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Mechanistic study on phytase stabilization using alginate encapsulation

delete2024-06-01
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OA
AI
Y
Yilun Weng
B
Baode Sun
W
Wanli Jin
P
Penghui Yan
X
Xiaojing Chen
H
Hao Song
赵春霞 cover
赵春霞 (Chun‐Xia Zhao) *
DOI:10.1016/j.foodhyd.2024.109837delete
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Abstract

Abstract

En 中文
Enzyme encapsulation has emerged as a promising strategy for protecting enzymes against denaturation under harsh conditions. Alginate encapsulation using a dripping and gelation method is a common technique for encapsulating enzymes, however, the encapsulation efficiency is often limited due to the quick diffusion of water-soluble enzymes into the gelation bath. Herein, we report a novel post-loading enzyme encapsulation method with a 100% encapsulation efficiency and a high enzyme loading. We demonstrate a 20-fold enzyme thermal stability improvement upon encapsulation. Furthermore, we investigate the effects of alginate pore size, enzyme concentration, and enzyme distribution on the thermal stability of encapsulated enzyme using both experimental and computational methods, elucidating the mechanism underlying the stability improvement of the encapsulated enzyme. Additionally, the encapsulated enzyme demonstrates successful release under simulated gastric conditions. This highly efficient enzyme encapsulation system, utilizing food-grade encapsulation materials and an environmentally friendly synthesis approach, holds great promise for various applications in the food industry.
Keywords:
Enzyme
Thermal stabilization mechanism
Encapsulation efficiency
Controlled release
Alginate beads
Industrial applications

Journal

Food Hydrocolloids cover
Food Hydrocolloids
IF:
12.4
Papers:
1.3W
Citations:
9.6W

Organization

U
University of Adelaide
Scholars:
2.3W
Papers: 2.4W
Citations: 4.2W
U
University of Queensland
Scholars:
5.0W
Papers: 5.1W
Citations: 9.2W