. Physicochemical study of the formation of complexes between pancreatic proteases and polyanions"

J. LOMBARDI; G. PICÓ; V. BOERIS;

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2015 vol. 79 p. 160 - 166

0141-8130

The formation of insoluble complexes between proteins and oppositely charged polyelectrolytes wasassessed. Two pancreatic enzymes: trypsin and chymotrypsin, and two anionic synthetic polyelectrolytes:polyacrylate and polyvinylsulfonate, were used for the study at the pH range between 3.00and 5.00. Two different titration curve shapes, representing two insoluble complexes formation mechanisms,were found. The turbidity of enzyme?polyelectrolyte mixtures is related to the increase eitherin the size or in the quantity of the insoluble complexes. Ionic strength destabilized insoluble complexformation. Finally, the kinetics of the process of insoluble complex formation at different conditions wasstudied.