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Home > Publication > Substrate selectivity and optimization of immobilized SMG1‐F278N lipase in synthesis of propylene glycol monooleate

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 Propylene glycol dioleate 105-62-4 Price
ACM1330809 Propylene glycol monooleate Propylene glycol monooleate 1330-80-9 Price

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Tel:1-201-478-8534
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