TY - JOUR
T1 - Activation of lipase in ionic liquids by modification with comb-shaped poly(ethylene glycol)
AU - Nakashima, Kazunori
AU - Okada, Jun
AU - Maruyama, Tatsuo
AU - Kamiya, Noriho
AU - Goto, Masahiro
N1 - Funding Information:
This work is supported by a Grant-in-Aid for the 21st Century COE Program, ‘‘Functional Innovation of Molecular Informatics’’ from the Ministry of Education, Culture, Sports, Science and Technology of Japan. K.N. was supported by Research Fellowships from the Japan Society for the Promotion of Science (JSPS) for Young Scientists. The authors would like to thank Prof. Atsushi Maruyama (Kyushu University) for his helpful discussions.
PY - 2006/10
Y1 - 2006/10
N2 - Outstanding activation of an enzyme in ionic liquids (ILs) has been demonstrated by covalent modification with comb-shaped poly(ethylene glycol) (PEG) (PM13). Candida rugosa lipase modified with PM13 (PM13-CRL) was readily solubilized in all the ILs tested ([Emim][Tf2N], [C2OC1mim][Tf2N] and [C2OHmim][Tf2N]) containing 0.5% (v/v) of water, whereas native lipase did not dissolve in any of the ILs. The results for transesterification of 2-phenyl-1-propanol with vinyl acetate using lipase in ILs revealed that the PM13-CRL conjugate exhibits a high catalytic activity while suspended native lipase shows little activity. The hydrophobicity of ILs somewhat affected the enzyme activity and a more hydrophobic IL such as [Emim][Tf2N] was preferable for the lipase reaction, as was also observed in enzymatic reaction in conventional organic solvents. The enzyme activities in ILs were much higher than those in organic solvents, the excellent activity being associated with unique properties such as the hydrophobicity and the high polarity of ILs. Furthermore, the PM13--CRL conjugate exhibited a high storage stability in [Emim][Tf2N].
AB - Outstanding activation of an enzyme in ionic liquids (ILs) has been demonstrated by covalent modification with comb-shaped poly(ethylene glycol) (PEG) (PM13). Candida rugosa lipase modified with PM13 (PM13-CRL) was readily solubilized in all the ILs tested ([Emim][Tf2N], [C2OC1mim][Tf2N] and [C2OHmim][Tf2N]) containing 0.5% (v/v) of water, whereas native lipase did not dissolve in any of the ILs. The results for transesterification of 2-phenyl-1-propanol with vinyl acetate using lipase in ILs revealed that the PM13-CRL conjugate exhibits a high catalytic activity while suspended native lipase shows little activity. The hydrophobicity of ILs somewhat affected the enzyme activity and a more hydrophobic IL such as [Emim][Tf2N] was preferable for the lipase reaction, as was also observed in enzymatic reaction in conventional organic solvents. The enzyme activities in ILs were much higher than those in organic solvents, the excellent activity being associated with unique properties such as the hydrophobicity and the high polarity of ILs. Furthermore, the PM13--CRL conjugate exhibited a high storage stability in [Emim][Tf2N].
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U2 - 10.1016/j.stam.2006.06.008
DO - 10.1016/j.stam.2006.06.008
M3 - Article
AN - SCOPUS:37849188833
SN - 1468-6996
VL - 7
SP - 692
EP - 698
JO - Science and Technology of Advanced Materials
JF - Science and Technology of Advanced Materials
IS - 7
ER -