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Controlled enzyme-immobilisation on capillaries for microreactors for peptide mapping.

A Bossi¹, L Guizzardi, M R D'Acunto

¹Department of Science and Technology, University of Verona, Strada Le Grazie 15, 34137, Verona, Italy. bossi@sci.univr.it

Analytical and Bioanalytical Chemistry

|December 6, 2003

Summary

Researchers developed a novel capillary electrophoretic (CE)-microreactor using photo-immobilised trypsin for efficient peptide mapping. This miniaturised device offers rapid, high-quality protein analysis, paving the way for advanced screening applications.

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Area of Science:

Analytical Chemistry
Biochemistry
Materials Science

Background:

Peptide mapping is crucial for protein identification and characterization.
Traditional methods can be time-consuming and require complex setups.
Enzyme immobilization is key to developing efficient analytical devices.

Purpose of the Study:

To develop a novel capillary electrophoretic (CE)-microreactor for on-line peptide mapping.
To investigate the photo-immobilisation of trypsin on silica capillaries.
To assess the performance and stability of the constructed CE-microreactor.

Main Methods:

Covalent immobilization of trypsin onto a silica capillary using photo-immobilisation.
Construction of a single-piece CE-microreactor to prevent leakage.

Related Experiment Videos

Characterization of enzyme surface density, stability, and conversion rate.

On-line protein mapping of various protein sizes.

Main Results:

Achieved high enzyme surface density (15.8 microg/cm(2)) and stability (80% after 38 days).
Demonstrated efficient conversion rate (0.2 ng/s).
Successfully performed on-line protein mapping within 15 minutes, providing exhaustive maps for small proteins.

Conclusions:

The developed CE-microreactor enables rapid and efficient peptide mapping.
The photo-immobilisation technique offers a robust method for enzyme integration.
This technology holds significant potential for miniaturised enzymatic screening devices and high-throughput analysis.