Several surfactant‐coated enzymes have been prepared by coating lipases of various origins with a nonionic surfactant, glutamic acid dioleylester ribitol (2C18Δ9GE). Enzymatic interesterification of tripalmitin with oleic acid using the surfactant‐coated lipase was carried out in organic media. The surfactant‐coated lipases could effectively catalyze the interesterification of glycerides better than did the powder 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 activity for the interesterification of glycerides, although its powder lipase did not show enzymatic activity. Selective interesterification of glycerides could be performed by adjusting the concentration ratio of oleic acid to tripalmitin in isooctane. Di‐substituted glyceride could be selectively produced when the concentration ratio of carboxylic acid to glycerides was 7. © 1995 John Wiley & Sons, Inc.
|Number of pages||6|
|Journal||Biotechnology and Bioengineering|
|Publication status||Published - Jan 5 1995|
All Science Journal Classification (ASJC) codes
- Applied Microbiology and Biotechnology