Immobilized enzymes: electrokinetic effects on reaction rates in a porous medium.
The effect of the internal diffusion and electrical surface charge on the overall rate of a reaction catalyzed by an enzyme immobilized on a porous medium are examined. Effectiveness factors have been calculated which compare the global reaction rate to that existing in the absence of the internal diffusion and/or the electrical field. The surface charge, assumed to arise from the dissociation equilibria of the acidic and basic surface groups of the enzyme, generates an electrical double layer at the pore surface. The double-layer potential is governed by the Poisson-Boltzmann equation. It is shown that the diffusion potential can be characterized by a modulus which depends upon the surface reaction rate, the charges and diffusivities of the substrate and products, the ionic strength, and the pore dimensions. The flux of a charged species in the pore occurs under the influences of the concentration gradient and the electrical potential gradient. The governing equations are solved by an iterative numerical method. The effects of pH, enzyme concentration, and substrate concentration on the rates of two different hydrolysis reactions catalyzed by immobilized papain are examined. The release of H(+) in one of the reactions causes the lowering of internal pH, and also a constancy of the internal pH when the external pH in creases beyond a certain value. The latter reaction also shows a maximum in the reaction rate with respect to enzyme concentration. The reaction not involving H(+) as a product shows a maximum in the reaction rate with respect to external pH, but a monotonic increase in the reaction rate as the enzyme concentration increases.
State University of New York at Buffalo, Department of Chemical Engineering, Amherst, New York 14260, USA.
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Ruckenstein
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Kalthod