Purification, characterization and modular organization of a cellulose-binding protein, CBP105, a processive b-1,4-endoglucanase from Cellulomonas flavigena

A cellulose-binding protein of 105 kDa (CBP105) from Cellulomonas flavigena was purified and its gene was cloned. CBP105 is a processive endoglucanase with maximum activity on carboxymethyl cellulose (CMC) at pH 7.5 and 60C. Limited proteolysis suggested that CBP105 is composed of one catalytic doma...

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Bibliographic Details
Published in:Biotechnology letters 2008-04, Vol.30 (4), p.681-687
Main Authors: Mejia-Castillo, Teresa, Hidalgo-Lara, Maria Eugenia, Brieba, Luis G, Ortega-Lopez, Jaime
Format: Article
Language:English
Subjects:
Cellulomonas flavigena
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Summary:A cellulose-binding protein of 105 kDa (CBP105) from Cellulomonas flavigena was purified and its gene was cloned. CBP105 is a processive endoglucanase with maximum activity on carboxymethyl cellulose (CMC) at pH 7.5 and 60C. Limited proteolysis suggested that CBP105 is composed of one catalytic domain (CD) and two carbohydrate-binding modules (CBM). The nucleotide sequence of the cbp105 gene (AY729806) indicates that CBP105 is a modular enzyme with a family 9 glycoside hydrolase CD linked to a family 3 CBM, two fibronectin III-like domains and a family 2 CBM. This structural organization may be responsible for CBP105 processive CMC degradation.
ISSN:0141-5492
DOI:10.1007/s10529-007-9589-x