Active oxygen improves the quality of food.
| Project/Area Number |
14580150
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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 |
食生活
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| Research Institution | Doshisha Women's College of Liberal Arts |
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Principal Investigator |
NISHIMURA Kimio Doshisha Women's College of Liberal Arts, Faculty of Human Life and Science, professor, 生活科学部, 教授 (60167567)
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| Project Period (FY) |
2002 – 2004
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| Project Status |
Completed (Fiscal Year 2004)
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| Budget Amount *help |
¥3,500,000 (Direct Cost: ¥3,500,000)
Fiscal Year 2004: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2003: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2002: ¥2,200,000 (Direct Cost: ¥2,200,000)
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| Keywords | Vitamin C / Beneficial effect / Superoxide anion radical / Thiyl radical / Actomyosin / Glutathione (GSH) / Ovalbumin (OVA) / Bovine serum albumin (BSA) / 品質改良 / 卵白アルブミン / 牛血清アルブミン / チィールラジカル / 活性酸素 / 電子スピン共鳴法 / パン / 小麦タンパク質 / スーパーオキサイドアニオンラジカル / かまぼこ / N-Ethylmaleimide |
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| Research Abstract |
Glutathione (GSH), actomysin, ovalbumin (OVA), bovine serum albumin (BSA) and GP-1, a peptide of gluten origin, were analyzed by ESR under illumination by white light. A solution of 20 mM GSH in 0.2 M sodium phosphate buffer (pH 7.0) containing 0.2 mM Rf was analyzed by ESR measurement under illumination by white light (520,000 lux), and a typical thiyl radical (S・) quartet signal of 1:2:2:1 intensity was detected. Although the presence of SOD (200 units/ml) gave a reduced signal intensity of 63.2±14.3% (n=3), the addition of Catalase did not. The signal obtained for 20 mM GSH solution was similar to the signal of DMPO-OOH with reduction in the concentration of GSH. Actomyosin sol (0.9±0.11 mmoles/ml) (n=3) prepared from Alaska Pollack frozen surimi, and containing 0.2 mM Rf was analyzed by ESR under illumination by white light (455,000 lux). The detected signal was similar to that obtained a GSH concentration of 1 mmoles/ml. This intensity decreased to 51.1±0.8 % (n=3) by modifying th
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e sulfhydryl group on actomyosin. Again, the presence of SOD (200 units/ml) gave a decreased signal intensity of 33.0±11.5 % (n=3), while the addition of Catalase did not. A 8.1% OVA in 0.2 M sodium phosphate buffer (pH 7.0) solution containing 0.2 mM Rf was illuminated by white light (650,000 lux), and a quartet signal of 1:2:2:1 intensity, which was the same as that obtained with GSH, indicating the presence of S・. The intensity of this signal was decreased by addition of SOD (2000 units/ml) to 42.72±9.2 % (n= 3), but no change was observed for Catalase addition. Also, the ESR signal of 8.1% OVA with modified sulfhydryl group solution was similar to DMPO-OOH. In the case of BSA, the simillar results were obtained. Additionally, a signal with 1:2:2:1 intensity was also obtained for reduced GP-1 which has a sulthydryl group generated by the reduction of SS linkages. Consistent with the previous results, the signal intensity decreased with addition of SOD to 58.33±6.53 % (n= 9 at least), but there was no effect with Catalase. However, a different signal from the 1:2:2:1 intensity pattern was obtained for GP-1. These results indicate that the beneficial effect of AsA on food protein is due to the creation of O^+_2 during oxidization of AsA, which promotes the generation of protein S・radicals leading to SS bonding between proteins through radical oxidization. Less
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Report
(4 results)
Research Products
(6 results)
