Evidence of structural changes of an enzymatic extract entrapped into alginate beads
| Autor: | Nelio Ariel Ochoa, Cristian Omar Illanes, Gerardo Enrique Camí, Evelina Quiroga |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Conformational change
Environmental Engineering Chromatography Recubrimientos y Películas Diffuse reflectance infrared fourier transform Chemistry ENTRAPMENT Biomedical Engineering Tryptophan Infrared spectroscopy Bioengineering INGENIERÍAS Y TECNOLOGÍAS ARAUJIAIN IMMOBILIZATION ENZYMES ALGINATE BEADS Ingeniería de los Materiales Thermal stability Fourier transform infrared spectroscopy Thermal analysis Protein secondary structure Biotechnology |
| Popis: | In this work, we analyzed the structural changes of araujiain entrapped into alginate beads. Araujiain is an enzymatic preparation containing three known enzymatic fractions with each fraction individually presenting a similar catalytic performance. Fluorescence and infrared spectroscopy, thermal analysis and residual catalytic activity studies were carried out. A small red shift in the spectrum of araujiain was observed after the entrapment process. Changes in the polarity around the tryptophan (Trp) residues were associated with an enzyme conformational change. From the Fourier transform infrared spectroscopy (FTIR) analysis, it was demonstrated that interactions between the enzyme extract and Ca alginate caused different structural behavior in araujiain. According to the diffuse reflectance infrared Fourier transform spectroscopy (DRIFT) study, it was possible to conclude that a secondary structure with a high α-helical character was responsible for the highest activity of entrapped araujiain. Finally, from thermal analysis measurements, it was proved that entrapment of araujiain augments the thermal stability of both the enzyme extract and Ca alginate, indicating a possible interaction between enzyme extract and its support. Fil: Illanes, Cristian Omar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada "Dr. Jorge Andrés Zgrablich". Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto de Física Aplicada "Dr. Jorge Andrés Zgrablich"; Argentina Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada "Dr. Jorge Andrés Zgrablich". Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto de Física Aplicada "Dr. Jorge Andrés Zgrablich"; Argentina Fil: Camí, Gerardo Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Investigaciones en Tecnología Química. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Instituto de Investigaciones en Tecnología Química; Argentina Fil: Ochoa, Nelio Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Física Aplicada "Dr. Jorge Andrés Zgrablich". Universidad Nacional de San Luis. Facultad de Ciencias Físico Matemáticas y Naturales. Instituto de Física Aplicada "Dr. Jorge Andrés Zgrablich"; Argentina |
| Databáze: | OpenAIRE |
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