Barnase encapsulation into submicron porous CaCO<sub>3</sub> particles: studies of loading and enzyme activity
Alexey M. Yashchenok, Оlga I. Gusliakova, Е. В. Коновалова, Marina V. Novoselova, Victoria O. Shipunova, Tatiana O. Abakumova, Olga Efimova, Р. В. Холоденко, Alexey Schulga, Timofei S. Zatsepin, Dmitry A. Gorin, Sergey M. Deyev
Abstract
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.
Topics & Concepts
BarnaseEncapsulation (networking)Materials sciencePolyelectrolytePorosityChemical engineeringRibonucleaseComposite materialChemistryPolymerBiochemistryComputer scienceGeneRNAComputer networkEngineeringEnzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationCalcium Carbonate Crystallization and Inhibition