Role of intestinal brush border peptidases in the simulated digestion of milk proteins

Molecular Nutrition and Food Research

Volumn 59, Issue 5, 2015, Pages 948-956

  Picariello, Gianluca ^a   Miralles, Beatriz ^b   Mamone, Gianfranco ^a   Sánchez Rivera, Laura ^b   Recio, Isidra ^b   Addeo, Francesco ^c   Ferranti, Pasquale ^c  

^a CNR   (Italy)

^b INSTITUTE OF FOOD SCIENCE RESEARCH CIAL   (Spain)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Brush border membrane hydrolases; Degree of hydrolysis; Gastrointestinal digestion; In vitro digestion models; Milk proteins

Indexed keywords

SUS;

MILK PROTEIN; PEPTIDE HYDROLASE;

ANIMAL; DIGESTION; ENZYMOLOGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; JEJUNUM; METABOLISM; MICROVILLUS; PHYSIOLOGY; PIG; REVERSED PHASE LIQUID CHROMATOGRAPHY;

ANIMALS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, REVERSE-PHASE; DIGESTION; JEJUNUM; MICROVILLI; MILK PROTEINS; PEPTIDE HYDROLASES; SWINE;

EID: 84928763372     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201400856     Document Type: Article

References (30)

1. Picariello, G., Ferranti, P., Fierro, O., Mamone, G. et al., Peptides surviving the simulated gastrointestinal digestion of milk proteins: biological and toxicological implications. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2010, 878, 295-308.
2. Picariello, G., Iacomino, G., Mamone, G., Ferranti, P. et al., Transport across Caco-2 monolayers of peptides arising from in vitro digestion of bovine milk proteins. Food Chem. 2013, 139, 203-212.
3. Minekus, M., Alminger, M., Alvito, P., Balance, S. et al., A standardised static in-vitro digestion method suitable for food-an international consensus. Food Funct. 2014, 5, 1113-1124.
4. Bouzerzour, K., Morgan, F., Cuinet, I., Bonhomme, C. et al., In vivo digestion of infant formula in piglets: protein digestion kinetics and release of bioactive peptides. Br. J. Nutr. 2012, 108, 2105-2114.
5. Boutrou, R., Gaudichon, C., Dupont, D., Jardin, J. et al., Sequential release of milk protein-derived bioactive peptides in the jejunum in healthy humans. Am. J. Clin. Nutr. 2013, 97, 1314-1323.
6. Quirós, A., Dávalos, A., Lasunción, M. A., Ramos, M. et al., Bioavailability of the antihypertensive peptide LHLPLP. Transepithelial flux of HLPLP. Int. Dairy J. 2008, 18, 279-286.
7. Holmes, R., Lobley, R. W., Intestinal brush border revisited. Gut 1989, 30, 1667-1678.
8. McConnell, R. E., Benesh, A. E., Mao, S., Tabb, D. L. et al. Proteomic analysis of the enterocyte brush border. Am. J. Physiol. Gastrointest. Liver Physiol. 2011, 300, G914-G26.
9. Shan, L., Molberg, Ø., Parrot, I., Hausch, F. et al., Structural basis for gluten intolerance in celiac sprue. Science 2002, 297, 2275-2279.
10. Hausch, F., Shan, L., Santiago, N. A., Gray, G. M. et al. Intestinal digestive resistance of immunodominant gliadin peptides. Am. J. Physiol. Gastrointest. Liver Physiol. 2002, 283, G996-G1003.
11. Mamone, G., Ferranti, P., Rossi, M., Roepstorff, P. et al., Identification of a peptide from alpha-gliadin resistant to digestive enzymes: implications for celiac disease. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2007, 855, 236-241.
12. Sánchez-Rivera, L., Diezhandino, I., Gómez-Ruiz, J. Á., Fresno, J. M. et al., Peptidomic study of Spanish blue cheese (Valdeón) and changes after simulated gastrointestinal digestion. Electrophoresis 2014, 35, 1627-1636.
