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All issues Volume 90 / No 5 (September–October 2010) Dairy Sci. Technol., 90 5 (2010) 549-563 References
Open Access
Issue
Dairy Sci. Technol.
Volume 90, Number 5, September–October 2010
Page(s) 549 - 563
DOI https://doi.org/10.1051/dst/2010018
Published online 07 April 2010
  1. Almaas H., Berner V., Holm H., Langsrud T., Vegarud G.E., Degradation of whey from caprine milk by human proteolytic enzymes, and the resulting antibacterial effect against Listeria monocytogenes, Small Rum. Res. 79 (2008) 11–15. [CrossRef] [Google Scholar]
  2. Almaas H., Cases A.-L., Devold T.G., Holm H., Langsrud T., Aabakken L., Ådnøy T., Vegarud G.E., In vitro digestion of bovine and caprine milk by human gastric and duodenal enzymes, Int. Dairy J. 16 (2006) 961–968. [CrossRef] [Google Scholar]
  3. Almaas H., Holm H., Langsrud T., Flengsrud R., Vegarud G.E., In vitro studies of the digestion of caprine whey proteins by human gastric and duodenal juice and the effects on selected microorganisms, Br. J. Nutr. 96 (2006) 562–569. [PubMed] [Google Scholar]
  4. Bos C., Mahé S., Gaudichon C., Benamouzig R., Gausserès N., Luengo C., Ferrière F., Rautureau J., Tomé D., Assessment of net postprandial protein utilization of N-15-labelled milk nitrogen in human subjects, Br. J. Nutr. 81 (1999) 221–226. [PubMed] [Google Scholar]
  5. Dalgleish D.G., Spagnuolo P.A., Douglas Goff H., A possible structure of the casein micelle based on high-resolution field-emission scanning electron microscopy, Int. Dairy J. 14 (2004) 1025–1031. [CrossRef] [Google Scholar]
  6. Dangin M., Boirie Y., Guillet C., Beaufrère B., Influence of the protein digestion rate on protein turnover in young and elderly subjects, J. Nutr. 132 (2002) 3228S–3233S. [PubMed] [Google Scholar]
  7. Dangin M., Guillet C., Garcia-Rodenas C., Gachon P., Bouteloup-Demange C., Reiffers-Magnani K., Fauquant J., Ballèvre O., Beaufrère B., The rate of protein digestion affects protein gain differently during aging in humans, J. Physiol. 549 (2003) 635–644. [Google Scholar]
  8. de Kruif C.G., Holt C., Casein micelle structure, function and interactions, in: Fox P.F., McSweeney P.L.H. (Eds.), Advanced Dairy Chemistry, Vol. 1: Proteins, Kluwer Academic/Plenum Publishers, New York, USA, 2003, pp. 233–276. [Google Scholar]
  9. Eriksen E.K., Vegarud G.E., Langsrud T., Almaas H., Lea T., Effect of milk proteins and their hydrolysates on in vitro immune responses, Small Rum. Res. 79 (2008) 29–37. [CrossRef] [Google Scholar]
  10. Exposito I.L., Recio I., Antibacterial activity of peptides and folding variants from milk proteins, Int. Dairy J. 16 (2006) 1294–1305. [CrossRef] [Google Scholar]
  11. Fox P.F., McSweeney P.L.H., Dairy Chemistry and Biochemistry, Blackie Academic and Professional, London, UK, 1998. [Google Scholar]
  12. Holm H., Hanssen L.E., Krogdahl A., Florholmen J., High and low inhibitor soybean meals affect human duodenal proteinase activity differently – in vivo comparison with bovine serum-albumin, J. Nutr. 118 (1988) 515–520. [PubMed] [Google Scholar]
  13. Jenness R., Koops J., Preparation and properties of a salt solution which simulates milk ultrafiltrate, Neth. Milk Dairy J. 16 (1962) 153–164. [Google Scholar]
  14. Kim S.B., Ki K.S., Khan M.A., Lee W.S., Lee H.J., Ahn B.S., Kim H.S., Peptic and tryptic hydrolysis of native and heated whey protein to reduce its antigenicity, J. Dairy Sci. 90 (2007) 4043–4050. [CrossRef] [PubMed] [Google Scholar]
