The processive endoglucanase EngZ is active in crystalline cellulose degradation as a cellulosomal subunit of Clostridium cellulovorans

New Biotechnology

Volumn 29, Issue 3, 2012, Pages 365-371

  Jeon, Sang Duck ^a   Yu, Kyung Ok ^a   Kim, Seung Wook ^a   Han, Sung Ok ^a  

^a Korea University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC MODULES; CELLO-OLIGOSACCHARIDES; CELLOBIOSE; CELLULASE ACTIVITY; CLOSTRIDIUM CELLULOVORANS; COHESINS; CRYSTALLINE CELLULOSE; ENDOGLUCANASES; ENZYME COMPLEXES; GLYCOSYL HYDROLASES; HYDROLYSIS PRODUCTS; LIGNOCELLULOSIC BIOMASS; OPTIMAL ACTIVITY; PROTEIN SPOTS; REDUCING ENDS; SOLUBLE SUGARS; SPECIFIC ACTIVITY; TWO-DIMENSIONAL GEL ELECTROPHORESIS;

CLOSTRIDIUM; CRYSTALLINE MATERIALS; DEGRADATION; ELECTROPHORESIS; ENZYMES; HYDROLYSIS; SUGARS;

CELLULOSE;

CELLOBIOSE; CELLULASE; CELLULOSOME; GLUCAN SYNTHASE; GLUCAN SYNTHASE ENGZ; GLYCOSIDASE; MICROCRYSTALLINE CELLULOSE; OLIGOSACCHARIDE; SUGAR; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CLOSTRIDIUM CELLULOVORANS; CONTROLLED STUDY; DEGRADATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; VISCOSITY;

BACTERIAL PROTEINS; CELLOBIOSE; CELLULASE; CELLULOSE; CLOSTRIDIUM CELLULOVORANS; HYDROGEN-ION CONCENTRATION; MULTIENZYME COMPLEXES;

CLOSTRIDIUM CELLULOVORANS;

EID: 84856367884     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2011.06.008     Document Type: Article

References (35)

