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Volumn 5, Issue 1, 2010, Pages 81-98

Regulation of cellulase synthesis in Chaetomium erraticum

Author keywords

glucosidase; Catabolite repression; Cellulases; Endoglucanase; Exoglucanase; Regulation

Indexed keywords

CATABOLITE REPRESSION; CELLULASES; ENDOGLUCANASES; EXOGLUCANASE; GLUCOSIDASE; REGULATION;

EID: 77956093089     PISSN: None     EISSN: 19302126     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 38249036023 scopus 로고
    • Cellulase formation by Aspergillus nidulans
    • Bagga, P. S., and Sandhu, D. K. (1987). "Cellulase formation by Aspergillus nidulans," J. Ferment. Technol. 65, 635-642.
    • (1987) J. Ferment. Technol. , vol.65 , pp. 635-642
    • Bagga, P.S.1    Sandhu, D.K.2
  • 2
    • 0024312523 scopus 로고
    • Developmentally related changes in the production and expression of endo-B-1,4-glucanases in Aspergillus nidulans
    • Bagga, P. S., Sharma, S., and Sandhu, D. K. (1989). "Developmentally related changes in the production and expression of endo-B-1,4-glucanases in Aspergillus nidulans," Genome 32, 288-292.
    • (1989) Genome , vol.32 , pp. 288-292
    • Bagga, P.S.1    Sharma, S.2    Sandhu, D.K.3
  • 3
    • 0026338104 scopus 로고
    • Effect of exogenous cyclic-AMP on catabolite repression of cellulase formation in Aspergillus nidulans
    • Bagga, P. S., Sandhu, D. K., and Sharma, S. (1991). "Effect of exogenous cyclic-AMP on catabolite repression of cellulase formation in Aspergillus nidulans," Acta Biotechnol. 11, 395-402.
    • (1991) Acta Biotechnol. , vol.11 , pp. 395-402
    • Bagga, P.S.1    Sandhu, D.K.2    Sharma, S.3
  • 5
    • 0017144336 scopus 로고
    • Factors influencing the production of cellulases by Sporotrichum thermophile
    • Coutts, A. D., and Smith, R. E. (1976). "Factors influencing the production of cellulases by Sporotrichum thermophile," Appl. Environ. Microbiol. 31, 819-825.
    • (1976) Appl. Environ. Microbiol. , vol.31 , pp. 819-825
    • Coutts, A.D.1    Smith, R.E.2
  • 6
    • 0344333348 scopus 로고
    • Some characteristics of the cellulolyticum enzyme system of Chaetomium cellulolyticum
    • Fahnrich, P., and Irrgang, K. (1982). "Some characteristics of the cellulolyticum enzyme system of Chaetomium cellulolyticum," Biotechnol. Lett. 4, 519-524.
    • (1982) Biotechnol. Lett. , vol.4 , pp. 519-524
    • Fahnrich, P.1    Irrgang, K.2
  • 7
    • 0014064552 scopus 로고
    • Yeast malate dehydrogenase: Enzyme inactivation in catabolite repression
    • Ferguson, J. J., Boll, Jr. M., and Holzer, H. (1967). "Yeast malate dehydrogenase: Enzyme inactivation in catabolite repression," Eur. J. Biochem. 1, 21-25.
    • (1967) Eur. J. Biochem. , vol.1 , pp. 21-25
    • Ferguson, J.J.1    Boll M., Jr.2    Holzer, H.3
  • 8
    • 0025349947 scopus 로고
    • Factors influencing production of cellulases by Chaetomium thermophile var. coprophile
    • Ganju, R. K., Vithayathil, P. J., and Murthy, S. K. (1990). "Factors influencing production of cellulases by Chaetomium thermophile var. coprophile," Indian J. Exp. Biol. 28, 254-264.
    • (1990) Indian J. Exp. Biol. , vol.28 , pp. 254-264
    • Ganju, R.K.1    Vithayathil, P.J.2    Murthy, S.K.3
  • 9
    • 0018401344 scopus 로고
    • Studies on the mechanism of enzymatic hydrolysis of cellulosic substances
    • Ghose, T. K., and Bisaria, V. S. (1979). "Studies on the mechanism of enzymatic hydrolysis of cellulosic substances," Biotechnol. Bioeng. 21, 131-146.
    • (1979) Biotechnol. Bioeng. , vol.21 , pp. 131-146
    • Ghose, T.K.1    Bisaria, V.S.2
  • 10
    • 2942732260 scopus 로고
    • Microbial β-glucanases
    • Halliwell, G. (1979). "Microbial β-glucanases," Prog. Ind. Microbiol. 32, 1-50.
