H. Gunnlaugsdottir et al., ALCOHOLYSIS AND GLYCERIDE SYNTHESIS WITH IMMOBILIZED LIPASE ON CONTROLLED-PORE GLASS OF VARYING HYDROPHOBICITY IN SUPERCRITICAL CARBON-DIOXIDE, Enzyme and microbial technology, 22(5), 1998, pp. 360-367
Lipases from Humicola lanuginosa and Candida antarctica lipase B were
adsorbed onto methylated controlled-glass bends with varying degrees o
f hydrophobicity. The effect of support hydrophobicity on the amount o
f lipase adsorbed was studied. The immobilized lipases were examined f
or their activity in an alcoholysis reaction of cod liver oil with eth
anol in supercritical carbon dioxide. Furthermore, the activity of the
immobilized Humicola lanuginosa lipase in glyceride synthesis in supe
rcritical carbon dioxide was studied. For both lipases investigated, t
he amount adsorbed decreased with decreasing hydrophobicity of the sup
port; moreover, for Humicola lanuginosa lipase, the lipolytic activity
was found to depend largely on the substrate and the hydrophobicity o
f the immobilization support. In the alcoholysis reaction, a highly hy
drophobic carrier enhanced lipase activity whereas in glyceride synthe
sis, the reverse effect was observed. For Candida antarctica lipase, t
he support hydrophobicity did riot affect the activity of the lipase.
In addition, the results showed that the lipid class composition of th
e reaction mixture reflected the lipolytic activity of the lipases imm
obilized on the different supports tested. (C) 1998 Elsevier Science I
nc.