1997 Fiscal Year Final Research Report Summary
The Study on Enzymic Synthesis of Sugar-Fatty Acid Ester
| Project/Area Number |
08650955
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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 |
生物・生体工学
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| Research Institution | Kitakyushu National College of Technology |
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Principal Investigator |
HATANAKA Chiaki Kitakyushu National College of Technology, Chemical Engineering, Professor, 化学工学科, 教授 (80180884)
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| Co-Investigator(Kenkyū-buntansha) |
GOTO Muneharu Kitakyushu National College of Technology, Chemical Engineering, Assistant, 化学工学科, 助手 (40259966)
IDE Shunsuke Kitakyushu National College of Technology, Integrated Arts & Science, Professor, 総合科学科, 教授 (10041550)
HARAGUCHI Toshihide Kitakyushu National College of Technology, Chemical Engineering, Professor, 化学工学科, 教授 (00038598)
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| Project Period (FY) |
1996 – 1997
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| Keywords | FOOD CHEMICAL ENGINEERING / LIPASE-CATALYZED ESTERIFICATION / LIPASE / SUGAR FATTY ACID ESTER / FATTY ACID / SUGAR ALCOHOL |
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| Research Abstract |
The enzymic eaterification reaction between sugar and oleic acid was examined by using the lipase from Candida Cylindracea and the conversion to the ester was investigated. The saturated aqueous solution of sugar alcohols such as Sorbitol, Erithritol, Xylitol, Mannnitol and Inositol were used as substrates. The reaction was carried out in a reaction system with a controlled very small water content. High cinversion was obtained in the case of Xylitol, Sorbitol, Erithritol and Mannitol, especially over 80% of conversion was attained in Xylitol and Sorbitol. From the result of DSC and UV-spectrum analysis, it seemed that the esterification reaction occurred at the interface between fatty acid and aqueous solution of sugars. When the water content of the reaction system was decreased, the concentration of the sugars at interface became higher and the reaction rate inceased, high conversion was obtained simultaneously by a shift of the equilibrium to the esterification. Sugar alcohols prod
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uced a higher conversion than sugar, but the ring sugar alcohol such as Inositol produced low conversion. The smaller the carbon number of the sugar and sugar alcohol, the greater the conversion. The minimum level of water content needed for esterification was estimated at the range of 300 to 4000 ppm. In these cases the water in the reaction system was bound to the enzyme protein and this water was needed to support the three-dimensional structure and the enzyme activity. From these results, the esterification conversion seemed to be influenced by the adsorption amounts of the sugar alcohol to the interface between water and oleic acid, and the amounts increased proportionally to the concentration and adsorption equilibrium constant of the sugar alcohol.
In order to produce the ester by the bioreactor continuously the lipase have to immobilize in the insoluble carrier. It was clear that the lipase was able to entrap in to the high molecular gels which were obtained by polymerization of suspended monomer, N-isopropylacrylamide.. The stability of the enzyme to the temperature and pH increase by this immobilization. And then the feasibility of immobilization of the lipase to silica and polystylene microspheres to which the amino or glycidyl methacylate group were introduced by plasma technique was investigated. These methods were available for the immobilization of lipase. Less
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