Related Experiment Video
Updated: Jul 10, 2026

Expression of Recombinant Cellulase Cel5A from Trichoderma reesei in Tobacco Plants
Published on: June 13, 2014
Purification, characterization and modular organization of a cellulose-binding protein, CBP105, a processive
Teresa Mejia-Castillo1, Maria Eugenia Hidalgo-Lara, Luis G Brieba
1Departamento de Biotecnología y Bioingeniería, Centro de Investigación y de Estudios Avanzados del Instituto Politécnico Nacional (CINVESTAV-IPN), Av. IPN 2508, Col. San Pedro Zacatenco, 07360 México, DF, México.
Abstract:
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 60 degrees C. 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.
Related Concept Videos
Role of Microtubules in Cell Wall Deposition
Cellulose and Pectic Polysaccharides
As a cell matures, its cell wall specializes according to its type. For example, the parenchyma cells of...
Protein Folding Quality Check in the RER
Oligosaccharide Assembly
Multiple sugar molecules that may or may...

