Project/Area Number |
07680043
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
家政学
|
Research Institution | KYORITSU WOMEN'S UNIVERSITY |
Principal Investigator |
UTSUNOMIYA Nobuko KYORITSU WOMEN'S UNIVERSITY,FACULTY OF HOME ECONOMICS,DEPARTMENT OF FOOD SCIENCE,ASSOCIATE PROFESSOR, 家政学部・食物学科, 助教授 (40086731)
|
Project Period (FY) |
1995 – 1996
|
Project Status |
Completed (Fiscal Year 1996)
|
Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1996: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1995: ¥1,500,000 (Direct Cost: ¥1,500,000)
|
Keywords | MODIFIED PROTEIN / CASEIN / SOY-PROTEIN / BOVINE SERUM ALBUMIN (BSA) / UREA CYCLE / DIGESTION-ABSORPTION / AMINO CARBONYL REACTION / 牛血清アルブミン / 消化 / 吸収 / メイラード反応 / アマドリ転位生成物 / Modified Proteins / Digestion / Absorption |
Research Abstract |
This study investigates the physiological effects on rats of protein (casein, soy-protein and bovine serum albumin) modified by D-glucose at 50゚C and RH 75%. 1) Digestion-absorption of protein modified by glucose : We analyzed the in vitro and in vivo free amino acids and peptides produced by the digestion or absorption of modified BSA.The in vitro digestion of modified BSA was slower than that of native BSA.A decrease in free amino acids in the products of modified BSA digested by pepsin-pancreatin was observed in comparison with native BSA.The in vivo digested peptide patterns in rat small intestine was similar between modified and native BSA.These result show that while there was a difference in the quantity of each peptide, there was no great difference in the pattern of these peptides. 2) Effects of modified protein on the urea cycle in rats : Modified soy-protein and casein were each used as a protein source for the experiments in this study. We analyzed the urea nitrogen (BUN), creatinine and nitrogen in the serum, feces and urine of rats. There was generally no difference in the level of BUN or creatinine in the serum and urine. There results imply no difference in the effect on the urea cycle of the modified and native proteins. 3) Physiological effects of low-molecular-weight products on the amino carbonyl reaction in rats : When a protein or peptide was reacted with carbonyl compounds, peptide bond cleavage occurred from the C-terminal amino acid, and free amino acids, secondary products and products of low-molecular-weight were generated. The degree of modification of glycine residues in an aqueous solution with glucose heated at 95゚C was controlled at the level of 30% or 70%. These results indicate that the low-molecular-weight fraction of the glycine-glucose reaction products reduced the absorption of glucose, triglyceride and free amino acids in the serum of rats.
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