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Volumn 69, Issue , 2012, Pages 204-210

Co-production of a whole cellulase system in Escherichia coli

Author keywords

Cellulase; Cellulose; Co expression; Enzyme production; Enzymes; Escherichia coli

Indexed keywords

CELLULASE; CELLULOLYTIC ENZYME; CELLULOSE HYDROLYSIS; CO-EXPRESSION; CO-PRODUCTION; E. COLI; ENDOGLUCANASES; ENZYME PRODUCTION; EXOGLUCANASE; FILTER PAPERS; GLUCOSE PRODUCTION; GLUCOSE YIELDS; GLUCOSIDASE; SPECIFIC ACTIVITY; SYNERGISTIC ACTION; SYNERGISTIC EFFECT;

EID: 84867088743     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2012.09.011     Document Type: Article
Times cited : (22)

References (26)
  • 1
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: screening and selection strategies
    • Zhang Y.H.P., Himmel M.E., Mielenz J.R. Outlook for cellulase improvement: screening and selection strategies. Biotechnol. Adv. 2006, 24:452-481.
    • (2006) Biotechnol. Adv. , vol.24 , pp. 452-481
    • Zhang, Y.H.P.1    Himmel, M.E.2    Mielenz, J.R.3
  • 3
    • 76649123913 scopus 로고    scopus 로고
    • Improving enzymes for biomass conversion: a basic research perspective
    • Banerjee G., Scott-Craig J.S., Walton J.D. Improving enzymes for biomass conversion: a basic research perspective. Bioenerg. Res. 2010, 3:82-92.
    • (2010) Bioenerg. Res. , vol.3 , pp. 82-92
    • Banerjee, G.1    Scott-Craig, J.S.2    Walton, J.D.3
  • 5
    • 70349772781 scopus 로고    scopus 로고
    • Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina
    • Kubicek C.P., Mikus M., Schuster A., Schmoll M., Seiboth B. Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina. Biotechnol. Biofuels 2009, 2:1-14.
    • (2009) Biotechnol. Biofuels , vol.2 , pp. 1-14
    • Kubicek, C.P.1    Mikus, M.2    Schuster, A.3    Schmoll, M.4    Seiboth, B.5
  • 6
    • 80052499822 scopus 로고    scopus 로고
    • A minimal set of bacterial cellulases for consolidated bioprocessing of lignocellulose
    • Liao H., Zhang X.-Z., Rollin J.A., Zhang Y.-H.P. A minimal set of bacterial cellulases for consolidated bioprocessing of lignocellulose. Biotechnol. J. 2011, 6:1409-1418.
    • (2011) Biotechnol. J. , vol.6 , pp. 1409-1418
    • Liao, H.1    Zhang, X.-Z.2    Rollin, J.A.3    Zhang, Y.-H.P.4
  • 9
    • 79960713837 scopus 로고    scopus 로고
    • A whole cell biocatalyst for cellulosic ethanol production from dilute acid-pretreated corn stover hydrolyzates
    • Ryu S., Karim M.N. A whole cell biocatalyst for cellulosic ethanol production from dilute acid-pretreated corn stover hydrolyzates. Appl. Microbiol. Biotechnol. 2011, 91:529-542.
    • (2011) Appl. Microbiol. Biotechnol. , vol.91 , pp. 529-542
    • Ryu, S.1    Karim, M.N.2
  • 11
    • 84864417909 scopus 로고    scopus 로고
    • Cocktail production of an endo-β-xylanase and a β-glucosidase from Trichoderma reesei QM 9414 in Escherichia coli
    • Liu M., Yu H. Cocktail production of an endo-β-xylanase and a β-glucosidase from Trichoderma reesei QM 9414 in Escherichia coli. Biochem. Eng. J. 2012, 68:1-6.
    • (2012) Biochem. Eng. J. , vol.68 , pp. 1-6
    • Liu, M.1    Yu, H.2
  • 12
    • 0029988341 scopus 로고    scopus 로고
    • Substrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6
    • Damude H.G., Ferro V., Withers S.G., Warren R.A. Substrate specificity of endoglucanase A from Cellulomonas fimi: fundamental differences between endoglucanases and exoglucanases from family 6. Biochem. J. 1996, 315(Pt 2):467-472.
    • (1996) Biochem. J. , vol.315 , Issue.PART 2 , pp. 467-472
    • Damude, H.G.1    Ferro, V.2    Withers, S.G.3    Warren, R.A.4
  • 13
    • 0024297010 scopus 로고
    • Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis
    • Gilkes N.R., Warren R.A., Miller R.C., Kilburn D.G. Precise excision of the cellulose binding domains from two Cellulomonas fimi cellulases by a homologous protease and the effect on catalysis. J. Biol. Chem. 1988, 263:10401-10407.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10401-10407
    • Gilkes, N.R.1    Warren, R.A.2    Miller, R.C.3    Kilburn, D.G.4
  • 14
    • 0028180319 scopus 로고
    • Cellobiohydrolase-A (Cbha) from the cellulolytic bacterium Cellulomonas fimi is a beta-1,4-exocellobiohydrolase analogous to Trichoderma reesei Cbh-Ii
    • Meinke A., Gilkes N.R., Kwan E., Kilburn D.G., Warren R.A.J., Miller R.C. Cellobiohydrolase-A (Cbha) from the cellulolytic bacterium Cellulomonas fimi is a beta-1,4-exocellobiohydrolase analogous to Trichoderma reesei Cbh-Ii. Mol. Microbiol. 1994, 12:413-422.
    • (1994) Mol. Microbiol. , vol.12 , pp. 413-422
