1. Barnase encapsulation into submicron porous CaCO 3 particles: studies of loading and enzyme activity.
- Author
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Yashchenok AM, Gusliakova OI, Konovalova EV, Novoselova MV, Shipunova VO, Abakumova TO, Efimova OI, Kholodenko R, Schulga AA, Zatsepin TS, Gorin DA, and Deyev SM
- Subjects
- Adsorption, Bacterial Proteins biosynthesis, Bacterial Proteins metabolism, Calcium Carbonate metabolism, Dextran Sulfate chemistry, Dextran Sulfate metabolism, Escherichia coli enzymology, Particle Size, Polyelectrolytes metabolism, Porosity, RNA chemistry, RNA metabolism, Ribonucleases biosynthesis, Ribonucleases metabolism, Saccharomyces cerevisiae chemistry, Saccharomyces cerevisiae metabolism, Surface Properties, Bacterial Proteins chemistry, Calcium Carbonate chemistry, Polyelectrolytes chemistry, Ribonucleases chemistry
- Abstract
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 CaCO3 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.- Published
- 2021
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