Investigations of stabilities,pH, and temperature profiles and kinetic parameters of glucoamylase immobilized on plastic supports |
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Authors: | M G Roig A Slade J F Kennedy D W Taylor M G Garaita |
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Institution: | (1) Departamento de Quimica Fisica, Facultad de Farmacia, Uniuersidad de Salamanca, Espa⋬;(2) Birmingham Carbohydrate and Technology Group, Research Laboratory for the Chemistry of Bioactive Carbohydrates and Proteins, School of Chemistry, Birmingham University, B15 2TT, UK |
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Abstract: | The covalent immobilization of glucoamylase on new epoxide-, isocyanate-, acid chloride-, and carboxylic acid-activated plastic
supports shows the viability of such supports for immobilizing enzymes (especially those reacting with 1,6-diaminohexane and
glutaraldehyde) for producing side arms. The operational stability of immobilized glucoamylase could be extended by crosslinking
the enzyme, by increasing the substrate concentration, or by extending the support’s side arm. The pH curves for the immobilized
enzyme were in general not found to be shifted from the pH optimum of the soluble enzyme. However, the immobilized enzyme’s
temperature activity profiles were shifted to a lower temperature range when compared to the soluble enzyme. The immobilized
glucoamylase Michaelis constants increased, and the maximum rates and specific activities decreased with respect to the soluble
enzyme kinetic parameters. |
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Keywords: | Stability pH temperature activity kinetic enzyme glucoamylase immobilization plastic supports |
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