Functionality of Bovive Milk Fat Globule Membrane
| Project/Area Number |
01470132
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
畜産化学
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| Research Institution | Utsunomiya University |
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Principal Investigator |
KANNO Choemonn Utsunomiya Univ. ・Fac. of Agric., Prof.,, 農学部, 教授 (30011969)
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| Co-Investigator(Kenkyū-buntansha) |
AZUMA Norihiro Utsunomiya Univ. ・Fac. of Agric., Agric., Assoc. Prof.,, 農学部, 助教授 (30151062)
TANAKA Hideyuki Utsunomiya Univ. ・Fac. of Agric., Assoc. Prof.,, 農学部, 助教授 (70091949)
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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 |
¥5,600,000 (Direct Cost: ¥5,600,000)
Fiscal Year 1990: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 1989: ¥4,300,000 (Direct Cost: ¥4,300,000)
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| Keywords | milk, / emulsification, / intestinal absorption, / riboflavin, / vitamin B_2, / lipoprotein lipase / lipolysis, / milk fat globule membrane, / 乳脂肪球皮膜 / ビタミンB_2 / リポタンパク質リパ-ゼ / エマルション / 栄養機能 / ラクトフォリン / リポリシス |
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| Research Abstract |
We studied on the functionality of bovine milk fat globule membrane (MFGM) with special reference to 1) the emusifying ability of MFGM in milk fat globules (MFG), 2) the acceleration of intestinal absorption of riboflavin (RF) by MFGM and 3) inhibition of lipolysis due to lipoprotein lipase (LPL) in milk.
1) MFG emulsions were reconstituted by homogenizing 25% milk fat and 1% MFGM in 0.01M phosphate buffer (pH 7.0) for 1 min at 19 k rpm and at 45^0C. Maximal emulsifying properties were attained at 25% milk fat, 1% MFGM, neutral pH and the increased amount of MFGM. The major variables influencing the reconstitution of MFG were emulsifying time, MFGM and milk fat contents, and pH. Viscosity was highest at pH 5.0 and at 4 min of emulsifying time, and increased with MFGM content. The composition of MFGM protein adsorbed on MFG was not affected by the major variables. However, the amount of adsorbed protein increased at acidic pH and with the increased amount of MFGM. Diameter of MFG was 0.9
… More
-17.4mum and median diameter was 5.0mum and its specific surface area was 15.6 m^2/m^3.
2) Riboflavin bound MFGM was administered (3mug/g of diet) TO RF-defficient rats in who glutathion reductase activity ration (EGRAR, +FAD/-FAD) was 3.5, in comparison with free RF, after RF deprivation for 4 weeks. After RF feeding, EGRAR recovered to 1.6-1.9 and body weights increased in the fifth weeks. Gain of body weights for 1 week in the fifth weeks was 50.2<plus-minus>3.8 g for MFGM-RF-fed group, 40.4<plus-minus>3.9 g for free RF-fed group, and 33.1<plus-minus>5.4 g for pair-fed group. Significant differences were found among 3 groups (P<0.0 1). MFGM seemed to accelerate the absorption of RF from the intestine of rats. The peptides from MFGM may act as a signal peptide for the acceleration of the incorporating RF from intestinal mem
3) Lactophrin (LP), which is immunologically identical to the soluble glycoprotein (SGP) of MFGM, was isolated from milk whey. LP added in fresh bovine milk sonicated for 2 min at 200 W inhibited the lipolysis induced by milk indigeneus LPL. The ratio of inhibition was about 62-67% for LP and 30-43% for the LP- enriched component-3 fraction of proteose-peptone at 40 mg of protein/ml of milk over the control. LP and SGP seemed to be inhibited the lipolytic action of LPL by a high ability to replenish the surface of MFG. Less
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Report
(3 results)
Research Products
(7 results)
