Lipase-catalyzed methanolysis of triricinolein in organic solvent to produce 1,2(2,3)-diricinolein |
| |
Authors: | Charlotta Turner Xiaohua He Tasha Nguyen Jiann-Tsyh Lin Rosalind Y Wong Robert E Lundin Leslie Harden Thomas McKeon |
| |
Affiliation: | (1) Western Regional Research Center, USDA, 800 Buchanan St., 94710 Albany, CA |
| |
Abstract: | The objective of this study was to find the optimal parameters for lipase-catalyzed methanolysis of triricinolein to produce
1,2(2,3)-diricinolein. Four different immobilized lipases were tested, Candida antarctica type B (CALB), Rhizomucor miehei (RML), Pseudomonas cepacia (PCL), and Penicillium roquefortii (PRL). n-Hexane and diisopropyl ether (DIPE) were examined as reaction media at three different water activities (a
w), 0.11, 0.53, and 0.97. The consumption of triricinolein and the formation of 1,2(2,3)-diricinolein, methyl ricinoleate,
and ricinoleic acid were followed for up to 48 h. PRL gave the highest yield of 1,2(2,3)-diricinolein. Moreover, this lipase
showed the highest specificity for the studied reaction, i.e., high selectivity for the reaction with triricinolein but low
for 1,2(2,3)-diricinolein. Recoveries of 93 and 88% DAG were obtained using PRL in DIPE at a
w of 0.11 and 0.53, respectively. Further, NMR studies showed that a higher purity of the 1,2(2,3)-isomer vs. the 1,3-isomer
was achieved at higher a
w (88% at a
w=0.53), compared to lower a
w (71% at a
w=0.11). The DAG obtained was acylated by the DAG acyltransferase from Arabidopsis thaliana. Therefore, this enzymatic product is a useful enzyme substrate for lipid biosynthesis. Accordingly, the use of PRL in DIPE
at a
w 0.53 is considered optimal for the synthesis of 1,2(2,3)-diricinolein from triricinolein. |
| |
Keywords: | |
本文献已被 PubMed SpringerLink 等数据库收录! |
|