Study on the microstructure control for aggregated protein nanoparticles by using freezing
Project/Area Number |
26450177
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Food science
|
Research Institution | Kyoto University |
Principal Investigator |
|
Project Period (FY) |
2014-04-01 – 2017-03-31
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
|
Keywords | 食品工学 / 凍結濃縮 / マイクロカプセル / ナノ粒子 |
Outline of Final Research Achievements |
Sodium caseinate is known to form aggregated clusters (nanoparticle) under low pH conditions. Freezing potentially has effects on the nano-scale structural change of the clusters because of the formation of the freeze-concentrated phase. Sodium caseinate particles associated with β-carotene were prepared in this study via freeze-aging. Resultant properties were analyzed in terms of β-carotene encapsulation efficiency, surface hydrophobicity, small angle X-ray scattering, and digestively in a simulated gastric solution. The β-carotenes were found to distribute between the surface and interior of the freeze-dried specimens depending on the aging conditions. The surface hydrophobicity of the clusters also indicated a change in the particle microstructures due to the aging. Detail of this structural change in the freeze-concentrate was investigated by SAXS analyses. Interestingly, the freeze-aging also affect the microstructures of the casein clusters during digestion reaction.
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Report
(4 results)
Research Products
(11 results)