    • Meinke, A.1    Gilkes, N.R.2    Kwan, E.3    Kilburn, D.G.4    Warren, R.A.J.5    Miller, R.C.6
  • 15
    • 0043093279 scopus 로고    scopus 로고
    • Analysis of molecular size distributions of cellulose molecules during hydrolysis of cellulose by recombinant Cellulomonas fimi beta-1,4-glucanases
    • Stalbrand H., Mansfield S.D., Saddler J.N., Kilburn D.G., Warren R.A., Gilkes N.R. Analysis of molecular size distributions of cellulose molecules during hydrolysis of cellulose by recombinant Cellulomonas fimi beta-1,4-glucanases. Appl. Environ. Microbiol. 1998, 64:2374-2379.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2374-2379
    • Stalbrand, H.1    Mansfield, S.D.2    Saddler, J.N.3    Kilburn, D.G.4    Warren, R.A.5    Gilkes, N.R.6
  • 16
    • 0022478427 scopus 로고
    • Characterization and structure of an endoglucanase gene cenA of Cellulomonas fimi
    • Wong W.K., Gerhard B., Guo Z.M., Kilburn D.G., Warren A.J., Miller R.C. Characterization and structure of an endoglucanase gene cenA of Cellulomonas fimi. Gene 1986, 44:315-324.
    • (1986) Gene , vol.44 , pp. 315-324
    • Wong, W.K.1    Gerhard, B.2    Guo, Z.M.3    Kilburn, D.G.4    Warren, A.J.5    Miller, R.C.6
  • 17
    • 0036729340 scopus 로고    scopus 로고
    • Enzymatic properties and intracellular localization of the novel Trichoderma reesei beta-glucosidase BGLII (Cel1A)
    • Saloheimo M., Kuja-Panula J., Ylösmäki E., Ward M., Penttilä M. Enzymatic properties and intracellular localization of the novel Trichoderma reesei beta-glucosidase BGLII (Cel1A). Appl. Environ. Microbiol. 2002, 68:4546-4553.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4546-4553
    • Saloheimo, M.1    Kuja-Panula, J.2    Ylösmäki, E.3    Ward, M.4    Penttilä, M.5
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 20444401525 scopus 로고    scopus 로고
    • Microplate-based carboxymethylcellulose assay for endoglucanase activity
    • Xiao Z., Storms R., Tsang A. Microplate-based carboxymethylcellulose assay for endoglucanase activity. Anal. Biochem. 2005, 342:176-178.
    • (2005) Anal. Biochem. , vol.342 , pp. 176-178
    • Xiao, Z.1    Storms, R.2    Tsang, A.3
  • 20
    • 10844228836 scopus 로고    scopus 로고
    • Microplate-based filter paper assay to measure total cellulase activity
    • Xiao Z., Storms R., Tsang A. Microplate-based filter paper assay to measure total cellulase activity. Biotechnol. Bioeng. 2004, 88:832-837.
    • (2004) Biotechnol. Bioeng. , vol.88 , pp. 832-837
    • Xiao, Z.1    Storms, R.2    Tsang, A.3
  • 21
    • 84943470296 scopus 로고
    • Measurement of cellulase activities
    • Ghose T.K. Measurement of cellulase activities. Pure Appl. Chem. 1987, 59:257-268.
    • (1987) Pure Appl. Chem. , vol.59 , pp. 257-268
    • Ghose, T.K.1
  • 23
    • 0032937042 scopus 로고    scopus 로고
    • Molecular cloning and expression of the novel fungal beta-glucosidase genes from Humicola grisea and Trichoderma reesei
    • Takashima S., Nakamura A., Hidaka M., Masaki H., Uozumi T. Molecular cloning and expression of the novel fungal beta-glucosidase genes from Humicola grisea and Trichoderma reesei. J. Biochem. 1999, 125:728-736.
    • (1999) J. Biochem. , vol.125 , pp. 728-736
    • Takashima, S.1    Nakamura, A.2    Hidaka, M.3    Masaki, H.4    Uozumi, T.5
  • 24
    • 0037203041 scopus 로고    scopus 로고
    • Effect of gene location, mRNA secondary structures, and RNase sites on expression of two genes in an engineered operon
    • Smolke C.D., Keasling J.D. Effect of gene location, mRNA secondary structures, and RNase sites on expression of two genes in an engineered operon. Biotechnol. Bioeng. 2002, 80:762-776.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 762-776
    • Smolke, C.D.1    Keasling, J.D.2
  • 25
    • 79960614137 scopus 로고    scopus 로고
    • Fundamental relationship between operon organization and gene expression
    • Lim H.N., Lee Y., Hussein R. Fundamental relationship between operon organization and gene expression. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:10626-10631.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10626-10631
    • Lim, H.N.1    Lee, Y.2    Hussein, R.3
  • 26
    • 70350491151 scopus 로고    scopus 로고
    • Engineering multigene expression in vitro and in vivo with small terminators for T7 RNA polymerase
    • Du L.P., Gao R., Forster A.C. Engineering multigene expression in vitro and in vivo with small terminators for T7 RNA polymerase. Biotechnol. Bioeng. 2009, 104:1189-1196.
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 1189-1196
    • Du, L.P.1    Gao, R.2    Forster, A.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.