RESUMEN
The aim of this research was to design a method of immobilization of high-purity human butyrylcholinesterase on the surface of gold nanoparticles preserving the activity of the enzyme. In order to achieve this aim, the method of fractionation and purification of human butyrylcholinesterase from plasma was modified. The synthesis of 15-nm gold nanoparticles was carried out by citrated method. A method of conjugation of the high-purity butyrylcholinesterase with gold nanoparticles was developed. It was found that the Immobilization of butyrylcholinesterase on the surface of gold nanoparticles resulted in a significant (to 23%) increase in the specific activity of the enzyme.
Asunto(s)
Butirilcolinesterasa , Compuestos de Oro/síntesis química , Nanopartículas del Metal , Butirilcolinesterasa/química , Butirilcolinesterasa/aislamiento & purificación , Estabilidad de Enzimas , Compuestos de Oro/química , Humanos , Concentración de Iones de Hidrógeno , Nanopartículas del Metal/química , Tamaño de la PartículaRESUMEN
The dynamics of changes in spectra of oligosaccharide fragments formed during enzymatic degradation of plant pectins at low enzyme/substrate ratio was studied. It is shown that degradation of deesterified pectin molecules is a discrete and determined process manifested in establishment of a stable polysaccharide spectrum. It is noted that introduction of chemical modifications into the polysaccharide substrate structure preserves the discreteness of the polymer molecule fragmentation but changes the spectrum of formed oligosaccharide fragments. It is supposed that degradation is defined by the spatial (three-dimensional) organization of the polysaccharide molecule.
