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Updated: May 28, 2025

Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins
Published on: August 31, 2019
Cage-like ferritin and lysozyme heteroprotein complexes coacervation for encapsulation, stabilization, and sustained
Xinmei Sha1, Yichen Li1, Jiaqi Ding1
1Tianjin Key Laboratory of Food Quality and Health, Tianjin University of Science and Technology, Tianjin 300457, PR China.
Abstract:
The ferritin (FRT) with a modifiable cavity can interact with the lysozyme (LYS) to form a heteroprotein complex coacervation (HPCC). This interaction is believed to combine the unique properties of FRT and LYS to form a novel structure with enhanced characteristics. The study aimed to explore the pH-dependent complexation between FRT and LYS and evaluate the protective effects of the heteroprotein complex on curcumin (Cur). Results showed that pH and protein ratios influenced the formation of the complex. ζ-potential measurements indicated that interactions between oppositely the charged molecules and hydrogen bonding drove the formation of FRT-LYS (FL) complexes, enhancing their hydrophobicity and thermal stability. Cur-encapsulated in FL (FCL) demonstrated an increased stability when exposed to heat, natural light, and ultraviolet light (FL/Cur, 1:50) treatments, and showed a controlled and sustained release behavior. This study emphasizes the potential of FL heteroprotein complexes as nanocarriers for encapsulation and protection of bioactive molecules.
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