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RevistaChemical Society Reviews
Año2013
Volumen42
Páginas6290 - 6307
Internacional

Modifying enzyme activity and selectivity by immobilization

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Rafael C. Rodrigues, Claudia Ortiz, Ángel Berenguer-Murcia, Rodrigo Torres, Roberto Fernández-Lafuente.
 
a  Biocatalysis and Enzyme Technology Lab, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil.
b Escuela de Bacteriología y Laboratorio Clínico, Universidad Industrial de Santander, Bucaramanga, Colombia.
c Instituto Universitario de Materiales, Departamento de Química Inorgánica, Universidad de Alicante, Campus de San Vicente del Raspeig, Ap. 99 - 03080 Alicante (Spain)
dEscuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.
 eDepartamento de Biocatalisis. Instituto de Catálisis-CSIC. Campus UAM-CSIC. Cantoblanco. 28049 Madrid (Spain).
Immobilization of enzymes may produce alterations on their observed activity, specificity or selectivity. Although in many cases an impoverishment of the enzyme properties is observed upon immobilization (caused by the distortion of the enzyme due to the interaction with the support) in some instances such properties may be enhanced by this immobilization. These alterations in enzyme properties are sometimes associated with changes in the enzyme structure. On occasions, these variations will be positive. For example, they may be related to the stabilization of a hyperactivated form of the enzyme, like in the case of lipases immobilized on hydrophobic supports via interfacial activation. In some other instances, these improvements will be just a consequence of random modifications on the enzyme properties that in some reactions will be positive while in others may be negative. For this reason, the preparation of as broad a library of biocatalysts as possible may be a key turning point to find an immobilized biocatalyst with improved properties when compared to the free enzyme. Immobilized enzymes will be dispersed on the support surface and aggregation will no longer be possible, while the free enzyme may suffer aggregation, which greatly decreases enzyme activity. Moreover, enzyme rigidification may produce a preservation of the enzyme properties under drastic conditions in which the enzyme tends to become distorted thus decreasing its activity. However, immobilization of enzymes on a support, mainly on a porous support, may in many cases also have a positive impact on the observed enzyme behavior, not really related to structural changes. For example, the promotion of diffusional problems (e.g., pH gradients, substrate or product gradients), partition (towards or away the enzyme environment, for substrate or products), or the blocking of some areas (e.g., reducing inhibitions) may greatly improve enzyme performance. Thus, in this tutorial review, we will try to list and explain some of the main reasons that may produce an improvement in enzyme activity, specificity or selectivity, either real or apparent, due to immobilization.
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