INVESTIGADORES
ROMANINI Diana
artículos
Título:
Protein-flexible chain polymer interactions to explain protein partition in two aqueous two-phase systems and the protein–polyelectrolyte complex formation
Autor/es:
BOERIS, VALERIA; FARRUGGIA, BEATRIZ; NERLI, BIBIANA; ROMANINI, DIANA; PICĂ“, GUILLERMO
Revista:
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Editorial:
Elsevier
Referencias:
Año: 2007 vol. 41 p. 286 - 286
ISSN:
0141-8130
Resumen:
Complexes formation between two model proteins (catalase and chymotrypsin) and polyelectrolytes (polyvinyl sulphonate and polyacrilic acid) and a non-charged flexible chain polymer (PCF) as polyethylene propylene oxide (molecular mass 8400) was studied by a spectroscopy technique combination: UV absorption, fluorescence emission and circular dichroism. All the polymers increase the protein surface hydrophobicity (S0) parameter value as a proof of the modification of the protein surface exposed to the solvent. Chymotrypsin showed an increase in its biological activity in polymer presence, which suggests a change in the superficial microenvironment. The decrease in the biological activity of catalase might be due to a competition between the polymer and the substrate. This result agrees with the polymer effect on the catalase superficial hydrophobicarea. It was found that, when flexible chain polymers increase protein stability and the enzymatic activity they could be used to isolate this enzyme without inducing loss of protein enzymatic activity. Our findings suggest that the interactions are dependent on the protein physico-chemical parameters such as: isoelectric pH, hydrophobic surface area, etc.