Douglas G. Kilburn

TL;DR: The beta-1, 4-glycanases appear to have arisen by the shuffling of a relatively small number of progenitor sequences, and some of the enzymes contain repeated sequences up to 150 amino acids in length.

TL;DR: Two enzymes prepared from Escherichia coli expressing recombinant DNA of the cellulolytic bacterium Cellulomonas fimi cleaved both enzymes in vivo in a highly specific manner, implying a critical role for the binding domain of CenA in the hydrolysis of crystalline substrate.

TL;DR: It is shown that the isolated cellulose binding domain of endoglucanase A (GenA) from the bacterium Cellulomonas fimi disrupts the structure of cellulose fibres and releases small particles but has no detectable hydrolytic activity.

TL;DR: A new model for adsorption was developed to describe the interaction of a large ligand (protein) with a lattice of overlapping potential binding sites (cellobiose residues) and a relative equilibrium association constant (Kr) of 40.5 and 45.3 liter was estimated for CenA and CBD.

TL;DR: It is shown that naturally occurring cellulases with similar catalytic activity on a model cellulosic substrate can differ significantly in their affinities for lignin, indicating the presence of lignIn-binding sites on the catalytic domain.