Immobilization of carbohydrases on epoxide-, isocyanate-, acid chloride-, and carboxylic acid-activated plastic supports.
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.
Roig
M G
MG
Departmento de Quimica Fisica, Facultad de Farmacia, Universidad de Salamanca, España.
Kennedy
J F
JF
Garaita
M G
MG
D000143:Acids; D002264:Carboxylic Acids; D002712:Chlorides; D004800:Enzymes, Immobilized; D004852:Epoxy Compounds; D005087:Glucan 1,4-alpha-Glucosidase; D006863:Hydrogen-Ion Concentration; D017953:Isocyanates; D008320:Maltose; D010316:Particle Size; D010969:Plastics; D013696:Temperature; D000516:alpha-Amylases
D000143:Acids; D002264:Carboxylic Acids; D002712:Chlorides; D004800:Enzymes, Immobilized; D004852:Epoxy Compounds; D017953:Isocyanates; D010969:Plastics; D008320:Maltose; D000516:alpha-Amylases; D005087:Glucan 1,4-alpha-Glucosidase