DETERMINATION OF CATALYTIC RATE CONSTANTS OF LYSOZYME CATALYZED REACTION BY A KINETIC ANALYSIS OF TRANSGLYCOSYLATION REACTION

摘要

1. A kinetic model, involving both mechanisms of hydrolysis and transglycosylation, for the lysozyme-catalyzed reaction of oligosaccharides is formulated.-n2. Numerically solving the kinetic equations, we have analyzed how the time-course profiles of the reaction depend on the rate-constants for the bond-cleavage, transglycosylation and hydration;k+1, k-1 and k+2, and of the binding constants for the sites OF, CD and EF;KC~F, KCD and KEF.n3. From the kinetic analysis, it is found that the ratio k-1,X KEF/k+2 determines the essential pattern of the distribution of the oligomer concentrations in the time-course graphs, and that the values of k+1, and k+2 with which the calculated graphs fit a single time-course graph of experiments are of the hyperbolic-like relation and cannot be determined inde¬pendently.