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Barnase encapsulation into submicron porous CaCO particles: studies of loading and enzyme activity

The present study focuses on the immobilization of the bacterial ribonuclease barnase (Bn) into submicron porous calcium carbonate (CaCO 3 ) particles. For encapsulation, we apply adsorption, freezing-induced loading and co-precipitation methods and study the effects of adsorption time, enzyme conce...

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Published in:Journal of materials chemistry. B, Materials for biology and medicine Materials for biology and medicine, 2021-11, Vol.9 (42), p.8823-8831
Main Authors: Yashchenok, Alexey M, Gusliakova, Olga I, Konovalova, Elena V, Novoselova, Marina V, Shipunova, Victoria O, Abakumova, Tatiana O, Efimova, Olga I, Kholodenko, Roman, Schulga, Alexey A, Zatsepin, Timofei S, Gorin, Dmitry A, Deyev, Sergey M
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Summary:The present study focuses on the immobilization of the bacterial ribonuclease barnase (Bn) into submicron porous calcium carbonate (CaCO 3 ) particles. For encapsulation, we apply adsorption, freezing-induced loading and co-precipitation methods and study the effects of adsorption time, enzyme concentration and anionic polyelectrolytes on the encapsulation efficiency of Bn. We show that the use of negatively charged dextran sulfate (DS) and ribonucleic acid from yeast (RNA) increases the loading capacity (LC) of the enzyme on CaCO 3 particles by about 3-fold as compared to the particles with Bn itself. The ribonuclease (RNase) activity of encapsulated enzyme depends on the LC of the particles and transformation of metastable vaterite to stable calcite, as studied by the assessment of enzyme activities in particles. The encapsulation efficiency of ribonuclease barnase in submicron CaCO 3 particles can be enhanced by the use of anionic polyelectrolytes. The enzymatic activity of enzyme loaded particles is consistent with the loading capacity of these particles.
ISSN:2050-750X
2050-7518
DOI:10.1039/d1tb01315g