13. Shirazi-Beechey, S. P., Davies, A. G., Tebbutt, K., Dyer, J. et al., Preparation and properties of brush-border membrane vesicles from human small intestine. Gastroenterology 1990, 98, 676-685.
14. Piper, J. L., Gray, G. M., Khosla, C., Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo. J. Pharmacol. Exp. Ther. 2004, 311, 213-219.
15. Adler-Nissen, J., Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. Food Chem. 1979, 27, 1256-1262.
16. Hermanson, G. T., Bioconjugate Techniques, Academic Press, San Die go, CA 1996, pp. 112-113.
17. Kitabatake, N., Kinekawa Y.-I., Digestibility of bovine milk whey protein and β-lactoglobulin in vitro and in vivo. J. Agric. Food Chem. 1998, 46, 4917-4923.
18. Nielsen, P. M., Petersen, M., Dambmann, C., Improved method for determining food protein degree of hydrolysis. J. Food Sci. 2001, 66, 642-646.
19. Moreno, F. J., Mackie, A. R., Mills, C. E. N., Phospholipid interactions protect the milk allergen alpha-lactalbumin from proteolysis during in vitro digestion. J. Agric. Food Chem. 2005, 53, 9810-9816.
20. Mandalari, G., Mackie, A. M., Rigby, N. M., Wickham, M. S. et al., Physiological phosphatidylcholine protects bovine beta-lactoglobulin from simulated gastrointestinal proteolysis. Mol. Nutr. Food Res. 2009, 53, S131-S139.
21. Berecz, B., Mills, C. E. N., Parádi, I., Láng, F. et al., Stability of sunflower 2S albumins and LTP to physiologically relevant in vitro gastrointestinal digestion. Food Chem. 2013, 138, 2374-2381.
22. Gass, J., Vora, H., Hofmann, A. F., Gray, G. M. et al., Enhancement of dietary protein digestion by conjugated bile acids. Gastroenterology 2007, 133, 16-23.
23. Kopf-Bolanz, K. A., Schwander, F., Gijs, M., Vergères, G. et al. Validation of an in vitro digestive system for studying macronutrient decomposition in humans. J. Nutr. 2012, 142, 245-250.
24. Moreno, F. J., Quintanilla-López, J. E., Lebrón-Aguilar, R., Olano, A. et al., Mass spectrometric characterization of glycated beta-lactoglobulin peptides derived from galacto-oligosaccharides surviving the in vitro gastrointestinal digestion. J. Am. Soc. Mass Spectrom. 2008, 19, 927-937.
25. Ohsawa, K., Satsu, H., Ohki, K., Enjoh, M. et al. Producibility and digestibility of antihypertensive beta-casein tripeptides, Val-Pro-Pro and Ile-Pro-Pro, in the gastrointestinal tract: analyses using an in vitro model of mammalian gastrointestinal digestion. J. Agric. Food Chem. 2008, 56, 854-858.
26. Foltz, M., Cerstiaens, A., vanMeensel, A., Mols, R. et al. The angiotensin converting enzyme inhibitory tripeptides Ile-Pro-Pro and Val-Pro-Pro show increasing permeabilities with increasing physiological relevance of absorption models. Peptides 2008, 29, 1312-1320.
27. Regazzo, D., Mollé, D., Gabai, G., Tomé, D. et al. The (193-209) 17-residues peptide of bovine β-casein is transported through Caco-2 monolayer. Mol. Nutr. Food Res. 2010, 54, 1428-1435.
28. Sánchez-Rivera, L., Ares, I., Miralles, B., Gómez-Ruiz, J. et al. Bioavailability and kinetics of the antihypertensive casein-derived peptide HLPLP in rats. J. Agric. Food Chem. 2014, 62, 11869-11875.
29. Sélo, I., Clément, G., Bernard, H., Chatel, J. et al., Allergy to bovine beta-lactoglobulin: specificity of human IgE to tryptic peptides. Clin. Exp. Allergy 1999, 29, 1055-1063.
30. Mace, O. J., Marshall, F., Digestive physiology of the pig symposium: gut chemosensing and the regulation of nutrient absorption and energy supply. J. Anim. Sci. 2013, 91, 1932-1945.