    • (1979) Prog. Ind. Microbiol. , vol.32 , pp. 1-50
    • Halliwell, G.1
  • 11
    • 49549129756 scopus 로고
    • Catabolite inactivation in yeast
    • Holzer, H. (1976). "Catabolite inactivation in yeast," Trends Biochem. Sci. 1, 178-181.
    • (1976) Trends Biochem. Sci. , vol.1 , pp. 178-181
    • Holzer, H.1
  • 12
    • 0013894858 scopus 로고
    • Regulation of induced cellulase synthesis in Pyrenochaete terrestris by utilizable carbon compounds
    • Horton, J. C., and Keen, N. T. (1966). "Regulation of induced cellulase synthesis in Pyrenochaete terrestris by utilizable carbon compounds," Can. J. Microbiol. 12, 209-220.
    • (1966) Can. J. Microbiol. , vol.12 , pp. 209-220
    • Horton, J.C.1    Keen, N.T.2
  • 13
    • 0030480099 scopus 로고    scopus 로고
    • Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei
    • Ilmén, M., Onnela, M. L., Klemsdal, S., Keränen, S., and Penttilä. M. (1996). "Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei," Mol. Gen. Genet. 253, 303-314.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 303-314
    • Ilmén, M.1    Onnela, M.L.2    Klemsdal, S.3    Keränen, S.4    Penttilä, M.5
  • 14
    • 0011839935 scopus 로고
    • Partial purification, characterization and regulation of cellulolytic enzymes from Trichoderma longibrachiatum
    • Kalra, M. K., Sidhu, M. S., and Sandhu, D. K. (1986). "Partial purification, characterization and regulation of cellulolytic enzymes from Trichoderma longibrachiatum," J. Appl. Bacteriol. 61, 73-80.
    • (1986) J. Appl. Bacteriol. , vol.61 , pp. 73-80
    • Kalra, M.K.1    Sidhu, M.S.2    Sandhu, D.K.3
  • 15
    • 9744248282 scopus 로고    scopus 로고
    • Clostridium straminisolvens sp. nov., a moderately thermophilic, aerotolerant and cellulolytic bacerium isolated from a cellulose-degrading bacterial community
    • Kato, S., Haruta, S., Cui, Z. J., Ishii, M., Yokota, A., and Igarashi, Y. (2004). "Clostridium straminisolvens sp. nov., a moderately thermophilic, aerotolerant and cellulolytic bacterium isolated from a cellulose-degrading bacterial community," Int. J. Syst. Evol. Microbiol. 54, 2043-2047.
    • (2004) Int. J. Syst. Evol. Microbiol. , vol.54 , pp. 2043-2047
    • Kato, S.1    Haruta, S.2    Cui, Z.J.3    Ishii, M.4    Yokota, A.5    Igarashi, Y.6
  • 16
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives
    • Kumar, R., Singh, S., and Singh, O. V. (2008). "Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives," J. Ind. Microbiol. Biotechnol. 35, 377-391.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 17
    • 0344765400 scopus 로고
    • Cellulolytic activities of Chaetomium globosum on different substrates
    • Lakshmikant, K., and Mathur, S. N. (1990). "Cellulolytic activities of Chaetomium globosum on different substrates," World J. Microbiol. Biotechnol. 6, 23-26.
    • (1990) World J. Microbiol. Biotechnol. , vol.6 , pp. 23-26
    • Lakshmikant, K.1    Mathur, S.N.2
  • 18
    • 77956067786 scopus 로고    scopus 로고
    • Enhanced cellulose production of the Trichoderma viride mutated by microwave and ultraviolet
    • (in press)
    • Li, X., Yang, H., Roy, B, Park, E. Y., Jiang, L., Wang, D., and Miao, Y. (2009). "Enhanced cellulose production of the Trichoderma viride mutated by microwave and ultraviolet," Microbiol Res. (in press).
    • (2009) Microbiol Res.
    • Li, X.1    Yang, H.2    Roy, B.3    Park, E.Y.4    Jiang, L.5    Wang, D.6    Miao, Y.7
  • 20
    • 0014355437 scopus 로고
    • Extracellular proteinase from Penicillium notatum
    • Makonnen, B., and Porath, H. (1968). "Extracellular proteinase from Penicillium notatum," Eur. J. Biochem. 6, 425-431.
    • (1968) Eur. J. Biochem. , vol.6 , pp. 425-431
    • Makonnen, B.1    Porath, H.2
  • 21
    • 0020520351 scopus 로고
