2000 Fiscal Year Final Research Report Summary
Effect of aqueous solvent structure on protein functions and food properties.
| Project/Area Number |
11660123
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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 |
食品科学・栄養科学
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| Research Institution | THE UNIVERSITY OF TOKYO |
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Principal Investigator |
MIYAWAKI Osato Graduate School of Agriculture and Life Sciences Associate Professor, 大学院・農学生命科学研究科, 助教授 (80012053)
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| Project Period (FY) |
1999 – 2000
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| Keywords | aqueous solution structure / water activity / thermal stability of proteins / intramolecular hydrophobic interaction of protein / enzyme-substrate affinity / enzyme-substrate hydrophobic interaction / sol-gel transition temperature / intermolecular interaction of macromolecules |
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| Research Abstract |
Aqueous solution is the major environment where enzyme functions and food properties are presented. In this research, the role of aqueous solution structure on enzyme functions and food properties was in vestigated. For this purpose, we introduced the parameter α, as an index of the solution structure, which was determined by the following equation :
γ_W=αX_S^2+βX_S^3
where γ_W (=a_W/X_W ; a_W, water activity ; X_W, molar fraction of water) is activity coefficient of water and X_S is molar fraction ofsolute.
Thermal stabilities of lysozyme, α-chymotripsinogen A, and alcohlodehydrogenase were proved to be strongly affected by the aqueous solution structure represented by the parameter α probably through its effect on the intramolecular hydrophobic interaction for protein molecules.
Enzyme kinetics were also affected by the aqueous solution structure described by the parameter α for alcoholdehydrogenase, lysozyme, and β-galactosidase. In this case, the solution structure affected the enzyme-substrate affinity through its effect on intermolecular hydrophobic interaction.
The relationship between the mechanical properties of aqueous polymer solution and the solution structure was also investigated.
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