Premium
Substrate selectivity and optimization of immobilized SMG1‐F278N lipase in synthesis of propylene glycol monooleate
Author(s) -
Li Xingxing,
Liu Pengzhan,
Khan Faez Iqbal,
Li Daoming,
Yang Bo,
Wang Yonghua
Publication year - 2017
Publication title -
european journal of lipid science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 94
eISSN - 1438-9312
pISSN - 1438-7697
DOI - 10.1002/ejlt.201600423
Subject(s) - polyvinyl alcohol , oleic acid , lipase , chemistry , selectivity , organic chemistry , catalysis , enzyme , biochemistry
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. Practical applications: To our knowledge, the production of PGME using mono‐ and diacylglycerol lipases was reported for the first time. This study could contribute to develop potential applications of immobilized SMG1‐F278N in industries. 1,2‐Propylene glycol/1,3‐propylene glycol docked into the catalytic pocket of SMG1‐F278N, esterification of 1,2‐propylene glycol/1,3‐propylene glycol with oleic acid catalyzed by immobilized SMG1‐278N and optimization of production of 1,3‐propylene glycol monooleate.