Aim. Study of lysozyme molecules behaviour at immobilization in gelatin and carboxymethyl cellulose sodium salt solutions by matrix-assisted laser desorption/ionization (MALDI). Methods. Determination of the activity of lysozyme, both free and entrapped in gelatin and carboxymethyl cellulose sodium salt (Na-CMC) solutions, was conducted by bacteriolytic method. The enzyme interaction with polymers was confirmed by viscometry and mass-spectrometry methods. Results. The occurrence of lysozyme associates in aqueous solution in monomeric and oligomeric forms was shown. A non-valent interaction of the enzyme with solutions of polymers results in the dissociation of oligomeric associates into subunits, which depends on the support nature and mass ratio of lysozyme to polymer. The quantitative retention of immobilized lysozyme hydrolytic activity was established, which favours obtaining mucoadhesive film forms with bacteriolytic action. Conclusions. The lysozyme immobilization by non-valent interactions in gelatin solution and Na-CMC solutions causes dissociation of the enzyme oligomeric structures; a stronger lysozyme coupling with NaCMC was noted.

Keywords: lysozyme, oligomers, dissociation, gelatin, carboxymethyl cellulose sodium salt, MALDI