Enzymatic degradation of guar galactomannan is studied using gel permeation chromatography (GPC) and steady shear viscometry. In very dilute polymer solutions, reaction rate increases with first-order kinetics with substrate concentration. In the intermediate concentration regime, the enzyme/polymer binding saturates, and the degradation kinetics is zero-order. The observations are in accord with a Michaelis-Menton kinetics model. The Michaelis-Menton parameter, K-m and V-max, were determined to be 0.6 mM and 7.8 x 10(-10) mol/(mL s) for guar at pH = 7, where the maximal velocity of the reaction, V-max, was measured in terms of the molar concentration of glycosidic bonds broken per unit time. However, as the solution increases in concentration, the reaction rate decreases and the enzyme diffusion through the concentrated polymer gel becomes a limiting factor. A reaction-diffusion model is presented to express the competition between enzyme reaction and diffusion. The scaling theory and kinetic data are used to define the boundaries of the polymer concentration regimes between substrate (i.e., polymer strand) limited reactions, enzyme limited reactions. and hindered diffusion limited reactions. The influence of polymer derivatization on the degradation kinetics was also explored. The degradation rate was shown to be greatly affected by the type of substituent groups as well as the degree of substitution. The triggering mechanism and controlled degradation were found for the enzymatic hydrolysis of cationically derivatized guar solutions.