• Food Science of Animal Resources
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• v.31 no.1
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• pp.1-8
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• 2011

A unique biophysical membrane which surrounds the milk fat globules is called the milk fat globule membrane (MFGM). Various researches were studied about origin, composition, structure and bioactive components of MFGM. Bioactive protein components of MFGM play an important beneficiary function such as defense mechanism in new born. Among the bioactive lipid components from MFGM phospholipids showed health enhancing functions. The phospholipids also help in the production of certain dairy product from deterioration. MFGM phospholipids also showed antioxidant activity in some dairy products such as butter and ghee produced from milk of buffalo. Based on the beneficial effects, researchers developed MFGM as functional ingredients in various food products. This current review focuses on health enhancing function of MFGM and its components in various dairy products.

• Journal of Dairy Science and Biotechnology
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• v.15 no.1
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• pp.27-32
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• 1997

Most lipids in milk are dispetsed as the form of fat globules. Apical portion of plasma membrane is coated with fat globules, which are synthesized from mammary epithelial cells and then secreted into the lumen. The unique phenomenon in separation of the plasma membrane from the cell is observed only in mammary system. It has been suggested that milk fat globule membrane(MFGM) is formed from endoplasmic reticulum, Golgi apparatus, secretory granule to plasma membrane. For this reason MFGM is important for nuderstanding the structure and function of biological membrane. Because MFGM also plays an important role in inhibition of lipase action, stimulation of nutrient digestion and absorption, emulsion or function as natural liposome, study of the major components in MFGM will provide the opportunity for more broad industrial uses of MFGM in the future.

• Food Science of Animal Resources
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• v.42 no.3
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• pp.351-371
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• 2022

Milk fats are present as globules emulsified in the aqueous phase of milk and stabilized by a delicate membrane architecture called milk fat globule membrane (MFGM). The unique structure and composition of the MFGM play an important role in fat digestion and the metabolic programming of neonates. The objective of this review is to compare the structure, composition, and physicochemical characteristics of fat globules in human milk, bovine milk, and infant formula. It provides an overview of the fat digestion process and enzymes in healthy infants, and describes the possible roles of the MFGM in association with factors affecting fat digestion. Lastly, the health benefits of the MFGM on infant nutrition and future perspectives are discussed with a focus on brain development, metabolic response, and gut health.

• Food Science of Animal Resources
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• v.40 no.2
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• pp.209-220
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• 2020

Milk fat globule membrane (MFGM) is a lipid carrier in mammals including humans that consists mainly of polar lipids, like phospholipids and glycolipids. In this study, a process to enrich polar lipids in commercial butter and whey powder, including polar lipids of MFGM, was developed. WPC (whey protein concentrate) 60 was selected as the most suitable raw material based on the yield, phospholipid, protein, and lactose content of the polar lipid fraction obtained by ethanol extraction of two WPC (WPC60 and WPC70) and two buttermilk (A and B). After fractionation under optimum conditions, the polar-lipid enriched fraction from WPC60 contained 38.56% phospholipids. The content of glycolipids, cerebroside, lactosylceramide, ganglioside GM3, ganglioside GD3, was 0.97%, 0.55%, 0.09%, and 0.14%, respectively. Rancimat results showed that the oxidation stability of fish oil increased with an increase in the polar-lipid fraction by more than 30 times. In addition, the secretion of IL-6 and TNF-α decreased in a concentration-dependent manner after treatment of RAW 264.7 cells with 0.1 to 100 ppm of the polar lipid fraction. In this study, polar lipid concentrates with antioxidant and anti-inflammatory activity, were prepared from milk processing by-products. The MFGM polar lipid concentrates made from by-products are not only additives for infants, but are also likely to be used as antioxidants in cooking oils and as active ingredients for functional foods.

• Journal of Dairy Science and Biotechnology
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• v.14 no.2
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• pp.175-183
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• 1996

• Journal of Dairy Science and Biotechnology
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• v.19 no.1
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• pp.39-48
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• 2001

As the development of medical technology and the elevation of the standard of living, the population rate of elderly people in Korea is increasing gradually. To keep a good lift quality of the elderly, both appropriate exercise and nutrients intake are necessary for them. Dairy products are known for the good source of variable nutrients including functional components and bioactive peptides such as Ig, lactoferrin, MFGM, OPP, CPP, GMP, sialic acid etc that are required especially for elderly people. However, they are classified as the low dairy products consumption group recently. For the promotion of dairy product consumption of elderly people, variable and specialized dairy products for the elderly should be researched and developed with the strengthened publicity activities.

