scholarly journals The cellulose-binding domain of the major cellobiohydrolase of Trichoderma reesei exhibits true reversibility and a high exchange rate on crystalline cellulose.

1996 ◽  
Vol 93 (22) ◽  
pp. 12251-12255 ◽  
Author(s):  
M. Linder ◽  
T. T. Teeri
Keyword(s):  
Exchange Rate ◽  
Trichoderma Reesei ◽  
Binding Domain ◽  
Crystalline Cellulose ◽  
Cellulose Binding Domain ◽  
Cellulose Binding

Visualization of the adsorption of a bacterial endo-β-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose

1993 ◽  
Vol 15 (6) ◽  
pp. 347-351 ◽  
Author(s):  
N.R. Gilkes ◽  
D.G. Kilburn ◽  
R.C. Miller ◽  
R.A.J. Warren ◽  
J. Sugiyama ◽  
...  
Keyword(s):  
Binding Domain ◽  
Crystalline Cellulose ◽  
Cellulose Binding Domain ◽  
Cellulose Binding

Analogs of the cellulose binding domain of cellobiohydrolase I from Trichoderma reesei: Synthesis and binding

Peptides 1992 ◽  
1993 ◽  
pp. 780-781
Author(s):  
Gunnar Lindeberg ◽  
Per Hansen ◽  
Jerry Ståhlberg ◽  
Göran Pettersson
Keyword(s):  
Trichoderma Reesei ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Cellobiohydrolase I ◽  
Cellulose Binding

scholarly journals The non-catalytic C-terminal region of endoglucanase E from Clostridium thermocellum contains a cellulose-binding domain

1991 ◽  
Vol 273 (2) ◽  
pp. 289-293 ◽  
Author(s):  
A J Durrant ◽  
J Hall ◽  
G P Hazlewood ◽  
H J Gilbert
Keyword(s):  
Amino Acids ◽  
Clostridium Thermocellum ◽  
Catalytic Domain ◽  
Specific Activity ◽  
Binding Domain ◽  
Full Length ◽  
Crystalline Cellulose ◽  
Cellulose Binding Domain ◽  
Beta Glucan ◽  
Cellulose Binding

Mature endoglucanase E (EGE) from Clostridium thermocellum consists of 780 amino acid residues and has an Mr of 84,016. The N-terminal 334 amino acids comprise a functional catalytic domain. Full-length EGE bound to crystalline cellulose (Avicel) but not to xylan. Bound enzyme could be eluted with distilled water. The capacity of truncated derivatives of the enzyme to bind cellulose was investigated. EGE lacking 109 C-terminal residues (EGEd) or a derivative in which residues 367-432 of the mature form of the enzyme had been deleted (EGEb), bound to Avicel, whereas EGEa and EGEc, which lack 416 and 246 C-terminal residues respectively, did not. The specific activity of EGEa, consisting of the N-terminal 364 amino acids, was 4-fold higher than that of the full-length enzyme. The truncated derivative also exhibited lower affinity for the substrate beta-glucan than the full-length enzyme. It is concluded that EGE contains a cellulose-binding domain, located between residues 432 and 671, that is distinct from the active site. The role of this substrate-binding domain is discussed.

The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain

2011 ◽  
Vol 155 (4) ◽  
pp. 370-376 ◽  
Author(s):  
Mélanie Hall ◽  
Jonathan Rubin ◽  
Sven H. Behrens ◽  
Andreas S. Bommarius
Keyword(s):  
Trichoderma Reesei ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Cellulose Binding
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