Develop composite matrices using biocompatible polymers of natural and synthetic origin for immobilization of the proteolytic enzyme serratiopeptidase; to study the biochemical and physico-chemical properties of the free enzyme; explore the interaction of serratiopeptidase/polymers, serratiopeptidase/bacteriolytic enzyme lysozyme and BAR

Which priority area of ​​science and technology corresponds to: fundamental scientific research on the most important problems of developing scientific, technical, socio-economic, socio-political, human potential to ensure the competitiveness of Ukraine in the world and the sustainable development of society and the state;

Research: fundamental.

Future application perspective: ongoing research

Research level: no analogues in Ukraine.

Availability of a patent: no

What additional actions require further research: additional funding, modern scientific equipment.

Brief description, advantages, further perspective.

A homogeneous preparation of the proteolytic enzyme of bacterial origin serratiopeptidase was obtained from SERPATA tablets (molecular weight 45±4 kDa confirmed by electrophoretic studies). The biochemical and physicochemical characteristics of the enzyme were studied: protein content – 2.3±0.1 (*P<0.05), total proteolytic activity – 9.6±0.5 (*P<0.05) U/mg protein per minute, collagenase activity – 142.4 ± 0.1 (*P<0.05) nmol leucine/mg protein per minute, fibrinolytic activity – 6.1 ± 0.3 (*P<0.05) units/ mg protein per minute; pH-optimum 9.5, thermo-optimum – 45оС.

The following biocompatible polymers were selected for immobilization of serratiopeptidase by non-covalent bonding with the matrix: sodium carboxymethyl cellulose (3% solution), polyvinyl alcohol-sodium alginate (mass ratio 5:1).

Preservation of the total proteolytic activity of the enzyme after immobilization was 80% when using a solution of Na-carboxymethylcellulose and 88% when using a composition of polyvinyl alcohol-sodium alginate. The interaction of the enzyme with polymers was confirmed by viscometry and UV spectroscopy. It has been shown that in the presence of serratiopeptidase, the bacteriolytic enzyme lysozyme completely loses its activity, which makes their joint immobilization impossible.

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