Active site as the heart of carbohydrases

Abstract

Studies of the catalytic activity of carbohydrases toward various polysaccharides and the data on the effect of the amino acid residues in the active site or in its vicinity on the activity of enzymes, their thermal stability, the pH optimum of the activity, and the susceptibility to inhibitors confirm the complexity of the spatial arrangement of their active site. The introduction of amino acid substitutions into carbohydrases made it possible to increase the activity of the enzymes, enhance the efficiency of polysaccharide hydrolysis, and increase the thermal stability of the enzymes and their resistance to inhibitors.