    • Production and regulation of extracellular endocellulase by Agaricus bisporus
    • Manning, K., and Wood, D. A. (1983). "Production and regulation of extracellular endocellulase by Agaricus bisporus," J. Gen. Microbiol. 129, 1839-1847.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 1839-1847
    • Manning, K.1    Wood, D.A.2
  • 22
    • 37049006919 scopus 로고    scopus 로고
    • Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates
    • Martins, L. F., Kolling, D., Camassola, M., Dillon, A. J., and Ramos, L. P. (2008). "Comparison of Penicillium echinulatum and Trichoderma reesei cellulases in relation to their activity against various cellulosic substrates," Bioresour. Technol. 99, 1417-1424
    • (2008) Bioresour. Technol. , vol.99 , pp. 1417-1424
    • Martins, L.F.1    Kolling, D.2    Camassola, M.3    Dillon, A.J.4    Ramos, L.P.5
  • 23
    • 2042470408 scopus 로고
    • Production of β-glucosidase by Penicillium rubrum O stall
    • Menon, K., Rao, K. K., and Pushalkar, S. (1994). "Production of β-glucosidase by Penicillium rubrum O stall," Indian J. Exp. Biol. 32, 706-709.
    • (1994) Indian J. Exp. Biol. , vol.32 , pp. 706-709
    • Menon, K.1    Rao, K.K.2    Pushalkar, S.3
  • 24
    • 0015360065 scopus 로고
    • Catabolite repression of cellulase formation in Trichoderma viride
    • Nisizawa, T., Suzuki, H., and Nisizawa, K. (1972). "Catabolite repression of cellulase formation in Trichoderma viride," J. Biochem. 71, 999-1007.
    • (1972) J. Biochem. , vol.71 , pp. 999-1007
    • Nisizawa, T.1    Suzuki, H.2    Nisizawa, K.3
  • 25
    • 0001023526 scopus 로고
    • Growth of Cellulomonas sp. ATCC 21399 on different polysaccharides as sole carbon source induction of extracellular enzymes
    • Poulsen, O. M., and Petersen, L. W. (1988). "Growth of Cellulomonas sp. ATCC 21399 on different polysaccharides as sole carbon source induction of extracellular enzymes," Appl. Microbiol. Biotechnol. 29, 480-484.
    • (1988) Appl. Microbiol. Biotechnol. , vol.29 , pp. 480-484
    • Poulsen, O.M.1    Petersen, L.W.2
  • 26
    • 0024791239 scopus 로고
    • Expression of β-glucosidase and endo-β-1,4-glucanase during development of Chaetomium fusisporale and their characterization
    • Sandhu, D. K., and Puri, R. (1989). "Expression of β-glucosidase and endo-β-1,4-glucanase during development of Chaetomium fusisporale and their characterization," J. Basic Microbiol. 29, 519-526.
    • (1989) J. Basic Microbiol. , vol.29 , pp. 519-526
    • Sandhu, D.K.1    Puri, R.2
  • 27
    • 77956068592 scopus 로고
    • Comparative cellulase isozyme pattern in different fungi
    • Sandhu, D. K., Puri, R., and Singh, S. (1991). "Comparative cellulase isozyme pattern in different fungi," Adv. Biosci. 10, 111-120.
    • (1991) Adv. Biosci. , vol.10 , pp. 111-120
    • Sandhu, D.K.1    Puri, R.2    Singh, S.3
  • 28
    • 84985730466 scopus 로고
    • Single cell protein production by Trichoderma longibrachiatum on treated sugar-cane bagasse
    • Sidhu, M. S., and Sandhu, D. K. (1980). "Single cell protein production by Trichoderma longibrachiatum on treated sugar-cane bagasse," Biotechnol. Bioeng. 22, 689-692.
    • (1980) Biotechnol. Bioeng. , vol.22 , pp. 689-692
    • Sidhu, M.S.1    Sandhu, D.K.2
  • 29
    • 9544230528 scopus 로고
    • Some aspects of cellulase enzyme complex in fungi
    • K. G. Mukerji, V. P. Agnihotri, and R. P. Singh (eds.), Print House (India), Lucknow
    • Sidhu, M. S., Sandhu, D. K., Sandhu, R. S., and Kalra, M. K. (1984). "Some aspects of cellulase enzyme complex in fungi," In: Progress in Microbial Ecology. K. G. Mukerji, V. P. Agnihotri, and R. P. Singh (eds.), Print House (India), Lucknow, pp. 527-547.
    • (1984) Progress in Microbial Ecology , pp. 527-547
