Microstructural and Hydrophilic Properties of Polylactide Polymer Samples with Various 3D Printing Patterns.

The aim of the work is to study the effect of the 3D printing process on the microstructural and hydrophilic properties of polylactic acid (PLA) samples with various model printing patterns obtained from the black filament PLA by sequentially applying polymer layers using the FDM (fused deposition modeling) method. X-ray phase analysis revealed the partial crystallization of PLA polymer chains in the printed samples, which occurs under thermal and mechanical action on the original amorphous PLA filament during 3D printing to varying degrees, depending on the geometry of the pattern and the morphology of its surface. At the same time, IR spectroscopy data indicate the preservation of all intrastructural chemical bonds of polylactide. Measured at the original installation, the values of the wetting edge angles on the surface of the printed samples are in the range φ = 50-60°, which is significantly less than the right angle. This indicates the hydrophilic properties of the whole sample's surface. At the same time, the influence of different geometries of model drawings in printed samples was found not only on the morphology of the sample's surface according to SEM data but also on its wettability.

Carboxymethyl Cellulose-Based Polymers as Promising Matrices for Ficin Immobilization.

The present work is devoted to research on the interaction between carboxymethyl cellulose sodium salt and its derivatives (graft copolymer of carboxymethyl cellulose sodium salt and N,N-dimethyl aminoethyl methacrylate) with cysteine protease (ficin). The interaction was studied by FTIR and by flexible molecular docking, which have shown the conjugates' formation with both matrices. The proteolytic activity assay performed with azocasein demonstrated that the specific activities of all immobilized ficin samples are higher in comparison with those of the native enzyme. This is due to the modulation of the conformation of ficin globule and of the enzyme active site by weak physical interactions involving catalytically valuable amino acids. The results obtained can extend the practical use of ficin in biomedicine and biotechnology.