1. Sun Y., Cheng J. Hydrolysis of lignocellulosic materials for ethanol production: a review. Bioresour. Technol. 2002, 83:1-11.
2. Kumar R., et al. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J. Ind. Microbiol. Biotechnol. 2008, 35:377-391.
3. Das M., et al. Diversity of fungi, bacteria, and actinomycetes on leaves decomposing in a stream. Appl. Environ. Microbiol. 2007, 73:756-767.
4. Sleat R., et al. Isolation and characterization of an anaerobic, cellulolytic bacterium, Clostridium cellulovorans sp. nov. Appl. Environ. Microbiol. 1984, 48:88-93.
5. Ng T.K., et al. Cellulolytic and physiological properties of Clostridium thermocellum. Arch. Microbiol. 1977, 114:1-7.
6. Rincon M.T., et al. Novel organization and divergent dockerin specificities in the cellulosome system of Ruminococcus flavefaciens. J. Bacteriol. 2003, 185:703-713.
7. Doi R.H., Kosugi A. Cellulosomes: plant-cell-wall-degrading enzyme complexes. Nat. Rev. Microbiol. 2004, 2:541-551.
8. Doi R.H., et al. Cellulosomes from mesophilic bacteria. J. Bacteriol. 2003, 185:5907-5914.
9. Zverlov V.V., et al. A major new component in the cellulosome of Clostridium thermocellum is a processive endo-beta-1,4-glucanase producing cellotetraose. FEMS Microbiol. Lett. 2005, 249:353-358.
10. Bayer E.A., et al. Cellulosomes-structure and ultrastructure. J. Struct. Biol. 1998, 124:221-234.
11. Bayer E.A., et al. Cellulose, cellulases and cellulosomes. Curr. Opin. Struct. Biol. 1998, 8:548-557.
12. Chiriac A.I., et al. Engineering a family 9 processive endoglucanase from Paenibacillus barcinonensis displaying a novel architecture. Appl. Microbiol. Biotechnol. 2010, 86:1125-1134.
13. Arai T., et al. Properties of cellulosomal family 9 cellulases from Clostridium cellulovorans. Appl. Microbiol. Biotechnol. 2006, 71:654-660.
14. Cho W., et al. Cellulosomic profiling produced by Clostridium cellulovorans during growth on different carbon sources explored by the cohesin marker. J. Biotechnol. 2010, 145:233-239.
15. 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.
16. Hazlewood G.P., et al. Gene sequence and properties of CelI, a family E endoglucanase from Clostridium thermocellum. J. Gen. Microbiol. 1993, 139:307-316.
17. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
18. Jeon E., et al. Production of cellulosic ethanol in Saccharomyces cerevisiae heterologous expressing Clostridium thermocellum endoglucanase and Saccharomycopsis fibuligera beta-glucosidase genes. Mol. Cells 2009, 28:369-373.
19. Miller G.L.B.R., et al. Measurement of carboxymethyl cellulase activity. Anal. Biochem. 1960, 1:127-132.
20. Macek K., et al. Bibliography of paper and thin-layer chromatography 1961-1965 and survey of applications. J. Chromatogr. Suppl. 1968, 1:1-1041.
21. Murashima K., et al. Synergistic effects on crystalline cellulose degradation between cellulosomal cellulases from Clostridium cellulovorans. J. Bacteriol. 2002, 184:5088-5095.
22. Reverbel-Leroy C., et al. The processive endocellulase CelF, a major component of the Clostridium cellulolyticum cellulosome: purification and characterization of the recombinant form. J. Bacteriol. 1997, 179:46-52.
23. Zhang X.Z., et al. Glycoside hydrolase family 9 processive endoglucanase from Clostridium phytofermentans: heterologous expression, characterization, and synergy with family 48 cellobiohydrolase. Bioresour. Technol. 2010, 101:5534-5538.
24. Park J.S., et al. Cohesin-dockerin interactions of cellulosomal subunits of Clostridium cellulovorans. J. Bacteriol. 2001, 183:5431-5435.
25. Han S.O., et al. Regulation of expression of cellulosomes and noncellulosomal (hemi)cellulolytic enzymes in Clostridium cellulovorans during growth on different carbon sources. J. Bacteriol. 2004, 186:4218-4227.
26. Han S.O., et al. Transcription of Clostridium cellulovorans cellulosomal cellulase and hemicellulase genes. J. Bacteriol. 2003, 185:2520-2527.
27. Gilad R., et al. CelI, a noncellulosomal family 9 enzyme from Clostridium thermocellum, is a processive endoglucanase that degrades crystalline cellulose. J. Bacteriol. 2003, 185:391-398.
28. Gal L., et al. CelG from Clostridium cellulolyticum: a multidomain endoglucanase acting efficiently on crystalline cellulose. J. Bacteriol. 1997, 179:6595-6601.
29. Jauris S., et al. Sequence analysis of the Clostridium stercorarium celZ gene encoding a thermoactive cellulase (Avicelase I): identification of catalytic and cellulose-binding domains. Mol. Gen. Genet. 1990, 223:258-267.
30. Irwin D., et al. Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis. J. Bacteriol. 1998, 180:1709-1714.
31. Zhang Y.H., Lynd L.R. Toward an aggregated understanding of enzymatic hydrolysis of cellulose: noncomplexed cellulase systems. Biotechnol. Bioeng. 2004, 88:797-824.
32. Belaich A., et al. Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome. J. Bacteriol. 2002, 184:1378-1384.
33. Avitia C.I., et al. Temporal secretion of a multicellulolytic system in Myxobacter sp. AL-1. Molecular cloning and heterologous expression of cel9 encoding a modular endocellulase clustered in an operon with cel48, an exocellobiohydrolase gene. Eur. J. Biochem. 2000, 267:7058-7064.
34. Meinke A., et al. Unusual sequence organization in CenB, an inverting endoglucanase from Cellulomonas fimi. J. Bacteriol. 1991, 173:308-314.
35. Berger E., et al. Two noncellulosomal cellulases of Clostridium thermocellum, Cel9I and Cel48Y, hydrolyse crystalline cellulose synergistically. FEMS Microbiol. Lett. 2007, 268:194-201.