Tryptic hydrolysis of bovine αs2-casein: Identification and release kinetics of peptides

International Dairy Journal

Volumn 13, Issue 1, 2003, Pages 15-27

  Tauzin, J ^a   Miclo, L ^a   Roth, S ^a   Molle D ^b   Gaillard, J L ^a  

^a UNIVERSITÉ DE LORRAINE   (France)

^b CEMAGREF   (France)

Author keywords

Bovine S2 casein; Mass spectrometry; Peptide kinetics; Trypsin

Indexed keywords

BOVINAE;

EID: 0037286541     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-6946(02)00127-9     Document Type: Article

References (65)

1. Antal, J., Pal, G., Asboth, B., Buzas, Z., Patthy, A., & Graf, L. (2001). Specificity assay of serine proteinases by reverse-phase high-performance liquid chromatography analysis of competing oligopeptide substrate library. Analytical Biochemistry, 288, 156-167.
2. Benore-Parsons, M., Seidah, N. G., & Wennogle, L. P. (1989). Substrate phosphorylation can inhibit proteolysis by trypsin-like enzyme. Archives of Biochemistry and Biophysics, 272(2), 274-280.
3. S2 bovines. FEBS Letters, 71, 111-116.
4. S2-casein. FEBS Letters, 76, 274-279.
5. Chaplin, L. C. (1986). Hydrophobic interaction fast protein liquid chromatography of milk proteins. Journal of Chromatography, 363, 329-335.
6. Chrysina, E. D., Brew, K., & Acharya, K. R. (2000). Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2-Å resolution reveal an effect of calcium on inter-lobe interactions. Journal of Biological Chemistry, 275, 37021-37029.
7. Church, F. C., Swaisgood, H. E., Porter, D. H., & Catignani, G. L. (1983). Spectrophotometric assay using o-phtaldialdehyde for determination of proteolysis in milk and isolated milk proteins. Journal of Dairy Science, 66, 1219-1227.
8. Clare, D. A., & Swaisgood, H. E. (2000). Bioactive milk peptides: A prospectus. Journal of Dairy Science, 83, 1187-1195.
9. Creamer, L. K., & Matheson, A. R. (1981). Separation of bovine caseins using hydrophobic interaction chromatography. Journal of Chromatography, 210, 105-111.
10. Dalgalarrondo, M., Chobert, J.-M., Dufour, E., Bertrand-Harb, C., Dumont, J.-P., & Haertle, T. (1990). Characterization of bovine β-lactoglobulin B tryptic peptides by reversed-phase high performance liquid chromatography. Milchwissenschaft, 45, 212-216.
11. Damodaran, S. (1994). Structure-function relationship of food proteins. In N. S. Hettiarachchy, & G. R. Ziegler (Eds.), Protein functionality in food systems (pp. 1-37). New-York: Marcel Dekker.
12. Deléage, G., Blanchet, C., & Geourjon, C. (1997). Protein structure prediction. Implications for the biologist. Biochimie, 79, 681-686.
13. Deléage, G., & Roux, B. (1997). An algorithm for protein secondary structure prediction based on class prediction. Protein Engineering, 1, 289-294.
14. Diaz, O., Gouldsworthy, A. M., & Leaver, J. (1996). Identification of peptides released from casein micelles by limited trypsinolysis. Journal of Agricultural and Food Chemistry, 44, 2517-2522.
15. Ellegård, K. H., Gammelgård-Larsen, C., Sørensen, E. S., & Fedosov, S. (1999). Process scale chromatographic isolation, characterization and identification of tryptic bioactive casein phosphopeptides. International Dairy journal, 9, 639-652.
16. Farrell Jr., H. M., Brown, E. M., & Kumosinski, T. F. (1993). Three-dimensional molecular modeling of bovine caseins. Food structure, 12, 235-250.
17. Farrell Jr., H. M., Wickham, E. D., Dower, H. J., Piotrowski, E. G., Hoagland, P. D., Cooke, P. H., & Groves, M. L. (1999). Characterization of the particles of purified κ-casein: Trypsin as a probe of surface-accessible residues. Journal of Protein Chemistry, 8(6), 637-652.
18. Frischman, D., & Argos, P. (1996). Incorporation of non-local interactions in protein structure prediction from the amino acid sequence. Protein Engineering, 9, 133-142.
