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Published on: September 28, 2018
Study of the complex coacervation mechanism between the lysing enzyme from T. harzianum and polyallylamine
Houda Bey1, Wala Gtari1, Adel Aschi1
1Université de Tunis El Manar, Faculté des Sciences de Tunis, LR99ES16 Laboratoire de Physique de la Matière Molle et de la Modélisation Électromagnétique, 2092 Tunis, Tunisia.
Abstract:
Complex coacervation was achieved by mixing the lysing enzyme from T. harzianum (LYS) with polyallylamine hydrochloride (PAH). We show in this work that the study electrostatic complexes conformation can lead to the formation of dense complexes. We systematically investigated the effects of pH and the mass ratio on the structure and properties of the complex. The different transition phases (pHc, pHφ1, and pHφ2) have been determined using dynamic light scattering, zeta potential and turbidimetric measurements. The interpolymeric bonds may be ionic or physical, depending on the pH of the system. For a pH value of 4.9, the mixture system [LYS]/[PAH] gives raise the formation of coacervate droplets. The effects of temperature on the structure of coacervate droplets are studied by small angle light scattering (SALS).
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