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RevistaRSC Advances
Año2016
Volumen6
Páginas27329 - 27334
Internacional

INACTIVATION OF IMMOBILIZED TRYPSIN UNDER DISSIMILAR CONDITIONS PRODUCES TRYPSIN MOLECULES WITH DIFFERENT STRUCTURE

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Alfredo Sancheza,+,  Jenifer Cruz,b,c, +,  Nazzoly Ruedab.c,  Jose C. S. dos Santobb,d, Rodrigo Torresc,e, Claudia Ortizf, Reynaldo Villalongaa,* and Roberto Fernandez-Lafuenteb*
a Department of Analytical Chemistry, Faculty of Chemistry, Complutense University of Madrid, 28040 Madrid, Spain.
b Departamento de Biocatálisis. Instituto de Catálisis-CSIC, Campus UAM-CSIC Madrid. Spain.
c Escuela de Química, Grupo de investigación en Bioquímica y Microbiología (GIBIM), Edificio Camilo Torres 210, Universidad Industrial de Santander, Bucaramanga, Colombia
d Instituto de Engenharias e Desenvolvimento Sustentável, Universidade da Integração Internacional da Lusofonia Afro-Brasileira, CEP 62785-000, Acarape, CE, Brazil.
e Current address: Laboratorio de Biotecnología, Instituto Colombiano del Petróleo-Ecopetrol, Piedecuesta, Bucaramanga, Colombia.
f. Escuela de Microbiología, Universidad Industrial de Santander, Bucaramanga, Colombia


Abstract
            Bovine trypsin has been immobilized on glyoxyl-agarose and two different preparations have been produced. One was reduced just after immobilization, while the other was left to continue the enzyme-support reaction. This strategy is a guarantee of the identical orientation of the enzyme regarding the support surface and identical physical properties of the support. Then, the two preparations were submitted to inactivations under different conditions: thermal and solvent inactivations under different pH values. After drying, the structures of the different enzymes preparations were analyzed by deconvolution of the amide I region, that provides information about the secondary structure of the protein in terms of α-helix, β-sheets, β-turns and non-ordered or irregular structures. The results confirm that the structures of the different preparations were very different, suggesting that the inactivation ways were different for each enzyme preparation and depending on the inactivation conditions. This information is very relevant for the design of strategies of enzyme stabilization, as show that the inactivation may follow different conformational changes depending on the degree of enzyme rigidification and inactivation conditions
Palabras clave:Enzyme stabilization, Enzyme immobilization, Enzyme inactivation, enzyme secondary structure, glyoxyl-agarose.
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