Tuesday, May 3, 2011
Substrate promiscuity has been found in glycoside hydrolases for a long time. Some glycoside hydrolases have the ability to hydrolyze polysaccharides or oligosaccharides composed of different sugar units with identical linkages. This phenomenon is interesting from a scientific and engineering perspective. For industrial applications, glycoside hydrolases with different substrate activities are an attractive option for the hydrolysis of complex biomass containing different polysaccharides. From a scientific point of view, research on the substrate promiscuity of glycoside hydrolases on a molecular level is still in its infancy. In this work, we examined a thermostable cellulase, Cel5A, from Thermotoga maritima as a model to study the substrate specificity of several key residues were predicted to be essential for its substrate specificity.