F.3    Brandl, H.4    Schulin, R.5
  • 27
    • 0031968246 scopus 로고    scopus 로고
    • β-Glucosidase activity in the presence of copper and goethite
    • Geiger G., Livingston M.P., Funk F., and Schulin R. β-Glucosidase activity in the presence of copper and goethite. Eur J Soil Sci 49 1 (1998) 17-23
    • (1998) Eur J Soil Sci , vol.49 , Issue.1 , pp. 17-23
    • Geiger, G.1    Livingston, M.P.2    Funk, F.3    Schulin, R.4
  • 28
    • 0032769250 scopus 로고    scopus 로고
    • Purification and characterisation of a cellulase from Catharanthus roseus stems
    • Sanwal S.G.G. Purification and characterisation of a cellulase from Catharanthus roseus stems. Phytochemistry 52 (1999) 7-13
    • (1999) Phytochemistry , vol.52 , pp. 7-13
    • Sanwal, S.G.G.1
  • 29
    • 0032126046 scopus 로고    scopus 로고
    • Characterisation of endoglucanases from the brown rot fungi Gloeophyllum sepiarium and Gloeophyllum traberum
    • Mansfield S.D., Saddler J.N., and Gubitz G.M. Characterisation of endoglucanases from the brown rot fungi Gloeophyllum sepiarium and Gloeophyllum traberum. Enzyme Microbiol Technol 23 (1998) 133-140
    • (1998) Enzyme Microbiol Technol , vol.23 , pp. 133-140
    • Mansfield, S.D.1    Saddler, J.N.2    Gubitz, G.M.3
  • 30
    • 0028962474 scopus 로고
    • Structural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase CelD
    • Chauvaux S., Souchon H., Alzari P.M., Chariot P., and Beguin P. Structural and functional analysis of the metal-binding sites of Clostridium thermocellum endoglucanase CelD. J Biol Chem 270 17 (1995) 9757-9762
    • (1995) J Biol Chem , vol.270 , Issue.17 , pp. 9757-9762
    • Chauvaux, S.1    Souchon, H.2    Alzari, P.M.3    Chariot, P.4    Beguin, P.5
  • 31
    • 0038692120 scopus 로고    scopus 로고
    • Purification and properties of a thermostable endoglucanase from Bacillus stearothermophilus MC 7
    • Kambourova M., Kirilova N., Mandeva R., and Derekova A. Purification and properties of a thermostable endoglucanase from Bacillus stearothermophilus MC 7. J Mol Catal 22 (2003) 307-313
    • (2003) J Mol Catal , vol.22 , pp. 307-313
    • Kambourova, M.1    Kirilova, N.2    Mandeva, R.3    Derekova, A.4
  • 32
    • 0022870763 scopus 로고
    • Kinetic properties of ß-glucosidase from Aspergillus ornatus
    • Yeoh H.H., Tan T.K., and Koh S.K. Kinetic properties of ß-glucosidase from Aspergillus ornatus. Appl Microbiol Biotechnol 25 (1986) 25-28
    • (1986) Appl Microbiol Biotechnol , vol.25 , pp. 25-28
    • Yeoh, H.H.1    Tan, T.K.2    Koh, S.K.3
  • 33
    • 0038019825 scopus 로고    scopus 로고
    • Kinetic dynamics in heterogeneous enzymatic hydrolysis of cellulose: an overview, an experimental study and mathematical modelling
    • Gan Q., Allen S.J., and Taylor G. Kinetic dynamics in heterogeneous enzymatic hydrolysis of cellulose: an overview, an experimental study and mathematical modelling. Process Biochem 38 7 (2003) 1003-1018
    • (2003) Process Biochem , vol.38 , Issue.7 , pp. 1003-1018
    • Gan, Q.1    Allen, S.J.2    Taylor, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.