    • Sidhu, M.S.1    Sandhu, D.K.2    Sandhu, R.S.3    Kalra, M.K.4
  • 30
    • 0344780787 scopus 로고    scopus 로고
    • Localization and optimization of cellulase production in Chaetomium erraticum
    • Soni, R., Sandhu, D. K., and Soni, S. K. (1999). "Localization and optimization of cellulase production in Chaetomium erraticum," J. Biotechnol. 73, 43-51.
    • (1999) J. Biotechnol. , vol.73 , pp. 43-51
    • Soni, R.1    Sandhu, D.K.2    Soni, S.K.3
  • 31
    • 77956071349 scopus 로고    scopus 로고
    • Qualitative and quantitative variability in cellulase enzyme complex and isozyme polymorphism of endo-β-1,4-glucanase and β-glucosidase in Chaetomium species
    • Soni, R., Sandhu, D. K., and Soni, S. K. (2005). "Qualitative and quantitative variability in cellulase enzyme complex and isozyme polymorphism of endo-β-1,4-glucanase and β-glucosidase in Chaetomium species," J. Basic Appl. Mycol. 4, 32-42.
    • (2005) J. Basic Appl. Mycol. , vol.4 , pp. 32-42
    • Soni, R.1    Sandhu, D.K.2    Soni, S.K.3
  • 33
    • 0017228551 scopus 로고
    • The control of Neurospora crassa morphology by cyclic adenosine 3′5-monophosphate and dibutylryl cyclic adenosine 3′-5′ mono phosphate
    • Terenzi, H. F., Flawia, M. M., Tellezinon, M.T., and Torres, H. N. (1976). "The control of Neurospora crassa morphology by cyclic adenosine 3′5-monophosphate and dibutylryl cyclic adenosine 3′-5′ mono phosphate," J. Bacteriol. 126, 91-99.
    • (1976) J. Bacteriol. , vol.126 , pp. 91-99
    • Terenzi, H.F.1    Flawia, M.M.2    Tellezinon, M.T.3    Torres, H.N.4
  • 34
    • 45449118076 scopus 로고    scopus 로고
    • An acidic and thermostable carboxymethyl cellulose from the yeast Cryptococcus sp. S-2: Purification, characterization and improvement of its recombinant enzyme production by high cell-density fermentation of Pichia pastoris
    • Thongekkaew, J., HirokoIkeda, H., Masaki, K., and Iefuji, H. (2008). "An acidic and thermostable carboxymethyl cellulose from the yeast Cryptococcus sp. S-2: Purification, characterization and improvement of its recombinant enzyme production by high cell-density fermentation of Pichia pastoris," Protein Expression Purif. 60, 140-146.
    • (2008) Protein Expression Purif. , vol.60 , pp. 140-146
    • Thongekkaew, J.1    HirokoIkeda, H.2    Masaki, K.3    Iefuji, H.4
  • 35
    • 0018989542 scopus 로고
    • Cellulase induction in Aspergillus fumigatus M-216
    • Trivedi, L. S., and Rao, K. K. (1980). "Cellulase induction in Aspergillus fumigatus M-216," Ind. J. Exp. Biol. 18, 240-242.
    • (1980) Ind. J. Exp. Biol. , vol.18 , pp. 240-242
    • Trivedi, L.S.1    Rao, K.K.2
  • 36
    • 0000340165 scopus 로고
    • Chemical and genetic control of induction of monokaryotic fruiting bodies in Coprinus macrorhizus
    • Uno, I., and Ishikawa, T. (1971). "Chemical and genetic control of induction of monokaryotic fruiting bodies in Coprinus macrorhizus," Mol. Gen. Genet. 113, 228-239.
    • (1971) Mol. Gen. Genet. , vol.113 , pp. 228-239
    • Uno, I.1    Ishikawa, T.2
  • 37
    • 0001963674 scopus 로고
    • A convenient growth medium for Neurospora (Medium N)
    • Vogel, H. J. (1956). "A convenient growth medium for Neurospora (Medium N)," Microbial Gen. Bull. 13, 42-43.
    • (1956) Microbial Gen. Bull. , vol.13 , pp. 42-43
    • Vogel, H.J.1
  • 38
    • 0005264410 scopus 로고    scopus 로고
    • Studies of the regulation of cellulase systems by ATP and cAMP in mycelial fungi
    • Wang, D. Z., Zu, Y., and Gao, P. (1996). "Studies of the regulation of cellulase systems by ATP and cAMP in mycelial fungi," Weishengwu Xuebao 36, 12-18.
    • (1996) Weishengwu Xuebao , vol.36 , pp. 12-18
    • Wang, D.Z.1    Zu, Y.2    Gao, P.3


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