ENZYMATIC INTERESTERIFICATION OF TRIGLYCERIDE WITH SURFACTANT-COATED LIPASE IN ORGANIC MEDIA

Citation
M. Goto et al., ENZYMATIC INTERESTERIFICATION OF TRIGLYCERIDE WITH SURFACTANT-COATED LIPASE IN ORGANIC MEDIA, Biotechnology and bioengineering, 45(1), 1995, pp. 27-32
Citations number
14
Categorie Soggetti
Biothechnology & Applied Migrobiology
ISSN journal
00063592
Volume
45
Issue
1
Year of publication
1995
Pages
27 - 32
Database
ISI
SICI code
0006-3592(1995)45:1<27:EIOTWS>2.0.ZU;2-K
Abstract
Several surfactant-coated enzymes have been prepared by coating lipase s of various origins with a nonionic surfactant, glutamic acid dioleyl ester ribitol (2C(18)Delta(9)GE). Enzymatic interesterification of tri palmitin with oleic acid using the surfactant-coated lipase was carrie d out in organic media. The surfactant-coated lipases could effectivel y catalyze the interesterification of glycerides better than did the p owder lipases. A suitable organic solvent was an aliphatic hydrocarbon such as isooctane. The enzymatic activity for the interesterification strongly depended on the origin of the lipase. The surfactant-coated lipase prepared by Mucor javanicus showed the highest enzymatic activi ty for the interesterification of glycerides, although its powder lipa se did not show enzymatic activity. Selective interesterification of g lycerides could be performed by adjusting the concentration ratio of o leic acid to tripalmitin in isooctane. Di-substituted glyceride could be selectively produced when the concentration ratio of carboxylic aci d to glycerides was 7. (C) 1995 John Wiley and Sons, Inc.