The cellulose-binding domain (CBDCex) of an exoglucanase fromCellulomonas fimi: Production inEscherichia coli and characterization of the polypeptide

1993 ◽  
Vol 42 (4) ◽  
pp. 401-409 ◽  
Author(s):  
Edgar Ong ◽  
Neil R. Gilkes ◽  
Robert C. Miller ◽  
R. Antony J. Warren ◽  
Douglas G. Kilburn
Keyword(s):  
Binding Domain ◽  
Inescherichia Coli ◽  
Cellulose Binding Domain ◽  
Cellulose Binding

scholarly journals Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A.

1993 ◽  
Vol 175 (18) ◽  
pp. 5762-5768 ◽  
Author(s):  
M A Goldstein ◽  
M Takagi ◽  
S Hashida ◽  
O Shoseyov ◽  
R H Doi ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Clostridium Cellulovorans ◽  
Cellulose Binding

Characterization of aNeocallimastixpatriciarumxylanase gene and its product

1999 ◽  
Vol 45 (11) ◽  
pp. 970-974 ◽  
Author(s):  
Jin-Hao Liu ◽  
Brent L Selinger ◽  
Cheng-Fang Tsai ◽  
Kuo-Jaon Cheng
Keyword(s):  
Catalytic Domain ◽  
Xylanase Activity ◽  
Binding Domain ◽  
Glycosyl Hydrolases ◽  
Cellulose Binding Domain ◽  
Xylanase Gene ◽  
Neocallimastix Patriciarum ◽  
Cellulose Binding ◽  
Linker Domain

A xylanase gene (xynC) isolated from the anaerobic ruminal fungus Neocallimastix patriciarum was characterized. The gene consists of an N-terminal catalytic domain that exhibited homology to family 11 of glycosyl hydrolases, a C-terminal cellulose binding domain (CBD) and a putative dockerin domain in between. Each domain was linked by a short linker domain rich in proline and alanine. Deletion analysis demonstrated that the CBD was essential for optimal xylanase activity of the enzyme, while the putative dockerin domain may not be required for enzyme function.Key words: xylanase, cellulose binding domain, Neocallimastix patriciarum.

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