Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 102, Issue 1, Pages 225-235Publisher
SPRINGER
DOI: 10.1007/s00253-017-8597-6
Keywords
Sn-1,3 selectivity of lipase; Organic solvent; Water activity; Salt hydrate pair; Conformation
Categories
Funding
- National Natural Science Foundation of China [31660010]
- Innovation Fund of Guizhou University [2016059]
- Key Agricultural Project of Guizhou Province [QKHZC-[2016]2580]
- High-level innovative talents training project of Guizhou province [QKHPTRC[2016]5662]
- Natural Science Foundation of Jiangsu Province [BK2012229]
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We previously screened a whole-cell lipase EC 3.1.1.3 from the novel strain Aspergillus niger GZUF36, which exhibited 1,3-selectivity in the synthesis of 1,3-diacylglycerol via glycerolysis. However, the mechanism of lipase selectively in catalyzing the sn-1,3 position remains ambiguous. This work was performed to investigate the 1,3-selective mechanism of lipase using glycerolysis to synthesize 1,3-diacylglycerol (1,3-DG) as a model reaction by changing solvent(s) and water activity (a(w)), and addition of salt hydrate pair. The measured diacylglycerol yield was also used to examine lipase activity. Results indicated that not only organic solvent and a(w) have strong effect on the sn-1,3 selectivity, but also ions of salt hydrate pair also affected selectivity. Lipase conformation was altered by hydrophobic interactions of the solvent, a(w), or ions of salt hydrate, resulting in distinct sn-1,3 selectivity of the lipase. The salt hydrate pair changed the lipase conformation and selectivity not only by a(w) but also by static interactions, which was rarely reported. These parameters also affected lipase activity. The lipase displayed the highest selectivity (about 88%) and activity in solvents of t-butanol and n-hexane (1:29, v/v) at a(w) 0.43. The results demonstrated that the sn-1,3 selectivity and activity of the lipase from A. niger GZUF36 may be improved by control of some crucial factors. This work laid a foundation for the application of lipase in the synthesis of 1,3-DG and other structural and functional lipids.
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