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Improvement of ther...
Improvement of thermal stability of oyster (Crassostrea gigas) ferritin by point mutation
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- Li, Han (författare)
- Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Collaborat Innovat Ctr Seafood Deep Proc, Sch Food Sci & Technol, Dalian 116034, Peoples R China.
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- Tan, Xiaoyi (författare)
- China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China.
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- Xia, Xiaoyu (författare)
- Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Collaborat Innovat Ctr Seafood Deep Proc, Sch Food Sci & Technol, Dalian 116034, Peoples R China.
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- Zang, Jiachen (författare)
- China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China.
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- El-Seedi, Hesham (författare)
- Uppsala universitet,Farmakognosi
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- Wang, Zhenyu (författare)
- Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Collaborat Innovat Ctr Seafood Deep Proc, Sch Food Sci & Technol, Dalian 116034, Peoples R China.
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- Du, Ming (författare)
- Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Collaborat Innovat Ctr Seafood Deep Proc, Sch Food Sci & Technol, Dalian 116034, Peoples R China.
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Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Collaborat Innovat Ctr Seafood Deep Proc, Sch Food Sci & Technol, Dalian 116034, Peoples R China China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China. (creator_code:org_t)
- Elsevier, 2021
- 2021
- Engelska.
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Ingår i: Food Chemistry. - : Elsevier. - 0308-8146 .- 1873-7072. ; 346
- Relaterad länk:
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https://doi.org/10.1...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Ferritin
- Point mutation
- Structure
- Monodispersity
- Thermostability
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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