Kinetics of glucoamylase immobilized by ionic linkage and analysis of its adsorption and desorption processes
| Autor: | Ryuichi Matsuno, Shuji Adachi, Tadashi Kamikubo, Kazuhiro Nakanishi, Yasuko Kawamura |
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| Rok vydání: | 1978 |
| Předmět: | |
| Zdroj: | Agricultural and Biological Chemistry. 42:1707-1714 |
| ISSN: | 1881-1280 0002-1369 |
| DOI: | 10.1271/bbb1961.42.1707 |
| Popis: | Glucoamylase (from Rhizopus niveus) was immobilized to SP-Sephadex C-25 and C-50 by ionic linkage. The kinetic and physical properties of the immobilized glucoamylase were quantitatively investigated using maltose as substrate. The change of kinetic parameters, k0, and Km, due to immobilization was explained in terms of decrease of pH in the ion exchanger, which was estimated from Donnan's equilibrium. Binding equilibrium between the enzyme and the ion exchanger was investigated. A linear relationship between the concentrations of enzymes in the ion exchanger and in the outer solution phase was observed over a wide range of enzyme concentrations. Distribution coefficients were obtained, by which the amount of the enzyme immobilized can be calculated. Diffusion coefficients of the enzyme in the ion exchanges were also estimated from analysis of the adsorption process. A theoreti-cal equation to predict the half-life of the activity of immobilized enzymes caused by desorption of the enzymes was proposed in terms of the distribution coefficient, the diffusion coefficient and the operational variables of a continuous reaction. |
| Databáze: | OpenAIRE |
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