STABILITY OF HYDROLASE ENZYMES IN IONIC LIQUIDS

被引:27
作者
Hernandez-Fernandez, F. J. [1 ]
de los Rios, A. P. [1 ]
Tomas-Alonso, F. [2 ]
Gomez, D. [2 ]
Villora, G. [2 ]
机构
[1] Tech Univ Cartagena, Dept Chem & Environm Engn, E-30202 Murcia, Spain
[2] Univ Murcia, Dept Chem Engn, Fac Chem, E-30100 Murcia, Spain
关键词
stability; hydrolase enzyme; lipase; penicillin acylase; ionic liquid; ANTARCTICA LIPASE-B; PENICILLIN-G AMIDASE; ORGANIC-SOLVENTS; WATER ACTIVITY; SYSTEMS; MEDIA; TRANSESTERIFICATION; ACYLATION;
D O I
10.1002/cjce.20227
中图分类号
TQ [化学工业];
学科分类号
0817 ;
摘要
In this work we attempted to evaluate the stability of penicillin G acylase (PGA) from Escherichia coli in their native form and free Candida antarctica lipase B (CaLB) in ionic liquids (ILs) at low water content. The hydrolysis of penicillin G to 6-aminopenicillanic acid (6-APA), and phenyl acetic acid (PAA) catalysed by PGA and the synthesis of butyl butyrate from vinyl butyrate and 1-butanol catalysed by CaLB were chosen as activity tests. The influence of these new solvents on enzyme stability was studied by incubating the enzyme (PGA or CaLB) in ILs based on dialkylimidazolium cations associated with perfluorinated and dicyanamide anions at a given temperature. Stability studies indicate that CAB and PGA exhibited greater stability in water-immiscible ILs than in water-miscible ILs. Specifically, native PGA shows greater stability in IL media than in organic solvents. For example, a half-life time of 23 h was obtained in 1-ethyl-3-methylimidazolium bis{(trifluoromethyl)sulfonyl}imide, [emim(+)][NTf2-], which was about 2000-fold higher than that in 2-propanol. The higher half-life time of CaLB was observed in [omim(+)][PF6-] (t(1/2) =84 h).
引用
收藏
页码:910 / 914
页数:5
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