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β-Fructofuranosidase was immobilized covalently on the oxidized microbial wall of a Penicillium spp. $quot;PS-8$quot;, which is totally different from the conventional whole cell immobilization in concept. The immobilization of β-fructofuranosidase by a series of treatments; oxidation of microbial cells with sodium metaperiodate, enzyme loading on the oxidized cells, extrusion, and crosslinking induced by glutaradehyde, were carried out. The final product had a good mechanical strength and showed 26% of the applied enzyme activity. The specific activity was 750 units per g of the dry cell product. The immobilized enzyme showed the kinetic parameters as follows; optimum pH at 5, optimum temperature at 55, activation energy of 19kJ ㏖^(-1), and apparent Km of 55 mM.
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