An investigation of the properties of glucoamylase immobilized on glass beads involving 5-diazosalicylic acid bonded to a titanium (IV) oxide film |
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| Authors: | John F. Kennedy Martin F. Chaplin |
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| Affiliation: | Research Laboratory for Chemistry of Bioactive Carbohydrates and Proteins, Department of Chemistry, University of Birmingham, P.O. Box 363, Birmingham B15 2TT, UK |
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| Abstract: | Optimum conditions have been determined for the immobilization of glucoamylase on glass involving diazotized 5-aminosalicylic acid bonded to a deposited imperfectly crystallized film of TiO2. The changes in the kinetic and thermodynamic characteristics of the enzyme on immobilization have been determined. There are significant differences in the behaviour of the immobilized enzyme towards its substrates, maltose and starch. The apparent Km for starch increased on immobilization whereas that for maltose decreased. The pH optimum for the immobilized preparation showed a shift to acid pH relative to that of the free enzyme. |
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