Partial purification and characterization of the cellulases from clostridium cellulolyticum h10

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Abstract
The extracellular cellulolytic complex from Clostridium cellulolyticum H10 has been isolated and partially characterized. Through application of gel filtration and ion exchange chromatography techniques it has been established that in its native state this complex essentially consists of highly stable macromolecular structures (Mr c. 20 000 kDa) (similar to those described for different cellulolytic bacteria and currently termed cellulosomes) exhibiting avicelase, carboxymethylcellulase (CMCase) and xylanase activities. Furthermore, immunoaffinity assays show that this extracellular cellutosomal form of the complex is immunochemically similar to the cell‐associated form.Another feature of the C. cellulolyticum H10 complex is that the Avicel‐adsorbed fraction consists essentially of three major components, two of them (those of 160–170 and 72 kDa) having no detectable activity and one (that of 95 kDa) being associated with strong CMCase activity.