| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 70034 | Journal of Molecular Catalysis B: Enzymatic | 2013 | 5 Pages |
Lipases are excellent catalysts for industrial applications ranging from laundry detergents to fine chemicals synthesis. Bacillus pumilus lipase A (BplA) belongs to a subfamily of small hydrolases displaying a remarkable enantioselectivity in hydrolytic reactions. Recombinant BplA was immobilized in silica gel and its enantioselectivity was evaluated. BplA displays a notorious enantioselectivity towards the R enantiomer of 1-phenylethyl acetate in hydrolytic reactions. In agreement with this hydrolytic enantioselectivity, BplA immobilized in silica gel is enantioselective towards the R enantiomer of 1-phenylethanol for the synthesis of its hexanoic acid ester in n-hexane as solvent. In contrast, isoinversion was observed in the ionic liquids 1-ethyl-3-methylimidazolium methanesulfonate ([Emim][CH3SO3]) or 1-ethyl-3-methylimidazolium methylsulfate ([Emim][EtSO4]). At temperatures from 25 to 35 °C, BplA produces only the (R)-enantiomer of the ester, while at temperatures from 15 to 20 °C the enantioselectivity is inverted towards the corresponding (S)-enantiomer.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Bacillus pumilus lipase is enantioslective for the hydrolysis of (R,S)-1-phenylethylacetatte (ee = 89%). ► Immobilized lipase from B. pumilus synthetizes 1-phenylethylhexanoate from (R,S)-1-phenylethanol and hexanoic acid in ionic liquids. ► This biocatalyst is enantioselective towards the (R)-enantiomer of 1-phenylethanol at temperatures above 25 °C, while its enantioselectivity is inverted at temperatures below 20 °C.
