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Microencapsulation III: Preparation of invertase microcapsules
Journal of Pharmaceutical Sciences
|July 1, 1982
Summary
Researchers developed methods to encapsulate invertase enzyme within microcapsules. Protective proteins were added to prevent enzyme inactivation in acidic conditions, enhancing stability for various applications.
Area of Science:
- Biocatalysis and Enzyme Immobilization
- Materials Science and Engineering
- Chemical Engineering
Background:
- Enzyme immobilization is crucial for industrial applications, improving stability and reusability.
- Polyamide microcapsules offer a versatile matrix for enzyme encapsulation.
- Invertase enzyme stability can be compromised by environmental factors like pH.
Purpose of the Study:
- To optimize the encapsulation of invertase enzyme within polyamide microcapsules.
- To investigate methods for protecting encapsulated invertase from inactivation.
- To develop alternative protein-based microcapsule systems for enzyme immobilization.
Main Methods:
- Interfacial polymerization was used to create polyamide microcapsules containing invertase.
- Parameters such as pH, polymerization time, surfactant concentration, and stirring rate were studied.
- An emulsification-reticulation method using proteins and acylating agents was developed for enzyme immobilization.
Main Results:
- Optimization of interfacial polymerization parameters improved microcapsule formation and enzyme incorporation.
- Incorporation of protective proteins significantly enhanced invertase stability against pepsin inactivation in acidic media.
- Successful immobilization of invertase was achieved by cross-linking the enzyme within protein matrices.
Conclusions:
- Polyamide microcapsules provide a viable system for invertase encapsulation, with tunable properties.
- Protective protein incorporation is an effective strategy to enhance enzyme stability in microcapsules.
- The emulsification-reticulation method offers a novel approach for creating robust, immobilized enzyme systems.