Adsorption and desorption of cellulase components during the hydrolysis of a steam‐exploded birch substrate ¹

Abstract

Using a chromatofocusing method, all of the cellulase components from a commercial cellulase preparation were found to adsorb to a steam‐exploded birch substrate. Both common and distinct binding sites for cellulase components were found to exist on the substrate. During hydrolysis of the substrate, the composition of the bound cellulase components remained unchanged and maintained a similar proportion as that of the original cellulase mixture. The specific activity of cellulase components recovered in the reaction supernatant after about 80% of substrate conversion is similar to that of the original cellulase mixture. However, this accounts for only about 40‐50% of the total cellulase activity.