Abstract
A commercial fungal β-glucanase preparation was immobilized by various methods including adsorption to DEAE-cellulose, cross-linking with glutaraldehyde, adsorption to a phenol-formaldehyde resin (Duolite) and to perlite followed by fixation with glutaraldehyde, covalent binding to glutaraldehyde-treated, partially hydrolyzed or partially aminolyzed nylon, and covalent binding in the Ugi-reaction to polyisonitrile-nylon. The recovery of enzymatic activity varied from 0.02 to 4.5% and the immobilized enzyme preparations showed specific activities from 1 to 25% of that of the starting material.
DEAE-cellulose-, nylon- and Duolite-β-glucanase were used in packed bed reactors for continuous hydrolysis of barley β-glucan. The Duolite-β-glucanase was most active in depolymerizing this polysaccharide.
The action pattern of insoluble crude β-glucanase (Duolite-β-glucanase) on barley β-glucan was very different from that of the crude enzyme preparation in solution. Comparison with the mode of action of a homogeneous preparation of endo-1,4-β-glucanase in dissolved and immobilized form, respectively, indicated that this change in action pattern was partly due to coimmobilization of enzymes catalyzing consecutive steps in the hydrolysis of barley β-glucan to glucose and partly to steric hindrance of the interaction between the immobilized enzyme and the interior regions of the substrate.
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Svensson, B., Ottesen, M. Immobilization of β-glucanase and studies on its degradation of barley β-glucan. Carlsberg Res. Commun. 43, 5–14 (1978). https://doi.org/10.1007/BF02906545
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DOI: https://doi.org/10.1007/BF02906545