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Improving the thermal stability of phytase using core-shell hydrogel beads
Eunhye Yang1, Hongmin Dong1, Waritsara Khongkomolsakul1
1Department of Food Science, College of Agriculture & Life Sciences, Cornell University, Stocking Hall, Ithaca, NY 14853, United States.
Food Chemistry: X
|January 1, 2024
Summary
This study developed a core-shell hydrogel bead to protect phytase enzyme activity during heat treatment. The novel encapsulation method significantly enhanced phytase thermal stability for broader applications.
Area of Science:
- Biomaterials Science
- Enzyme Engineering
- Biotechnology
Background:
- Phytase is crucial for nutrient availability but sensitive to heat.
- Enzyme encapsulation is vital for protecting functionality during processing.
- Developing stable enzyme delivery systems is a key challenge.
Purpose of the Study:
- To design a core-shell hydrogel bead system for phytase.
- To enhance phytase encapsulation efficiency and thermal stability.
- To protect enzymatic functionality from heat treatment.
Main Methods:
- Core-shell hydrogel bead fabrication using chitosan-phytase complex core and alginate-carrageenan shell.
- Optimization of hydrogel for improved encapsulation and thermal stability.
- Analysis of catalytic activity, secondary structure, and thermal properties (FTIR, DSC).
Main Results:
- Encapsulated phytase retained ~70% catalytic activity post-heat treatment.
- The secondary structure of encapsulated phytase remained similar to free phytase.
- Core-shell structure exhibited increased melting point and strong core-shell interactions.
Conclusions:
- Core-shell hydrogel encapsulation effectively enhances phytase thermal stability.
- The system protects enzymatic functionality, maintaining secondary structure.
- This approach broadens potential applications for phytase delivery systems.
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