Biotechnology and Bioprocess Engineering:BBE

The Korean Society for Biotechnology and Bioengineering (한국생물공학회)
권호 표지

Description of Cellobiohydrolases Ce16A and Ce17A from Trichoderma reesei Using Langmuir-type Models

  • Kim, Dong-Won (Department of Chemistry, Physical Chemistry Laboratory, College of Natural Sciences, Chungbuk National University) ;
  • Hong, Young-Gwan (Department of Chemistry, Physical Chemistry Laboratory, College of Natural Sciences, Chungbuk National University)
  • Published : 2001.03.01
Download PDF
⟨ Previous Next ⟩

Abstract

The binding of cellobiohydrolases to cullulose is a crucial initial step in cellulose hydrolysis. In the search for a detailed understanding of the function of cellobiohydrolases, much information concerning how the enzymes and their constituent catalytic and cellulose-binding changes during hydrolysis is still needed. The adsorption of purified two cellobiohydrolases (Ce17A and Ce16A) from Trichoderma reesei cellulase to microcrystalline cellulose has been studied. Cellobiohydrolase II (Ce16A) does not affect the adsorption of cellobiohydrolase I (Ce17A) significantly, and there are specific binding sites for both Ce17A and Ce16A. The adsorption affinity and tightness of the cullulase binding domain (CBD) for Ce17A are larger than those of the CBD for Ce16A. The CBD for Ce17A binds more rapidly and tightly to Avicel than the CBD for Ce16A. The decrease in adsorption observed when the two cellobihydrolases are studied together would appear to be the result of competition for binding sites on the cellulose. Ce17A competes more efficiently for binding sites than Ce16A. Competition for binding sites is the dominating factor when the two enzymes are acting together, furthermore adsorption to sites specific for Ce17A and Ce16A, also contributes to the total adsorption.

Keywords

References

  1. Trends Biotechnol. v.15 Crystalline cellulose degradation: New insights into the function of cellobiohydrolases Teeri T.T.
  2. Biochemistry v.35 Identification of two functionally different classes of exocellulases Barr B.K.;Y.L. Hsieh;B. Ganem;D.B. Wilson
  3. FEBS Lett. v.425 Scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants Henrissat S.;T.T. Teeri;R.A. Warren
  4. Bioresoures Technol. v.36 Synergism in cellulase systems Woodward J.
  5. FEBS Lett. v.119 The 1.4-β-glucar cellobiohydrolase of Trichoderma reesi QM 9414;A new type of cellulolytic synergism Fagerstam L.G.;L.G. Pettersson
  6. Eur. J. Biochem. v.170 Studies of the cellulolytic system of Trichoderma reesei QM 9414: Analysis of domain function in two cellobiotydrolases by limited proteolysis Tomme P.;H. van Tilbeurgh;G. Pettersson;J. van Damne;J. Vandekerckhove;J. Knowles;T. Teeri;M. Claeyssens
  7. Trends Biotechnol. v.5 Cellulase familes and their genes Knowles J.;P. Lehtovaara;T. Teeri
  8. Trends Biotechnol. v.7 The cellulasebinding domains of cellulases: Tools for biotechnology Ong E.;J.M. Greenwood;N.R. Gilkes;D.G. Kilburn;R.C. Miller Jr;R.A.J. Warren
  9. FEBS Lett. v.243 Isolated fungal cellulase terminal domains and synthetic minimum analogue bind to cellubse Johansson G.;J. Sthlberg;G. Lindeberg;A. EngstrOm;G. Pettersson
  10. Biotechnol. Lett. v.19 Adsorption behaviors of two cellobiohydrolases and their core proteins from Trichoderma reesei on Avicel PH 101 Kim D.W.;Y.H. Jang;Y.K. Jeon
  11. Appl. Biochem. Biotechnol. v.81 Adsorption and activity of Trichoderma reesei cellobiohydrolase Ⅰ,endoglucanase Ⅱ, and the corresponding core proteins on steam pretreated willow Kotiranta P.;J. Karlsson;M. Siika-Aho;J. Medve;L. Viikari;M. Tjerneld;M. Tenkanen
  12. Biochemistry v.28 Determination of the three-dimensional Solution structure of the C-terminal domain of celloboohydrolase I from Trichoderma reesei Kraulis P.;M. Clore;M. Nilges;A. Jones;G. Pettersson;J. Knowles;A. Gronenboru
  13. Biochem. J. v.234 The cellulase of Penicillium pinophilium Wood T.M.;S.I. McCrae
  14. Biotechnol. Bioeng. v.27 Analysis of cellulose-cellulase adsorption data: A fundamental approach Stuart J.Y.;D.L. Ristroph
  15. Biotechnol. Bioeng. v.19 Adsorption of Trichoderma cellulase on cellulose Peitersen N.;J. Medeiros;M. Mandels
  16. J. Appl. Biochem. v.6 Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414 Bhikhabhai R.;G. Iohansson;G. Pettersson
  17. Laboratory Experiments in Biological Chemistry Summer J.B.;G.F. Somers
  18. J. Chromatogr. v.396 Analytical separation of Trichoderma reesei: cellulase by ion exchange fast protein liquid chromatography Ellouz S.;H. Durand;G. Tiraby
  19. Biotechnol. Bioeng. v.30 Adsorption and kinetic behavior of purified endoglucanase and exoglucanases from Trichoderma viride Belldman G.;A.G.J. Voragen;F.M. Rombouts;M.F. Scarle-van Leeuwen;W. Pilnik
  20. Bio/Technology v.9 A new model for enzymatic hydrolysis of cellulose based on the two-domain structure of cellobiohydrolase Stahlberg J.;G. Johansson;G. Pattersson
  21. Process Biochem. v.17 Elution of cellulase from cellulose Reese E.T.
  22. Bio/Technology v.6 Hydrolysis of cellulose by saturation and non-saturating concentrations of cellulose: Implications for synergism Woodward J.;M.K. Hayes;N.E. Lee
  23. Enzyme Microb. Technol. v.10 Effect of physical parameters on the adsorption characteristics of fractionated Trichoderma reesei cellulase components Kyriacou A.;R.J. Neufeld;C.R. MacKenzie
  24. FEBS Lett. v.172 Colloidal gold labeling of 1,4-beta-D-glucan cellobiohydrolase adsorbed on cellulose substrates Chanzy H.;B. Henrissat;R. Vuong