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A study was made to determine the controlling mass transfer resistance in the overall reaction rate for conversion of maltose to glucose, catalyzed by glucoamylase immobilized onto porous glass. For normal operation of a packed column and air‐stirred batch reactor, the rate controlling step was found to be the internal resistance of simultaneous pore diffusion and chemical reaction. Experimental effectiveness factors were determined and are compared with those derived from a theoretical diffusion model based on Michaelis‐Menten kinetics. Also given are temperature and pH relationships for the free and immobilized glucoamylase.
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Marsh et al. (1973) studied this question.
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