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Immobilization of invertase by encapsulation in polyelectrolyte complexes.
J Mansfeld1, M Förster, A Schellenberger
1Martin-Luther University, Department of Biotechnology, Halle, GDR.
Enzyme and Microbial Technology
|March 1, 1991
Summary
Encapsulating invertase enzyme within symplex membranes slightly altered its optimal conditions but improved stability. This enzyme immobilization technique offers potential for advanced fermentation technologies.
Area of Science:
- Biochemistry
- Biotechnology
- Enzyme Engineering
Background:
- Invertase enzyme from Saccharomyces cerevisiae is crucial for sucrose hydrolysis.
- Enzyme immobilization enhances enzyme stability and reusability.
- Symplex membranes offer a novel matrix for enzyme encapsulation.
Purpose of the Study:
- To encapsulate free and immobilized invertase within symplex membranes.
- To compare the kinetics and performance of encapsulated invertase with free invertase.
- To evaluate the stability and potential applications of encapsulated invertase.
Main Methods:
- Encapsulation of Saccharomyces cerevisiae invertase in symplex membranes (cellulose sulfate and poly(dimethyldiallylammonium chloride)).
- Kinetic analysis of encapsulated versus free invertase using sucrose hydrolysis.
- Assessment of pH and temperature optima, kinetic constants, and stability.
Main Results:
- Encapsulation caused minor shifts in pH and temperature optima.
- Diffusional limitations altered kinetic constants for encapsulated invertase.
- High storage and operational stability were observed at low substrate concentrations.
- Coimmobilization with non-sucrose-utilizing cells showed promise for fermentation.
Conclusions:
- Symplex membrane encapsulation is a viable method for invertase immobilization.
- Encapsulation impacts enzyme kinetics but enhances stability.
- This approach holds potential for applications in fermentation technology.