| Project/Area Number |
26660102
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Food science
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| Research Institution | Ibaraki University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2016: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2015: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2014: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
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| Keywords | 加熱凝固 / 筋原線維 / トリプシン / プロタミン / 分子間相互作用 / トリプシン処理 / ブタ筋原線維 / ミオシン結合タンパク質C / α‐アクチニン / ゲル化阻害能 / 塩基性ペプチド / 加熱ゲル化阻害 / ミオシン / C-タンパク質 / プロタミミン / トリプシン分解 / プロナーゼ分解 / 筋原線維タンパク質 / 加熱ゲル化阻害能 / タンパク質の不溶化 |
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| Outline of Final Research Achievements |
This study attempted to evaluate the mechanism of inhibition of thermal coagulation of porcine myofibril by protamine (PRO) which is basic peptide originated from salmon milt. Tryptic digested PRO (DP) was prepared and the effect of DP on the rheological properties of myofibril was studied. The more PRO was digested, the less DP inhibited the thermal coagulation of myofibril. Further, DP was dialyzed against distilled water and the retentate was recovered as R-DP. The inhibitory activity of R-DP against the coagulation of myofibril was higher than that of intact PRO. Judging from the analysis of protein-protein interaction using electrophoresis, it was suggested that the inhibitory activity of DP against the coagulation of myofibril would differ from that of intact PRO.
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