Estudio sobre la síntesis enzimática de péptidos en medios bifásicos

SONIA BARBERIS; EVELINA QUIROGA; MARÍA CECILIA ARRIBÉRE; NORA PRIOLO

Merlo, San Luis, Argentina

Congreso; XVII Reunión Científica Anual de la Sociedad de Biología de Cuyo; 1999

Sociedad de Biología de Cuyo

The objective of this work was to study the behavior of phytoproteasa of Morrenia brachystephana for the enzymatic peptide synthesis, in two-phase media.  The effect of solvents on the activity and stability of the enzyme and on the solubilities of the substrates demostrated that chloroform : water (50:50) system was the more advisable two-phase reaction media. The Fitoprotease demonstrated to be able to catalyze the synthesis of, at least, two peptide compounds, whose structural identifications were made by TLC, RMN and HPLC-EM. In agreement with that results, this work contributes a new variety of proteases like catalysts of the peptide synthesis. Nevertheless, this enzyme does not has a high stereoespecificity, since it reacts indifferently with isomers D and L of the involved substrates, which constitutes a disadvantage from the point of view of the bioactive peptides synthesis.