Phosphonium alkyl PEG sulfate ionic liquids as coating materials for activation of Burkholderia cepacia lipase.
Lipases are among the most widely used enzymes applicable for various substrates; however, the slow reactions or poor enantioselective reactions are sometimes obtained. To develop ionic liquid type activating agents for lipase, four types of phosphonium cetyl(PEG)10 sulfate ionic liquids have been synthesized and used as coating materials of Burkholderia cepacia lipase (Lipase PS) through the lyophilization process. Tributyl ([2-methoxy]ethoxymethyl)phosphonium cetyl(PEG)10 sulfate ([P444MEM ][C16 (PEG)10 SO4 ]) (PL1) worked best among them, and PL1-coated lipase PS displayed high reactivity in transesterification of broad types of secondary alcohols using vinyl acetate as an acylating reagent with perfect enantioselectivity (E > 200). The substrate preference of PL1-PS differs from that of commercial lipase PS or [bdmim] [C16 (PEG)10 SO4 ]-coated lipase (IL1-PS); PL1-PS displayed excellent enantioselectivity in the reaction of 2-chloro-1-phenylethanol with E > 200, though insufficient E values were recorded for lipase PS (E = 12) and IL1-PS (E = 123) for this alcohol. PL1-PS also showed perfect enantioselectivity (E > 200) for the reaction of 1-(pyridin-2-yl)ethanol, while IL1-PS showed E = 130 for this compound. We further succeeded in demonstrating the recyclable use of PL1-PS five times in tributyl(3-methoxypropyl)phosphonium bis(trifluoromethylsulfonyl)amide ([P444PM ][Tf2 N]) as a solvent. Since PL1-PS is easily applicable to 10-20 gram-scaled reactions, it is expected that the IL-coated enzyme might be useful for practical preparation of a wide variety of chiral secondary alcohols.
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
Yui
Y
Matsubara
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
Shiho
S
Kadotani
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
Takashi
T
Nishihara
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
Yoshichika
Y
Hikino
Center for Research on Green Sustainable Chemistry, Graduate School of Engineering, Tottori University, Tottori, Japan.
Yukinobu
Y
Fukaya
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.|Center for Research on Green Sustainable Chemistry, Graduate School of Engineering, Tottori University, Tottori, Japan.
Toshiki
T
Nokami
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan. titoh@chem.tottori-u.ac.jp.|Center for Research on Green Sustainable Chemistry, Graduate School of Engineering, Tottori University, Tottori, Japan. titoh@chem.tottori-u.ac.jp.
Toshiyuki
T
Itoh
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D016956:Burkholderia cepacia / Q000201:enzymology*; D004789:Enzyme Activation; D052578:Ionic Liquids / Q000737:chemistry; D008049:Lipase / Q000737:chemistry* / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000737:chemistry*; D013431:Sulfates / Q000737:chemistry
D001426:Bacterial Proteins; D052578:Ionic Liquids; D013431:Sulfates; D011092:Polyethylene Glycols; D008049:Lipase
Ionic Liquid; Lipase; Phosphonium salts; Transesterification acceleration