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Stabilization of native penicillin G acylase by ionic liquids
Author(s) -
de los Ríos Antonia P.,
HernándezFernández Francisco J.,
Rubio Manuel,
Gómez Demetrio,
Víllora Gloria
Publication year - 2007
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.1654
Subject(s) - ionic liquid , hexafluorophosphate , sulfonyl , chemistry , dichloromethane , tetrafluoroborate , imide , trifluoromethyl , bromide , toluene , hydrolysis , substrate (aquarium) , organic chemistry , solvent , catalysis , inorganic chemistry , alkyl , oceanography , geology
Five different ionic liquids, based on dialkylimidazolium cations associated with perfluorinated and bis{(trifluoromethyl)sulfonyl}imide anions, were used to investigate the scope and limitations of these new solvents as media for penicillin G acylase‐catalyzed reactions. Deactivation of the native enzyme in ionic liquids (ILs) and in organic solvents (toluene, dichloromethane and 2‐propanol) at low water content and 40 °C was investigated using the hydrolysis of penicillin G as activity test. Native penicillin G acylase 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 + ][Tf 2 N − ], which was about 2000‐fold higher than that in 2‐propanol. An enhancement of the PGA stability was observed by the presence of substrate in ionic liquids based on tetrafluoroborate and hexafluorophosphate anions, achieving the highest increase of the half‐life time in 1‐butyl‐3‐methylimidazolium hexafluorophosphate ([bmim + ][PF 6 − ]), which was about 9‐fold higher than the half‐life time in the absence of substrate. Copyright © 2007 Society of Chemical Industry