  15. Korhonen H., Pihlanto A., Bioactive peptides: production and functionality, Int. Dairy J. 16 (2006) 945–960. [CrossRef] [Google Scholar]
  16. Krogdahl A., Holm H., Inhibition of human and rat pancreatic proteinases by crude and purified soybean proteinase-inhibitors, J. Nutr. 109 (1979) 551–558. [PubMed] [Google Scholar]
  17. Lacroix M., Bos C., Léonil J., Airinei G., Luengo C., Dare S., Benamouzig R., Fouillet H., Fauquant J., Tomé D., Gaudichon C., Compared with casein or total milk protein, digestion of milk soluble proteins is too rapid to sustain the anabolic postprandial amino acid requirement, Am. J. Clin. Nutr. 84 (2006) 1070–1079. [PubMed] [Google Scholar]
  18. Laemmli U.K., Cleavage of structural proteins during assembly of head of bacteriophage-T4, Nature 227 (1970) 680–685. [CrossRef] [PubMed] [Google Scholar]
  19. Mahé S., Benamouzig R., Gaudichon C., Huneau J.F., Decruz I., Rautureau J., Tomé D., Nitrogen movements in the upper jejunum lumen in humans fed low amounts of casein or beta-lactoglobulin, Gastroenterol. Clin. Biol. 19 (1995) 20–26. [PubMed] [Google Scholar]
  20. Mahé S., Roos N., Benamouzig R., Davin L., Luengo C., Gagnon L., Gausserges N., Rautureau J., Tomé D., Gastrojejunal kinetics and the digestion of [N-15]beta-lactoglobulin and casein in humans: the influence of the nature and quantity of the protein, Am. J. Clin. Nutr. 63 (1996) 546–552. [PubMed] [Google Scholar]
  21. Malacarne M., Martuzzi F., Summer A., Mariani P., Protein and fat composition of mare’s milk: some nutritional remarks with reference to human and cow’s milk, Int. Dairy J. 12 (2002) 869–877. [CrossRef] [Google Scholar]
  22. Martin P., Grosclaude F., Improvement of milk protein-quality by gene technology, Livest. Prod. Sci. 35 (1993) 95–115. [CrossRef] [Google Scholar]
  23. McMahon D.J., Oommen B.S., Supramolecular structure of the casein micelle, J. Dairy Sci. 91 (2008) 1709–1721. [CrossRef] [PubMed] [Google Scholar]
  24. Miranda G., Mahé M.-F., Leroux C., Martin P., Proteomic tools to characterize the protein fraction of Equidae milk, Proteomics 4 (2004) 2496–2510. [CrossRef] [PubMed] [Google Scholar]
  25. Ochirkhuyag B., Chobert J.M., Dalgalarrondo M., Haertlé T., Characterization of mare caseins. Identification of αs1- and αs2-caseins, Lait 80 (2000) 223–235. [CrossRef] [EDP Sciences] [Google Scholar]
  26. Orsi N., The antimicrobial activity of lactoferrin: current status and perspectives, Biometals 17 (2004) 189–196. [CrossRef] [PubMed] [Google Scholar]
  27. Park Y.W., Goat milk – chemistry and nutrition, in: Park Y.W., Haenlein G.F.W. (Eds.), Handbook of Milk of Non-Bovine Mammals, Blackwell Publishing, Oxford, UK, 2006, pp. 34–58. [Google Scholar]
  28. Salami M., Yousefi R., Ehsani M.R., Dalgalarrondo M., Chobert J.-M., Haertlé T., Razavi S.H., Saboury A.A., Niasari-Naslaji A., Moosavi-Movahedi A.A., Kinetic characterization of hydrolysis of camel and bovine milk proteins by pancreatic enzymes, Int. Dairy J. 18 (2008) 1097–1102. [CrossRef] [Google Scholar]
  29. Sanchez-Chiang L., Cisternas E., Ponce O., Partial-purification of pepsins from adult and juvenile salmon fish Oncorhynchus keta. Effect of NaCl on proteolytic activities, Comp. Biochem. Physiol. B 87 (1987) 793–797. [CrossRef] [PubMed] [Google Scholar]
  30. Tomé D., Debabbi H., Physiological effects of milk protein components, Int. Dairy J. 8 (1998) 383–392. [CrossRef] [Google Scholar]