• Food Science of Animal Resources
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• v.18 no.2
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• pp.185-191
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• 1998

Human milk and bovine milk in normal stage were fractionated four parts : whey, skimmilk membrane, and casein pellet. The specific activity (nmole / mim / mg protein) and distribution ratio(%) of suborganella marker enzymes in each separated milk fraction were determined. Especially, neutral $Ca^{2+}$-ATPase, acid $Ca^{2+}$-ATPase, NADH-cytochrome C reductase, and acid phosphatase were higher in human milk. However, both $Ca^{2+}$-ATPases were not detected in all fractions of bovine milk. On the other hand, 5'-nucleotidase, phosphodiesterase I, alkaline phosphatase, and $\gamma$-glutamyl transpeptidase activities in bovine milk were higher than in human milk. Most of the marker enzymes were highly distributed in cream fraction of either human milk or bovine milk, and their specific activities were high to 24 fold from 3 fold when compared with that of whole milk. These results suggest that marker enzymes in mammary epitherial cell are transfered into cream fraction by the membrane rearrangement, and different biochemical reaction between human and bovine exists for milk secretion in mammary gland.

• Food Science of Animal Resources
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• v.21 no.4
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• pp.367-373
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• 2001

Glycoproteins PAS-6(50 kDa) and -7(47 kDa) from the bovine milk fat globule membrane share a common protein core but differ in their carbohydrate moiety. We have analyzed and proposed the structures of the N-linked sugar chains of PAS-7 by Oxford Glyco System(OGS) RAAM2000. The N-linked sugar chains were liberated from PAS-7 by hydrazinolysis and, after modifying the reducing ends with 2-aminobenzamide(2-AB), were separated into one neutral(7N, 55%) and two acidic(7M, mono-, 43%; 7D, di-, 2%) sugar chain groups. 7N was finally separated into 5 chains(a, b, c, d, and e), respectively. The structure of this 2AB-neutral sugar chain was determined by sugar analysis, exoglycosidase digestion with OGS glycosidase Kit and OGS RAAM2000 system. The results show that fraction e was the same of reported 7N1A, the biantennary complex type with a fucose on reducing end and two N-acetyllactosamine branch on non-reducing end. Therefore, it was proved that OGS RAAM2000 method is in conformity with conventional analysis of sugar chain structure from bovine PAS-7.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.4
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• pp.576-584
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• 2002

Bovine PAS-4 is an integral membrane glycoprotein expressed in mammary epithelial cells. Complementary DNA (cDNA) cloning of PAS-4 was performed by reverse-transcriptase polymerase chain reaction (RT-PCR) with oligonucleotide probes based on it's amino terminal and internal tryptic-peptides. The cloned PAS-4 cDNA was 1,852 nucleotides (nt) long and its open reading frame (ORF) was encoded 1,413 base long. The deduced amino acid sequence indicated that PAS-4 consisted of 471 amino acid residues with molecular weight of 52,796, bearing 8 potential N-glycosylation sites and 9 cysteine residues. Partial bovine CD36 cDNA from liver also was sequenced and the homology of both nucleotide sequence was 94%. Most of the identical amino acid residues were in the luminal/extracellular domains. Contrary to PAS-4, bovine liver CD36 displays 6 potential N-glycosylation sites, which were located, except for those at positions 101 and 171, at same positions as PAS-4 cDNA. Cysteine residues of PAS-4 and CD36 were same at position and in numbers. Northern blot analysis showed that PAS-4 was widely expressed, although its mRNA steady-state levels vary considerably among the analyzed cell types. PAS-4 possessed hydrophobic amino acid segments near the amino- and carboxyl-termini. Two short cytoplasmic tails of the amino- and carboxyl-terminal ends constituted of a 5-7 and 8-11 amino acid residues, respectively.