Use of ultrasound spectroscopy to examine the effect of fatty acid sodium salt on the self assembly and gel formation of milk proteins at ambient temperature
| Project/Area Number |
22500747
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Eating habits, studies on eating habits
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| Research Institution | Nihon University |
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Principal Investigator |
OHTA Naoko 日本大学, 短期大学部, 教授 (00203795)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2010: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | β-ラクトブロブリンのゲル化 / カゼインの自己会合 / 超音波分光分析 / タンパク質ゲル / カゼインミセル / 脂肪酸塩 / 相転移 / 乳ホエータンパク質 / カゼイン / 自発的会合 / 卵白アルブミン |
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| Research Abstract |
Although β-CN micelle formations are quite different from β-LG gel formation in the presence offatty acid salts, β-CN can participate in the gel formation in the mixed protein system by the additionof fatty acid salt with suppressing own micelle formation. FT-IR analysis showed that although theamount of intermolecular β-sheet (1623 cm-1) of the protein was temporarily increased concomitantlywith casein micelle formation, and then the β-sheet decreased. In the case of it, ultrasonic spectroscopy has some advantages to know transient structural changes such as self assembly of caseinprotein not only gelation, if we use some other tools together like FT-IR spectroscopy.
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Report
(4 results)
Research Products
(8 results)