19. Frister, H., Meisel, H., & Schlimme, E. (1988). OPA method modified by use of N, N-dimethyl-2-mercaptoethylammonium chloride as thiol component. Fresenius Zeitschrift fur Analytische Chemie, 330, 631-633.
20. Gagnaire, V., & Léonil, J. (1998). Preferential sites of tryptic cleavage on the major bovine caseins within the micelle. Lait, 78, 471-489.
21. Gagnaire, V., Pierre, A., Mollé, D., & Léonil, J. (1996). Phosphopeptides interacting with colloidal calcium phosphate isolated by tryptic hydrolysis of bovine casein micelles. Journal of Dairy Research, 63, 405-422.
22. Garnier, J., Gibrat, J. F., & Robson, B. (1996). GOR method for predicting protein secondary structure for amino acid sequence. Methods in Enzymology, 266, 540-553.
23. Gourley, L., Gauthier, S. F., Pouliot, Y., Mollé, D., Léonil, J., & Maubois, J.-L. (1998). Identification of casein peptides interacting with polysulfone ultrafiltration membranes. Lait, 78, 633-646.
24. Grosclaude, F. (1988). Le polymorphisme génétique des principales lactoprotéines bovines. INRA Productions Animales, 1(1), 5-17.
25. S2-casein. Journal of Dairy Research, 46, 211-213.
26. Grosclaude, F., Mahé, M. F., Mercier, J. C., Bonnemaire, J., & Teissier, J. H. (1976). Polymorphisme des lactoprotéines de bovinés népalais. Annales de Génétique et Sélection Animales, 8, 481-491.
27. Guermeur, Y. (1998). Combinaison de classifieurs statistiques, application à la prédiction de structure secondaire des protéines. Ph.D. thesis, Université Paris VI, Paris, France.
28. S2-group-casein. Agricultural and Biological Chemistry, 47(7), 1467-1471.
29. S2-casein: Theoretical and experimental approaches. Journal of Dairy Science, 84, 1944-1949.
30. S1-casein adsorbed onto oil surfaces of emulsions and improvement of the emulsifying properties of protein. Journal of American Oil Chemistry Society, 64(12), 1688-1691.
31. Keil, B. (1971). Trypsin. In P. D. Boyer (Ed.), The enzymes (pp. 249-275). New York: Academic Press.
32. King, R. D., & Sternberg, M. J. (1996). Identification and application of the concepts important for accurate and reliable protein secondary structure prediction. Protein Science, 5, 2298-2310.
33. Kinsella, J. E. (1984). Milk proteins: Physicochemical and functional properties. Critical Reviews in Food Science and Nutrition, 21, 197-262.
34. S2-casein and κ-casein as determined by gel filtration. New-Zealand Journal of Dairy Science Technology, 18, 225-232.
35. Kumosinski, T. F., Brown, E. M., & Farrell Jr., H. M. (1991). Three-dimensional molecular modeling of bovine caseins: Alpha s1-casein. Journal of Dairy Science, 74, 2889-2895.
36. Kumosinski, T. F., Brown, E. M., & Farrell Jr., H. M. (1993a). Three-dimensional molecular modeling of bovine caseins: An energy-minimized beta-casein structure. Journal of Dairy Science, 76, 931-945.
37. Kumosinski, T. F., Brown, E. M., & Farrell Jr., H. M. (1993b). Three-dimensional molecular modeling of bovine caseins: A refined, energy-minimized kappa-casein structure. Journal of Dairy Science, 76, 2507-2520.
38. Lasa-Benito, M., Martin, O., Meggio, F., & Pinna, L. A. (1996). Golgi apparatus mammary gland casein kinase: Monitoring by a specific peptide substrate and definition of specificity determinants. FEBS Letters, 382, 149-152.
39. Le Bars, D., & Gripon, J.-C. (1989). Specificity of plasmin towards bovine alpha S2-casein. Journal of Dairy Research, 56(5), 817-821.
40. Levin, J. M., Robson, B., & Garnier, J. (1986). An algorithm for secondary determination in proteins based on sequence similarity. FEBS Letters, 205, 303-308.
41. S1 casein. European Journal of Biochemistry, 78, 411-417.
