| Project/Area Number |
62560135
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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 |
製造化学・食品
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| Research Institution | Science University of Tokyo |
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Principal Investigator |
ASO Keiichi Science University of Tokyo, Faculty of Science and Technology, 理工学部, 講師 (70130325)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1988: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1987: ¥1,500,000 (Direct Cost: ¥1,500,000)
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| Keywords | hollow fiber reactor / papain / dextran-modified enzyme / polyethylene glycol-modified enzyme / low-phenylalanine peptides / ゼインの酵素修飾 / 食品蛋白質の酵素修飾 / ホローファイバー / ゼイン |
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| Research Abstract |
It is an important subject for food scientists to elucidate a structure-functionality relationship of food proteins and peptides. In order to produce basic food materiasl by enzymatic modification of food proteins, a basic research was conducted on a hollow fiber reactor system and on the application of enzymatic modification using proteolytic enzymes to improve functional properties of food proteins.
The results obtained were: 1. The efficiency of the hydrolytic reaction by papain in a hollow fiber reactor system was analyzed under several operating conditions. Inactivation of the enzyme by mechanical stress was noted as a serious cause of negative effects among various factors. 2. The modification of the enzyme with high molecular polymers such as dextran and polyethylene glycol enhanced its stability under various operating conditions and was recomended as a suitable method for tailoring reactor enzymes. 3. Peptide mixtures containing little phenylalanine were prepared from soy protein by a combination of -chymotrypsin and carboxypeptidase A or a use of pronase through a hollow fiber system. 4. Zein, a low applicable prolamin in maize, was converted to low molecular weight peptides by limited proteolysis in aqueous organic solvents based on its less susceptible secondary structure for the enzyme action.
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