Abstract
s-galactosidase from Escherichia coli was immobilized on porous bead cellulose by a benzoquinone coupling method. Optimum conditions for activation and coupling were investigated, and the kinetic parameters of the immobilized enzyme described. The binding capacity was 15.6mg/g of wet conjugate, corresponding to 109 mg/g dry matrix. A saturation activity of 4100 U/g dry cellulose beads was achieved. The apparent Michaelis constant of the immobilized s-galactosidase at pH 7.6 for orthonitrophenylgalactopyranoside was 2.4 x 10-3 mol/liter, as compared to 2.4 x 10-4 mol/liter of the native enzyme. The stability of benzoquinone-activated bead cellulose and of immobilized s galactosidase were also determined.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
