Substrate selectivity and optimization of immobilized SMG1‐F278N lipase in synthesis of propylene glycol monooleate
Li X, Liu P, Khan F I, et al.
European Journal of Lipid Science and Technology, 2017, 119(5).
In the present study, the immobilized SMG1-F278N lipase was employed for the esterification of 1,3-propylene glycol with oleic acid. This was the first report of using mono- and diacylglycerol lipase for the production of propylene glycol monoesters (PGME). It was found that immobilized SMG1-F278N preferred 1,3-propylene glycol than 1,2-propylene glycol. Molecular docking of 1,2-propylene glycol and 1,3-propylene glycol into SMG1-F278N suggested that the 1,3-propylene glycol preferentially binds to the active pocket of SMG1-F278N as compared to 1,2-propylene glycol. The maximum 1,3-propylene glycol monooleate content of 70.67% was obtained under the reaction conditions of 1,3-propylene glycol/oleic acid ratio of 5:1 (mol/mol), enzyme loading of 7.5% (w/w, with respect to total substrates), and water addition of 7% (w/w, with respect to total substrates) at 30°C. The present work offers insights into the selectivity of immobilized SMG1-F278N towards 1,2-propylene glycol and 1,3-propylene glycol, and suggests the extended applications of immobilized SMG1-F278N for industrial purpose.
Chemicals Used in the Paper:
|Catalog Number||Product Name||Structure||CAS Number||Price|
|ACM105624||Propylene glycol dioleate||105-62-4||Price|
|ACM1330809||Propylene glycol monooleate||1330-80-9||Price|