Abstract
The regularities have been studied for the formation of molecular associates upon the introduction of papain into a sodium alginate colloidal solution in the laminar low-speed, transient, and turbulent stirring regimes. The relationship between variations in the sorption capacity of the biopolymer composition and the kinetic regularities of the interphase transfer has been studied during the sorption binding of albumin, which is one of the protein-based components of wound exudates, with such components being subject to ensimatic cleavage. The state of the dispersed phase of the colloidal solutions has been estimated by the dynamic light scattering method. The properties of the formed biopolymer films have been studied using the methods of scanning electron microscopy, low-temperature nitrogen adsorption, and static albumin sorption from solutions of limited volumes. The data of the sorption experiments have been analyzed using the Boyd, Morris–Weber, and gel diffusion models, as well as the Lagergren pseudo-first-order and Ho–McKay pseudo-second-order kinetic models. The data have been obtained for substantiating the dosages of the biopolymermatrix used on wound-healing bandages and for the efficient binding of wound necrotic contamination during the time preset according to the technical requirements.
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