Binding of Thermobifida fusca CDCe15A, CDCe16B and CDCe148A to easily hydrolysable and recalcitrant cellulose fractions on BMCC

Enzyme and Microbial Technology

Volumn 31, Issue 7, 2002, Pages 941-948

  Jung, Hyungil ^a   Wilson, David B ^b   Walker, Larry P ^a  

^a Cornell University   (United States)

^b Department of Obstetrics Gynecology   (United States)

Author keywords

Catalytic domain (CD); Cellobiose; Easily hydrolysable; Endoglucanase; Exoglucanase; Recalcitrant; Thermobifida fusca

Indexed keywords

CATALYSIS; ENZYMES; HYDROLYSIS;

RECALCITRANT FRACTION;

BIOTECHNOLOGY;

CELLOBIOSE; CELLULOSE; GLUCAN GLUCOSIDASE; GLUCAN SYNTHASE;

ARTICLE; BINDING ASSAY; BINDING SITE; CATALYSIS; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME BINDING; ENZYME SUBSTRATE; HYDROLYSIS; MALE; MICROORGANISM; NONHUMAN; PROTEIN DOMAIN; SPECIES DIFFERENCE; TEMPERATURE DEPENDENCE; THERMOBIFIDA FUSCA; THERMODYNAMICS;

THERMOBIFIDA FUSCA;

EID: 2242420943     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(02)00181-3     Document Type: Article

References (38)

