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Related Experiment Video

Updated: Jul 3, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

Interaction of invertase with polyelectrolytes.

H Dautzenberg¹, J Kötz, B Philipp

¹Institute of Polymer Chemistry Erich Correns in Teltow-Seehof, Germany.

Biotechnology and Bioengineering

|November 1, 1991

Summary

Enzyme immobilization via direct polyelectrolyte complexation with invertase is ineffective. Complete immobilization is achievable through inclusion flocculation or symplex microcapsules for enhanced enzyme applications.

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Area of Science:

Biochemistry and Polymer Science
Enzyme Immobilization Techniques

Background:

Investigating polyelectrolyte complex formation with polyampholytes.
Understanding the interaction between enzymes (invertase) and linear polyelectrolytes.

Purpose of the Study:

To investigate the interaction between invertase and linear polyelectrolytes.
To determine the effectiveness of polyelectrolyte complexation for enzyme immobilization.

Main Methods:

Turbidimetry
Light scattering measurements
Enzyme activity determination

Main Results:

Invertase forms polyelectrolyte complexes exclusively with cationic polyelectrolytes.
Light scattering reveals aggregation and desegregation during complex formation.
Only a portion of invertase molecules participates in Coulombic interactions, with reduced enzyme activity.

Conclusions:

Direct interaction between invertase and cationic polyelectrolytes is inefficient for enzyme binding.
Effective invertase immobilization can be achieved via 'inclusion flocculation' using anionic/cationic polyelectrolyte symplexes.
Immobilization within symplex microcapsules offers a viable alternative for complete enzyme capture.