Inhibition of Cellulases

Publisher Website
Google Scholar
Abstract
Cellulases are remarkably stable to pH and temperature changes and to chemical inhibitors. They are competitively inhibited by cellobiose and methocel and inactivated by such protein reactants as halogens, heavy metals, and detergents. A type of polymeric leucoanthocyanin found in many plants, notably in the unripe fruit of persimmon, is a powerful, but nonspeciiic inhibitor of cellulase. The susceptibility of cellulases to chemical inhibitors increases with purification. The C1 component, which allows cellulase to attack insoluble cellulose, is more labile than the hydrolytic Cx components. Formation of cellulolytic enzymes is repressed by growth on sugars. There are 134 referenees.