Abstract
Cellobiose dehydrogenase (CDH) is produced as an extracellular enzyme by many fungal species grown on cellulose and plant biomass. CDH is the flavoheme enzyme which oxidizes the end group of cellobiose to form the lactone via extraction of two electrons from the substrate to an appropriate electron acceptor. We investigated the electron transfer mechanism during the catalytic cycle of CDH and clarified a sophisticated regulatory function of cellobiose metabolism involving the interaction between the flavin and heme of CDH. In addition to its catalytic activity, CDH can bind to the amorphous surface of cellulose. These properties of CDH are important for understanding the fungal system of cellulose degradation and useful for application of CDH. We have developed a method for real-time and sensitive detection of cellulase activity using a CDH catalytic system and a method for surface analysis of cellulosic materials based on the evaluation of CDH adsorption.
