Urease was encapsulated within alginate beads, coated with poly(methylene c
o-guanidine) membranes via polyelectrolyte complexation. Membrane thickness
increased with reaction time to 53 mu m after 80 min, and to 59 mu m with
an increase in co-guanidine concentration from 2.5 to 20 mg ml(-1). A 70% m
ass and 31% activity yield of urease resulted following encapsulation. Alth
ough co-guanidine strongly inhibited freely soluble urease (I-0.5 = 5.8 mu
g ml(-1) co-guanidine), immobilization stabilized the enzyme against inacti
vation. Encapsulated activity declined as the polycation concentration used
for membrane formation increased; however an activity loss of only 35% was
observed when the co-guanidine concentration was as high as 5 mg ml(-1). G
lucose protected against inactivation, with I-0.5 increasing to 28.5 mu g m
l(-1) for the freely soluble enzyme. When the beads were coated with co-gua
nidine in the presence of glucose, encapsulated urease activity was fully r
etained. (C) 2000 Elsevier Science Ltd. All rights reserved.