Kinetic-thermodynamic aspects of catalysis of polysaccharides by native end immobilized amylases

It was shown that covalent immobilization of 1.4-alpha-glucanohydrolase (glucoamylase) and 2.1-beta-D-fructanfructanohydrolase (inulase) on ionites leads to an increase in the activation energy Eact of hydrolysis of polysaccharides and a change in entalphy delta H as compared with native enzymes. During binding to the matrix, multipoint interactions of polypeptide chains with active groups take place, which are accompanied by an increase in the Michaelis constant KM, a decrease in the maximum rate of hydrolysis Vmax, and a substantial decrease in the constant of conformational transition L0. It was also shown that the kinetics of the hydrolysis of starch and inulin upon immobilization of glucoamylase and inulase on ionites does not correspond to the Michaelis-Menten equiation and is characterized by a shift of equilibrium from state R to state T.