42. McSweeney, P. L., Olson, N. F., Fox, P. F., & Healy, A. (1994). Proteolysis of bovine alpha s2-casein by chymosin. Zeitschrift fur Lebensmittel - Untersuchung und Forschung, 199(6), 429-432.
43. Meisel, H. (1998). Overview on milk protein-derived peptides. International Dairy Journal, 8, 363-373.
44. Mercier, J.-C. (1981). Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie, 63, 1-17.
45. Miclo, L, Perrin, E., Driou, A., Papadopoulos, V., Boujrad, N., Vanderesse, R., Boudier, J. F., Desor, D., Linden, G., & Gaillard, J.-L. (2001) Characterization of alpha-casozepine, a tryptic peptide from bovine alpha(s1)-casein with benzodiazepine-like activity. FASEB Journal (June 8, 2001) 10.1096/fj.00-0685fje.
46. Mihalyi, E. (1972). Application of proteolytic enzymes to protein structure studies. Cleveland: CRC Press.
47. Mora-Gutierrez, A., Kumosinski, T. F., & Farrell Jr., H. M. (1998). κ-carrageenan interaction with bovine and caprine caseins as shown by sedimentation and nuclear magnetic resonance spectroscopic techniques. Journal of Agricultural and Food Chemistry, 46, 4987-4996.
48. Ng-Kwai-Hang, K. F., & Kroeker, E. M. (1984). Rapid separation and quantification of major caseins and whey proteins of bovine milk by polyacrylamide gel electrophoresis. Journal of Dairy Science, 67, 3052-3056.
49. Perrin, E., Miclo, L., Driou, A., & Linden, G. (1995). Rapid determination of the ratios of three aromatic amino acid residues in peptides by reversed-phase high-performance liquid chromatography with a high-resolution photodiode-array detector. Journal of Chromatography B, 664, 267-276.
50. S2-casein in solution by chymosin, plasmin, trypsin and Lactobacillus-proteinases. Agricultural Science in Finland, 2, 133-138.
51. Qin, B. Y., Bewley, M. C., Creamer, L. K., Baker, E. N., & Jameson, G. B. (1999). Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin. Protein Science, 8, 75-83.
52. S2-casein. European Journal of Biochemistry, 203, 381-386.
53. S2-casein from bovine milk. Journal of Dairy Research, 61, 485-493.
54. Rost, B., & Sander, C. (1993). Prediction of protein secondary structure at better than 70% accuracy. Journal of Molecular Biology, 232, 584-599.
55. S1-casein by fast protein liquid chromatography. Journal of Dairy Science, 72, 2242-2246.
56. Schanbacher, F. L., Talhouk, R. S., Murray, F. A., Gherman, L. I., & Willett, L. B. (1998). Milk-borne bioactive peptides. International Dairy Journal, 8, 393-403.
57. Schechter, I., & Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochemical and Biophysical Research Communications, 27, 157-162.
58. Schellenberger, V., Turck, C. W., Hedstrom, L., & Rutter, W. J. (1993). Mapping of the S′ of serine proteases using acyl transfer to mixtures of peptide nucleophiles. Biochemistry, 32, 4349-4353.
59. Schellenberger, V., Turck, C. W., & Rutter, W. J. (1994). Role of the S′ subsites in serine proteases. Active-site mapping of rat chymotrypsin, rat trypsin, α-lytic protease, and cercarial protease from Schistosoma mansoni. Biochemistry, 33, 4251-4257.
60. Schmidt, D. G. (1982). Association of caseins and casein micelle structure. In P. F. Fox (Ed.), Developments in dairy chemistry-1 (pp. 61-86). London and New-York: Applied Science Publishers.
61. Smart, J. L., & McCammon, J. A. (1999). Phosphorylation stabilizes the N-termini of α-helices. Biopolymers, 49, 225-233.
62. S2-casein. Biochimica et Biophysica Acta, 622, 268-276.
63. S2- and κ-casein from bovine milk. Milchwissenschaft, 47(9), 563-565.
64. Tomé, D., & Debabbi, H. (1998). Physiological effects of milk protein components. International Dairy Journal, 8, 383-392.
65. S2-casein. Milchwissenschaft, 44, 335-339.