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Amination of enzymes to improve the biocatalyst performance. Coupling genetic modification and physicochemical tools

Authors:Roberto Fernandez-Lafuente
Groups of research:Optimización de biocatalizadores y bioprocesos enzimáticos
Rafael C. Rodriguesa, Oveimar Barbosab, Claudia Ortizc, Ángel Berenguer-Murciad, Rodrigo Torresb,  Roberto Fernandez-Lafuentee,*.
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 Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia.
c Escuela de Bacteriología y Laboratorio Clínico, Universidad Industrial de Santander, Bucaramanga, Colombia.
d Instituto Universitario de Materiales, Departamento de Química Inorgánica, Universidad de Alicante, Campus de San Vicente del Raspeig, Ap. 99 - 03080 Alicante, Spain.
e Departamento de Biocatalisis. ICP-CSIC. Campus UAM-CSIC. Cantoblanco. 28049 Madrid. Spain.
Improvement of the features of an enzyme is in many instances a pre-requisite for the industrial implementation of these exceedingly interesting biocatalysts. To reach this goal, the researcher may utilize different tools. For example, amination of the enzyme surface produces an alteration of the isoelectric point of the protein along with its chemical reactivity (primary amino groups are the most widely used to obtain the reaction of the enzyme with surfaces, chemical modifiers, etc) and even its “in vivo” behavior. This review will show some examples of chemical (mainly modifying the carboxylic groups using the carbodiimide route), physical (using polycationic polymers like polyethyleneimine) and genetic amination of the enzyme surface. Special emphasis will be put on cases where the amination is performed to improve subsequent protein modifications. Thus, amination has been used to increase the intensity of the enzyme/support multipoint covalent attachment, to improve the interaction with cation exchanger supports or polymers, or to promote the formation of crosslinkings (both intra-molecular and in the production of crosslinked enzyme aggregates). In other cases, amination has been used to directly modulate the enzyme properties (both in immobilized or free form). Amination of the enzyme surface may also pursue other goals not related with biocatalysis. For example, it has been used to improve the raising of antibodies against different compounds (both increasing the number of haptamers per enzyme and the immunogenicity of the composite) or the ability to penetrate cell membranes. Thus, amination may be a very powerful tool to improve the use of enzymes and proteins in many different areas and a great expansion of its usage may be expected in the next future.

Keywords:Enzyme stabilization, enzyme modulation, polyethylenimine, enzyme chemical amination, enzyme genetic amination, polymer coating of enzymes, enzyme multipoint covalent attachment, crosslinking
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