Analysis of relationship between molecular structure and hydrophobic hydration for amino acids in water.
Project/Area Number |
24500949
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Eating habits, studies on eating habits
|
Research Institution | Kitami Institute of Technology (2015) Prefectural University of Hiroshima (2012-2014) |
Principal Investigator |
Sato Yukinori 北見工業大学, 工学部, 教授 (50226015)
|
Co-Investigator(Renkei-kenkyūsha) |
MIYAWAKI OSATO 石川県立大学, 生物資源環境学部, 教授 (80012053)
|
Project Period (FY) |
2012-04-01 – 2016-03-31
|
Project Status |
Completed (Fiscal Year 2015)
|
Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2014: ¥520,000 (Direct Cost: ¥400,000、Indirect Cost: ¥120,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥3,380,000 (Direct Cost: ¥2,600,000、Indirect Cost: ¥780,000)
|
Keywords | アミノ酸 / 水和 / リンゴ / 酵素的褐変 / 色 / 糖 / 構造 |
Outline of Final Research Achievements |
Analysis of the relationship between the molecular structure and hydration of amino acids in water was carried out with the aim of clarifying the solvent-solute interaction, as represented by the parameter α, and inhibition of enzyme activity. The hydration of Gly-Gly, which is a dimer of glycine, in water increased to a greater extent than expected. Further, hydration of the Gly-trimer increased to a greater degree than that of the Gly-dimer, but the rate of increase was variable. Thus, the hydration of these Gly-oligomers is not simply the sum of the hydration of their constituent Gly residues. Furthermore, the differences in hydration of several D- or L-type hydrophobic amino acids may be not due to differences in their stereostructure. The solvent-solute interaction, represented by the parameter α, does not inhibit the enzyme responsible for browning of apples, due to its limited contribution.
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Report
(5 results)
Research Products
(6 results)