M. Murray et al., IMMOBILIZATION OF LIPASE ONTO LIPOPHILIC POLYMER PARTICLES AND APPLICATION TO OIL HYDROLYSIS, Process biochemistry, 32(6), 1997, pp. 479-486
The immobilization of lipase onto two lipophilic particulate supports,
non-porous polystyrene latex and porous Accurel EP400 powder, for the
enzymic hydrolysis of sunflower oil is described. The activity of the
immobilized enzyme was compared to that in free enzyme hydrolyses and
the immobilization efficiency of lipase on each of the supports deter
mined. Results indicated that, although polystyrene latex exhibited a
very high affinity for the adsorption of lipase, enzyme activities wer
e very poor. Satisfactory immobilization of lipase onto EP400 particle
s was attained only at high enzyme loadings. However, under these cond
itions, rates of hydrolysis and equilibrium conversions obtained using
lipase immobilized onto EP400 particles were comparable to those achi
eved in free enzyme systems. In addition, once bound to the EP400 supp
ort, the enzyme displayed good recycle potential. (C) 1997 Elsevier Sc
ience Ltd.