Registration of asparaginase single molecule activity using a nanopore detector

Aim. The possibility of using a nanopore to monitor the functioning of asparaginase has been studied.

Methodology. In this work, a SiN-based nanopore was constructed in which the L-asparaginase molecule was embedded. The catalytic activity of the L-asparaginase molecule, embedded in the nanopore, has been monitored by observing the change in the ion current in the cell with this nanopore. This approach is useful for studying the catalytic activity based on single enzyme molecules embedded in a nanopore.

Results. A nanopore detector for studying the catalytic activity of L-asparaginase has been developed. It has been found that this detector made it possible to monitor the activity of this enzyme.

Research implications. It has been shown that a nanopore detector, with a nanopore size of the order of 6 nm, can be used to study the activity of asparaginase. It is possible to carry out realtime monitoring of changes in the form of L-asparaginase, which consisted in monitoring changes in the ion current passing through a nanopore, in which asparaginase was immobilized. The results obtained can be of use in the analysis of the functioning of enzymes at the level of single molecules. 

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