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Stability of milk fat globule membrane proteins toward human enzymatic gastrointestinal digestion

Trung Thien Le UGent, Tom Van de Wiele UGent, Ngoc Han Do Thi UGent, Griet Debyser UGent, Karin Struijs UGent, Bart Devreese UGent, Koen Dewettinck UGent and John Van Camp UGent (2012) JOURNAL OF DAIRY SCIENCE. 95(5). p.2307-2318
abstract
The milk fat globule membrane (MFGM) fraction refers to the thin film of polar lipids and membrane proteins that surrounds fat globules in milk. It is its unique biochemical composition that renders MFGM with some beneficial biological activities, such as anti-adhesive effects toward pathogens. However, a prerequisite for the putative bioactivity of MFGM is its stability during gastrointestinal digestion. We, therefore, subjected MFGM material, isolated from raw milk, to an in vitro enzymatic gastrointestinal digestion. Sodium dodecyl sulfate PAGE, in combination with 2 staining methods, Coomassie Blue and periodic acid Schiff staining, was used to evaluate polypeptide patterns of the digest, whereas mass spectrometry was used to confirm the presence of specific MFGM proteins. Generally, it was observed that glycoproteins showed higher resistance to endogenous proteases compared with non-glycosylated proteins. Mucin 1 displayed the highest resistance to digestion and a considerable part of this protein was still detected at its original molecular weight after gastric and small intestine digestion. Cluster of differentiation 36 was also quite resistant to pepsin. A significant part of periodic acid Schiff 6/7 survived the gastric digestion, provided that the lipid moiety was not removed from the MFGM material. Overall, MFGM glycoproteins are generally more resistant to gastrointestinal digestion than serum milk proteins and the presence of lipids, besides glycosylation, may protect MFGM glycoproteins from gastrointestinal digestion. This gastrointestinal stability makes MFGM glycoproteins amenable to further studies in which their putative health-promoting effects can be explored.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
milk fat globule membrane glycoprotein, gastrointestinal digestion, FRAGMENTS, INHIBITION, GLYCOPROTEIN, MUCIN, ROTAVIRUS INFECTIONS, PROTEOLYTIC DIGESTION, IN-VITRO, HUMAN-IMMUNODEFICIENCY-VIRUS, ACID, MODEL, dialysis, mucin 1
journal title
JOURNAL OF DAIRY SCIENCE
J. Dairy Sci.
volume
95
issue
5
pages
2307 - 2318
Web of Science type
Article
Web of Science id
000303074900007
JCR category
AGRICULTURE, DAIRY & ANIMAL SCIENCE
JCR impact factor
2.566 (2012)
JCR rank
3/54 (2012)
JCR quartile
1 (2012)
ISSN
0022-0302
DOI
10.3168/jds.2011-4947
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2108912
handle
http://hdl.handle.net/1854/LU-2108912
date created
2012-05-16 15:03:03
date last changed
2015-06-17 10:02:42
@article{2108912,
  abstract     = {The milk fat globule membrane (MFGM) fraction refers to the thin film of polar lipids and membrane proteins that surrounds fat globules in milk. It is its unique biochemical composition that renders MFGM with some beneficial biological activities, such as anti-adhesive effects toward pathogens. However, a prerequisite for the putative bioactivity of MFGM is its stability during gastrointestinal digestion. We, therefore, subjected MFGM material, isolated from raw milk, to an in vitro enzymatic gastrointestinal digestion. Sodium dodecyl sulfate PAGE, in combination with 2 staining methods, Coomassie Blue and periodic acid Schiff staining, was used to evaluate polypeptide patterns of the digest, whereas mass spectrometry was used to confirm the presence of specific MFGM proteins. Generally, it was observed that glycoproteins showed higher resistance to endogenous proteases compared with non-glycosylated proteins. Mucin 1 displayed the highest resistance to digestion and a considerable part of this protein was still detected at its original molecular weight after gastric and small intestine digestion. Cluster of differentiation 36 was also quite resistant to pepsin. A significant part of periodic acid Schiff 6/7 survived the gastric digestion, provided that the lipid moiety was not removed from the MFGM material. Overall, MFGM glycoproteins are generally more resistant to gastrointestinal digestion than serum milk proteins and the presence of lipids, besides glycosylation, may protect MFGM glycoproteins from gastrointestinal digestion. This gastrointestinal stability makes MFGM glycoproteins amenable to further studies in which their putative health-promoting effects can be explored.},
  author       = {Le, Trung Thien and Van de Wiele, Tom and Do Thi, Ngoc Han and Debyser, Griet and Struijs, Karin and Devreese, Bart and Dewettinck, Koen and Van Camp, John},
  issn         = {0022-0302},
  journal      = {JOURNAL OF DAIRY SCIENCE},
  keyword      = {milk fat globule membrane glycoprotein,gastrointestinal digestion,FRAGMENTS,INHIBITION,GLYCOPROTEIN,MUCIN,ROTAVIRUS INFECTIONS,PROTEOLYTIC DIGESTION,IN-VITRO,HUMAN-IMMUNODEFICIENCY-VIRUS,ACID,MODEL,dialysis,mucin 1},
  language     = {eng},
  number       = {5},
  pages        = {2307--2318},
  title        = {Stability of milk fat globule membrane proteins toward human enzymatic gastrointestinal digestion},
  url          = {http://dx.doi.org/10.3168/jds.2011-4947},
  volume       = {95},
  year         = {2012},
}

Chicago
Le, Trung Thien, Tom Van de Wiele, Ngoc Han Do Thi, Griet Debyser, Karin Struijs, Bart Devreese, Koen Dewettinck, and John Van Camp. 2012. “Stability of Milk Fat Globule Membrane Proteins Toward Human Enzymatic Gastrointestinal Digestion.” Journal of Dairy Science 95 (5): 2307–2318.
APA
Le, T. T., Van de Wiele, T., Do Thi, N. H., Debyser, G., Struijs, K., Devreese, B., Dewettinck, K., et al. (2012). Stability of milk fat globule membrane proteins toward human enzymatic gastrointestinal digestion. JOURNAL OF DAIRY SCIENCE, 95(5), 2307–2318.
Vancouver
1.
Le TT, Van de Wiele T, Do Thi NH, Debyser G, Struijs K, Devreese B, et al. Stability of milk fat globule membrane proteins toward human enzymatic gastrointestinal digestion. JOURNAL OF DAIRY SCIENCE. 2012;95(5):2307–18.
MLA
Le, Trung Thien, Tom Van de Wiele, Ngoc Han Do Thi, et al. “Stability of Milk Fat Globule Membrane Proteins Toward Human Enzymatic Gastrointestinal Digestion.” JOURNAL OF DAIRY SCIENCE 95.5 (2012): 2307–2318. Print.