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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 C 3 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. [ABSTRACT FROM AUTHOR]

• After adding about 1000 Fe2+ in vitro , oyster ferritin reached the saturation state. • Adding Fe2+ can improve the storage and thermal stability of oyster ferritin. • Heating at 80 ℃ and below does not affect the structure and Fe2+ content of GF1-1000 Fe2+. Ferritin, one of the storage forms of iron, which widely exists in all living organisms and shows its potential as functional nanomaterial. In this study, Fe2+ were added to oyster ferritin (GF1) in vitro until reached experimental saturation state. The structure characterization and monodisperse morphology of ferritin were showed that the protein structure of ferritin did not change significantly after adding Fe2+ and GF1 with 1000 Fe2+ (GF1-1000 Fe2+) was selected for subsequent experiments. The storage stability results showed that 11.27 % of the protein remained cage-like structure when GF1-1000 Fe2+ was stored at 4 °C for 12 days. The thermal treatment results showed that GF1-1000 Fe2+ still maintained certain structure and activity at 80 °C, and 82.8 % of Fe2+ was still retained at 80 °C. These experimental results may provide a theoretical basis for the development of novel iron supplement that are non-toxic and highly stable. [ABSTRACT FROM AUTHOR]

Highlights: [•] β-Carotene can be encapsulated within ferritin shell. [•] The β-carotene-containing ferritin nanocomposites become water-soluble. [•] Such encapsulation improves the thermal stability of β-carotene. [ABSTRACT FROM AUTHOR]

• Point mutation in D120G could improve the thermal stability of oyster ferritin. • The spherical shell of mutated ferritin can be kept well at 90 °C and below. • The stability of oyster ferritin was promoted via the improved 3-fold interfaces. Ferritin can be widely used as functional nanomaterial. But the physiological activity of ferritin can be damaged under excessive temperatures, which affect the self-assembly property. In this study, point mutation was produced in Asp120 to Gly120 of ferritin amino acid sequence and the heat resistance was improved significantly. The thermal denaturation temperature of mutated ferritin is 89.17 °C and has increased by 13 °C more than the wild-type oyster ferritin. The effect of thermal treatment on the denaturation, aggregation state, particle size and the structure of ferritin was not changed before 90 °C. The computational modeling and analysis indicated that mutated ferritin promotes the overall structural stability assembly via decreasing the interaction energies of 62 percent energies in 3-fold interface. Improving the thermal stability of oyster ferritin by point mutation enhances its applications as a food ingredient. [ABSTRACT FROM AUTHOR]