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- Li, Han, et al.
(författare)
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Advancements of nature nanocage protein : preparation, identification and multiple applications of ferritins
- 2022
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Ingår i: Critical reviews in food science and nutrition. - : Informa UK Limited. - 1040-8398 .- 1549-7852. ; 62:25, s. 7117-7128
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Forskningsöversikt (refereegranskat)abstract
- Ferritin is an important iron storage protein, which is widely existed in all forms of life. Ferritin can regulate iron homeostasis when iron ions are lacking or enriched in the body, so as to avoid iron deficiency diseases and iron poisoning. Ferritin presents a hollow nanocage, which can store ions or other small molecular substances in the cavity. Therefore, ferritin shows its potential as a functional nanomaterial that can deliver nutrients or drugs in a targeted manner to improve bioavailability. Due to the special structure, the research on ferritin has attracted more and more attention in recent years. In this paper, the structural characteristics of ferritin were introduced, and the natural purification and prokaryotic expression methods of ferritin from different sources were described. At the same time, ferritin can bind to small molecules, so that it has the activity of small molecules, to construct a new type of ferritin. As a result, ferritin plays an important role as a nutrient substance, in targeted transport, and disease monitoring, etc. In conclusion, the yield of ferritin can be improved by means of molecular biology. Meanwhile, molecular modification can be used to make ferritin have unique activity and function, which lays a foundation for subsequent research.
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| 2. |
- Li, Han, et al.
(författare)
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Improvement of thermal stability of oyster (Crassostrea gigas) ferritin by point mutation
- 2021
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Ingår i: Food Chemistry. - : Elsevier. - 0308-8146 .- 1873-7072. ; 346
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Tidskriftsartikel (refereegranskat)abstract
- 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 degrees C and has increased by 13 degrees C more than the wildtype oyster ferritin. The effect of thermal treatment on the denaturation, aggregation state, particle size and the structure of ferritin was not changed before 90 degrees 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.
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