Kinetics of Microaqueous Bioreactor System
Project/Area Number |
61470115
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Research Category |
Grant-in-Aid for General Scientific Research (B)
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Allocation Type | Single-year Grants |
Research Field |
反応工学
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Research Institution | Nagoya University |
Principal Investigator |
YAMANE Tsuneo Faculty of Agriculture, Nagoya University, Assoc. Prof., 農学部, 助教授 (70026102)
|
Project Period (FY) |
1986 – 1988
|
Project Status |
Completed (Fiscal Year 1988)
|
Budget Amount *help |
¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 1988: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1987: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1986: ¥1,900,000 (Direct Cost: ¥1,900,000)
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Keywords | Microaqueous Solvent System / Bioreactor / Lipase / Glycerolysis of Fats / Fat Hydroperoxide / Lactonization / Protein-bound Water / 自由水 / エステル合成 / 微水系 / 微孔性疎水性膜 / 酵素反応速度論 |
Research Abstract |
To establish the kinetics of enzynatic reaction in microaqueous organic solvent, quantitative investigations were performed on the states of water molecules in the microaqueous organic solvent, and on two different types of enzymatic reactions. The interesting results mentioned below were obtained. 1. Experimental procedure was established to determine separately protein-bound water and free water dissolved in organic solvent. Normal languimier-type ad-sorption isotherms were observed between the protein-bound water and the free water dissolved in water-miscible organic solvents, while abnormal monotonically rising isotherms were obtained between the protein-bound water and the free water dissolved in water-limmiscible organic solvents. Adsorption isotherms depend also on the purity of enzyme proteins, implying that water binds also impurities existing in the enzyme preparations. 2. Both batch and continuous glycerolysis of fat by lipase between two liquid phases consisting glycerik phas
… More
e and liquid fat phase were studied. The initial reaction rate of decreasing triglyceride content increased with the power of 1.7 of moisture content. the free fatty acid hardly formed below 4% moisture content in the glycerol phase, but started to form significantly above 4%. Half-life of the lipase was about 21 days at 40゜c. Fat peroxide not only inhibited the glycerolysis reaction but also inactivated it, but they were not serious. 3. Intramolecular esterification (lactonization) reaction of 15-hydroxypentadecanoic acid by lipase power suspended in microaqueous benzene was studied. Effects of moisture (both bound- and free -water) content on both initial reaction rate and product yield were made clear. The reaction rates increased first and decreased then with the increase in moisture content, giving rise to a maximum rate at a particular moisture content. The yield increased to almost 100% at decreasing moisture content. It was concluded that the reaction was limited by hydration of the enzyme protein at lower moisture content, while it was limited by true reversible reaction at elevated moisture content. Less
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Report
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Research Products
(31 results)