IIBYT   23944
INSTITUTO DE INVESTIGACIONES BIOLOGICAS Y TECNOLOGICAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
SUPRAMOLECULAR STRUCTURE REGULATE BETA-GAL FUNCTIONALITY
Autor/es:
JULIETA M. SANCHEZ; CLOP, PD; FLORES, SANDRA SOLEDAD; NOLAN, MV; CLOP, EM; MA PERILLO
Lugar:
Castellón
Reunión:
Congreso; 6th International Iberian Biophysics Congress and X Iberoamerican Congress of Biophysics; 2018
Resumen:
In our laboratory we studied the structure-function relationship of proteins in complex environment. We applied β-galactosidase from E. coli (β-Gal) as a model protein. Previously we proved that the soluble enzyme interacts with lipid/water interfaces and demonstrated that in this condition β-Gal activity increased and acquired a structure more hydrated and more resistant to thermal unfolding with respect to β-Gal in solution. We also prepared mixed β-Gal/phospholipid Langmuir films (LF) at the air/water interface. At high surface pressures the AFM analysis of LF suggested that β-Gal was in a state of higher order of oligomerization than the typical tetramer. Currently, we overexpress a recombinant β-Gal in E.coli. In some conditions we obtain β-Gal inclusion bodies (IBsβ-Gal). Interestingly, the IBsβ-Gal exhibits not only higher activity but also higher resistance to temperature and pH inactivation with respect to the soluble β-Gal. We conclude that the protein-protein contact at the lipid/water and at the protein/water interfaces confers β-Gal an activating environment allowing a non-native but active and stable structure