M. Goto et al., ENZYMATIC INTERESTERIFICATION OF TRIGLYCERIDE WITH SURFACTANT-COATED LIPASE IN ORGANIC MEDIA, Biotechnology and bioengineering, 45(1), 1995, pp. 27-32
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.