The favorable physicochemical properties are essential for the application of protein-based nanovehicles in the field of biomaterials. Herein, we found that the thermal stability of Marsupenaeus japonicus ferritin (MjFer) (T_m = 109.1 ± 0.4 °C) is markedly higher than human H-chain ferritin (HuHF) (T_m = 87.7 ± 0.3 °C), although they share a high structural similarity. Multiple results indicated that the promoted thermal stability of MjFer is mainly derived from the salt bridges located at the C₃ interface. Consequently, MjFer exhibits strong protective effects on encapsulated curcumin upon exposure at high temperatures. In contrast, most of the curcumin loaded HuHF composites precipitated rapidly under the same conditions. These findings elucidated the molecular mechanism of the hyperthermostability of MjFer and illustrated that MjFer could act as a robust insulation nanocarrier for bioactive compounds against various thermal treatments.

良好的理化性质对于基于蛋白质的纳米载体在生物材料领域的应用至关重要。在此，我们发现日本袋鱼铁蛋白 (MjFer) ( T _m  = 109.1 ± 0.4 °C)的热稳定性明显高于人类 H 链铁蛋白 (HuHF) ( T _m  = 87.7 ± 0.3 °C)，尽管它们具有高度的结构相似性。多项结果表明，促进 MjFer 的热稳定性主要来自位于C ₃的盐桥界面。因此，MjFer 在暴露在高温下时对封装的姜黄素表现出很强的保护作用。相比之下，大多数负载姜黄素的 HuHF 复合材料在相同条件下迅速沉淀。这些发现阐明了 MjFer 超热稳定性的分子机制，并说明 MjFer 可以作为生物活性化合物抵抗各种热处理的强大绝缘纳米载体。