Roig M G, Kennedy J F, Garaita M G
Departmento de Quimica Fisica, Facultad de Farmacia, Universidad de Salamanca, España.
J Biomater Sci Polym Ed. 1994;6(7):661-73. doi: 10.1163/156856294x00608.
Methods for the covalent immobilization of alpha-amylase and glucoamylase on to epoxide-, isocyanate-, acid chloride-, and carboxylic acid-activated plastic supports have been optimized. The effects of the following parameters have been examined: coupling time, pH, and temperature; availability of the free essential reacting groups on the supports; porosity of the supports; and enzyme loading. Properties of the immobilized enzymes, such as coupled activity and operational stability were assessed.