1. Van Tilbeurgh H., Tomme P., Claeyssens M., Bhikhabhai R., Pettersson G. Limited proteolysis of the cellobiohydrolase I from Trichoderma reesei: separation of functional domains. FEBS Lett. 204:1986;223-227.
2. Abuja P.M., Schmuck M., Pilz I., Tomme P., Claeyssens M., Esterbauer H. Structural and functional domains of cellobiohydrolase I from Trichoderma reesei. A small angle X-ray scattering study of the intact enzyme and its core. Eur. Biophys. J. 15:1988;339-342.
3. 2 gene in Streptomyces lividans: affinity purification and functional domains of the cloned gene product. Appl. Environ. Microbiol. 54:1988;2521-2526.
4. Gilkes N.R., Kilburn D.G., Miller R.C. Jr., Warren R.A.J. Structural and functional analysis of a bacterial cellulase by proteolysis. J. Biol. Chem. 264:1989;17802-17808.
5. Wilson D.B., Irwin D.C. Genetics and properties of cellulases. Adv. Biochem. Eng. Biotechnol. 65:1999;1-21.
6. Stone JE, Scallan AM, Donefer E, Ahlgren E. Digestibility as a simple function of a molecule of similar size to a celllulase enzyme. In: Cellulases and their Application. Washington, DC: American Chemical Society, 1969. p.219-41.
7. Fan L.T., Lee Y.H., Beardmore D.H. Mechanism of the enzymatic hydrolysis of cellulose: effects of major structural features of cellulose on enzymatic hydrolysis. Biotechnol. Bioeng. 22:1980;177-199.
8. Cowling E.B. Physical and chemical constraints in the hydrolysis of cellulose and lignocellulosic materials. Biotechnol. Bioeng. Symp. 5:1975;163-181.
9. Grethlein H.E. The effect of pore size distribution on the rate of enzymatic hydrolysis of cellulosic substrates. Bio/Technol. 3:1985;155-160.
10. Thompson D.N., Chen H.C., Grethlein H.E. Comparison of pretreatment methods on the basis of available surface area. Bioresour. Technol. 39:1992;155-163.
11. Gama F.M., Teixeira J.A., Mota M. Cellulose morphology and enzymatic reactivity: a modified solute exclusion technique. Biotechnol. Bioeng. 43:1994;381-387.
12. Carrard G., Linder M. Widely different off rates of two closely related cellulose-binding domains from Trichoderma reesei. Eur. J. Biochem. 262:1999;637-643.
13. Linder M., Teeri T.T. The roles and function of cellulose-binding domains. J. Biotechnol. 57:1997;15-28.
14. Linder M., Teeri T.T. The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose. Proc. Natl. Acad. Sci. U.S.A. 93:1996;12251-12255.
15. Jung H, Wilson DB, Walker LP. Binding mechanisms for Thermobifida fusca Ce15A, Ce16B and Ce148A cellulose binding modules on bacterial microcrystalline cellulose. Biotechnol Bioeng, in press.
16. 4 in cellulose hydrolysis. J. Bacteriol. 180:1998;1709-1714.
17. Nidetzky B., Steiner W., Claeyssens M. Cellulose hydrolysis by the cellulases from Trichoderma reesei: adsorptions of two cellobiohydrolases, two endocellulases and their core proteins on filter paper and their relation to hydrolysis. Biochem. J. 303:1994;817-823.
18. 5 and Trichoderma reesei CBHI. Enzyme Microbiol. Technol. 20:1997;411-417.
19. Kyriacou A., Neufeld R.J., MacKenzie C.R. Reversibility and competition in the adsorption of Trichoderma reesei cellulase components. Biotechnol. Bioeng. 33:1989;631-637.
20. Hanahan D. Transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:1983;557-580.
21. Lever M. A new reaction for colorimetric determination of carbohydrates. Anal. Biochem. 47:1972;273-279.
22. Sakata M., Ooshima H., Harano Y. Effects of agitation on enzymatic saccharification of cellulose. Biotechnol. Lett. 7:1985;689-694.
23. Lee S.B., Kim I.H., Ryu D.D.Y., Taguchi H. Structural properties of cellulose and cellulase reaction mechanism. Biotechnol. Bioeng. 25:1983;33-51.
24. Converse A.O., Matsuno R., Tanaka M. A model of enzyme adsorption and hydrolysis of microcrystalline cellulose with slow deactivation of the adsorbed enzyme. Biotechnol. Bioeng. 32:1988;38-45.
25. Ooshima H., Kurakake M., Kato J., Harano Y. Enzymatic activity of cellulase adsorbed on cellulose and its change during hydrolysis. Appl. Biochem. Biotechnol. 31:1991;253-266.
26. Nidetzky B., Steiner W. A new approach for modeling cellulase-cellulose adsorption and the kinetics of the enzymatic hydrolysis of microcrystalline cellulose. Biotechnol. Bioeng. 42:1993;469-479.
27. Väljamäe P., Sild V., Pettersson G., Johansson G. The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model. Eur. J. Biochem. 253:1998;469-475.
28. Matsuno R., Taniguchi M., Tanaka M., Kamikubo T. A model for hydrolysis of microcrystalline cellulose by cellulase. Ann. N.Y. Acad. Sci. 434:1984;158-160.
29. Zhang S., Irwin D.C., Wilson D.B. Site-directed mutation of noncatalytic residues of Thermobifida fusca exocellulase Cel6B. Eur. J. Biochem. 267:2000;3101-3115.
30. Divine C., Ståhlberg J., Teeri T.T., Jones T.A. High-resolution crystal structures reveal how a cellulose chain is bound in the 50A long tunnel of cellobiohydrolase I from Trichoderma reesei. J. Mol. Biol. 275:1998;309-325.
31. Warren R.A.J. Microbial hydrolysis of polysaccharides. Annu. Rev. Microb. 50:1996;183-212.
32. Parsiegla G., Juy M., Reverbel L.C., Tardif C., Belaich J.P., Driguez H.et al. The crystal structure of the processive endocellulase CelF of Clostridium cellulolyticum in complex with a thiooligosaccharide inhibitor at 2.0 Å resolution. EMBO J. 17:1998;5551-5562.
33. Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A. Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science. 249:1990;380-386.
34. Zou J., Kleywegt G., Ståhlberg J., Drigues H., Nerinckx W., Claeyssens M.et al. Crystalllographic evidence for ring distortion and protein conformational changes during catalysis in cellobiohydrolase Cel6A from Trichoderma reesei. Structure. 7:1999;1035-1042.
35. Varrot A., Schülein M., Davies G.J. Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form. J. Mol. Biol. 297:2000;819-828.
36. Davies G.J., Dauter M., Brzozowski A.M., Bjornvad M.E., Andersen K.V., Schulein M. Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 Å and its cellobiose complex at 2.0 Å resolution. Biochemistry. 37:1998;1926-1932.
37. Palonen H., Tenkanen M., Linder M. Dynamic interaction of Trichoderma reesei cellobiohydrolases Cel6A and Cel7A and cellulose at equilibrium and during hydrolysis. Appl. Environ. Microbiol. 65:1999;5229-5233.
38. Ståhlberg J., Johansson G., Pettersson G. A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase I. Bio/Technol. 9:1991;286-290.