Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

Abstract

Chemical modification and immobilization of enzymes have been usually considered unrelated tools to improve biocatalyst features. However, there are many examples where a chemically modified enzyme is finally used in an immobilized form, and that exemplifies how both tools may be complementary resulting in a synergism in the final results. In this review we present some of the strategies that may give that result. For example, the chemical modification of soluble enzymes may be used to improve their immobilization (reinforcing adsorption or improving multipoint covalent attachment), or just to improve enzyme stability and facilitate the selection of the immobilization conditions. Chemical modification of previously immobilized enzymes benefits from solid-phase chemistry due to the nature of enzymes (e.g., prevention of inactivation, aggregation, etc.). The use of different targets for chemical modifications with small molecules or multifunctional polymers are also discussed: intramolecular or intersubunit cross-linking, one-point modification, generation of artificial microenvironments, etc.

Enzyme immobilization by adsorption: a review

“…However, the enormous catalytic potential offered by the enzymes for innumerable transformations, has stimulated intense studies aimed at the improvement of their properties (Mateo et al 2007;Brady and Jordon 2009;FernandezLafuente 2009;Garcia-Galan et al 2011;Cowan and Fernandez-Lafuente 2011;Rodrigues et al 2013). Among several methods of this improvement that have been proposed, an immobilization of the enzymes is apparently most widely applied (Zhao 2010;Rodrigues et al 2011;Hanefeld et al 2013). The term first appeared in the literature at the beginning of twentieth century and referred to the enzymes bound directly to the carriers.…”

Heterofunctional Supports in Enzyme Immobilization: From Traditional Immobilization Protocols to Opportunities in Tuning Enzyme Properties

“…In fact, it has been recently reviewed how the joint use of 71 microbiological tools (use of thermopilic mircoorganisms), 17 genetic tools 18 or chemical 72 modification of enzymes 19 to achieve an improved immobilization has opened the door to new 73 strategies for enzyme properties enhancement. 74 It is true that any immobilization protocol (at least, if the enzyme is placed inside 75 porous particles) avoids some inactivation causes: aggregation, proteolysis (due to autolysis if 76 the enzyme is a protease or due to the action of some contaminant protease) or interaction with 77 external interfaces will no longer be possible (just a small percentage of enzymes placed on the 78 outer surface of the particle may suffer these detrimental phenomena).…”

Modificación Química en Fase Sólida de Lipasa B de Candida antarctica para mejorar sus propiedades de actividad, estabilidad y enantioselectividad

“…De igual manera, la modificación química puede usarse para modular las propiedades catalíticas de las enzimas. Sin embargo, los efectos de la modificación en las propiedades enzimáticas son difíciles de predecir (Torchilin et al, 1997;Rodrigues et al, 2011).…”