ALCOHOLYSIS AND GLYCERIDE SYNTHESIS WITH IMMOBILIZED LIPASE ON CONTROLLED-PORE GLASS OF VARYING HYDROPHOBICITY IN SUPERCRITICAL CARBON-DIOXIDE

Citation
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
Citations number
37
Categorie Soggetti
Biothechnology & Applied Migrobiology
ISSN journal
01410229
Volume
22
Issue
5
Year of publication
1998
Pages
360 - 367
Database
ISI
SICI code
0141-0229(1998)22:5<360:AAGSWI>2.0.ZU;2-D
Abstract
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.