Abstract
β-galactosidase from E. coli was immobilized on porous bead cellulose by a benzoquinone coupling method and to an epoxy-activated polyacrylic matrix. The optimum conditions for activation and coupling were determined and the kinetic parameters of the immobilized enzyme were investigated. Cellulose up to now was of little significance as a matrix for biotechnical application by reason of its poor flow properties due to the fibrous structure or powder form. This study presents the immobilization of β-galactosidase as a high molecular weight enzyme on porous cellulose in bead form (1,2,3) as a new type of matrix. For the immobilization a benzoquinone coupling method (4) has been used, which has not yet been applied to bead cellulose. Binding and kinetic properties are compared with those of β-galactosidase bound to epoxy-activated polyacrylic beads (5,6).
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