| Project/Area Number |
01550751
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
化学工学
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| Research Institution | Kansai University |
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Principal Investigator |
YAGI Hideharu Kansai Univ. Assoc. Prof. of Eengneering, 工学部, 助教授 (70109891)
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| Project Period (FY) |
1989 – 1990
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| Project Status |
Completed (Fiscal Year 1990)
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| Budget Amount *help |
¥2,300,000 (Direct Cost: ¥2,300,000)
Fiscal Year 1990: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1989: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | Coacervation / Separation and Purification / Polymerization of peptide / Hydrolysis of cellulose / Ultrafiltration / Salting in and Salting out / 限外濾過 / バイオセパレ-ション / ペプチド / 酵素反応 / レオロジ- |
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| Research Abstract |
Protein dissolving in water sometimes generates a new phase in the process, when it is separated from a raw material and chemically or enzymatically modified. The effects of these phenomena on the bioseparation and bioreaction were experimentally examined and the following results were obtained :
1. Coacervation from the viewpoint of bioseparation : the partitioning of a protein, a constituent of nucleic acid and a sugar between the coacervate and equilibrium phases were examined in the gelatin-Na_2SO_4-water system. Tendencies of partitioning were different with species.
2. Polymerization of peptide : The substrate obtained from soy bean protein was modified with -chymotrypsin. In the reaction, the product once degraded was polymerized. The non-Newtonian behavior of the solution became significant with increasing degree of polymerization.
3. Application of coacervation into bioreaction : On the basis of information obtained in the study 1, the hydrolysis of cellulose for which the separation of the inhibitory products was effective was carried out in the gelatin-Na_2SO_4-water. High conversion could be achieved by the semibatch operation to exchange the equilibrium phase with a new solution at constant intervals.
4. Effect of coexisting salt on characteristics of protein ultrafiltration : The ultrafiltration of an aqueous papain solution containing ammonium sulfate of various concentrations was carried out in a stirred vessel type. Although the papain concentrations in the bulk liquid were much less than its solubility and the difference in viscosity of solutions was small, the characteristics of ultrafiltration varied with ammonium sulfate concentration. The mass transfer coefficients and the concentrations of papain at the interface of gel layer suggests that the degrees of aggregation were different even if the protein was unsaturated.
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