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Improved Stabilization of Genetically Modified Penicillin G Acylase in the Presence of Organic Cosolvents by Co- Immobilization of the Enzyme with Polyethyleneimine

AuthorsMontes, Tamara ; Grazú, Valeria; Manso, Isabel ; Galán, Beatriz ; López-Gallego, Fernando; González García, Ramón ; Hermoso, Juan A. ; García, José Luis ; Guisán, José Manuel ; Fernández-Lafuente, Roberto
KeywordsEnzyme stability
Organic solvents
Issue Date8-Jan-2007
PublisherJohn Wiley & Sons
CitationAdvanced Synthesis & Catalysis 349(3): 459–464 (2007)
AbstractPenicillin G acylase (PGA) is an enzyme that hardly interacts with polycationic polymers (e.g., polyethyleneimine, PEI) and thus the enzyme cannot be stabilized against the action of organic solvents by its co-immobilization with the polymer in the same support, neither covalently attached to the support nor adsorbed on the already immobilized enzyme. However, a new mutant PGA bearing eight additional Glu residues homogenously distributed throughout the enzyme surface may interact with the polymer. The co-immobilization of the enzyme and PEI on glyoxyl-agarose allows one to fully take advantage of the stabilization produced by the multipoint covalent attachment and by the protective hydrophilic micro-environment generated by the polycationic polymer, enabling a significant stabilization of the immobilized PGA in the presence of organic solvents.
Publisher version (URL)http://dx.doi.org/10.1002/adsc.200600313
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