In vitro digestion of purified β-casein variants A1, A2, B, and I: Effects on antioxidant and angiotensin-converting enzyme inhibitory capacity

Journal of Dairy Science

Volumn 98, Issue 1, 2015, Pages 15-26

  Petrat Melin, B ^a   Andersen, P ^a   Rasmussen, J T ^a   Poulsen, N A ^a   Larsen, L B ^a   Young, J F ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

Bioactive peptide; Genetic polymorphism; Milk protein; casein

Indexed keywords

BOVINAE;

AMINO ACID; ANTIOXIDANT; CASEIN; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; MILK PROTEIN; PEPSIN A; PEPTIDE; TRYPSIN;

AMINO ACID SEQUENCE; ANALYSIS; ANIMAL; BOVINE; CHEESE; CHEMISTRY; DIGESTION; FEMALE; GENETIC POLYMORPHISM; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IN VITRO STUDY; METABOLISM; MILK; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; ANIMALS; ANTIOXIDANTS; CASEINS; CATTLE; CHEESE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIGESTION; FEMALE; IN VITRO TECHNIQUES; MILK; MILK PROTEINS; PEPSIN A; PEPTIDES; PEPTIDYL-DIPEPTIDASE A; POLYMORPHISM, GENETIC; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPSIN;

EID: 84918838645     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2014-8330     Document Type: Article

References (63)

1. •+) with amino acids. Kinetics and mechanism. Can. J. Chem. 2000, 78:1052-1059.
2. Anson M.L., Mirsky A.E. The estimation of pepsin with hemoglobin. J. Gen. Physiol. 1932, 16:59-63.
3. Barkholt V., Jensen A.L. Amino-acid analysis-Determination of cysteine plus half-cystine in proteins after hydrochloric-acid hydrolysis with a disulfide compound as additive. Anal. Biochem. 1989, 177:318-322.
4. Bobe G., Beitz D.C., Freeman A.E., Lindberg G.L. Separation and quantification of bovine milk proteins by reversed-phase high-performance liquid chromatography. J. Agric. Food Chem. 1998, 46:458-463.
5. Bonfatti V., Grigoletto L., Cecchinato A., Gallo L., Carnier P. Validation of a new reversed-phase high-performance liquid chromatography method for separation and quantification of bovine milk protein genetic variants (vol 1195, pg 101, 2008). J. Chromatogr. A 2009, 1216:1528.
6. Calbet J.A., Holst J.J. Gastric emptying, gastric secretion and enterogastrone response after administration of milk proteins or their peptide hydrolysates in humans. Eur. J. Nutr. 2004, 43:127-139.
7. Caroli A.M., Chessa S., Erhardt G.J. Invited review: Milk protein polymorphisms in cattle: Effect on animal breeding and human nutrition. J. Dairy Sci. 2009, 92:5335-5352.
8. s-, β- and κ-caseins by batchwise ion-exchange separation. J. Dairy Res. 1992, 59:551-556.
9. Chen H.M., Muramoto K., Yamauchi F., Fujimoto K., Nokihara K. Antioxidative properties of histidine-containing peptides designed from peptide fragments found in the digests of a soybean protein. J. Agric. Food Chem. 1998, 46:49-53.
10. Cheung H.S., Wang F.L., Ondetti M.A., Sabo E.F., Cushman D.W. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. J. Biol. Chem. 1980, 255:401-407.
11. Dalgleish D.G., Law A.J.R. pH-induced dissociation of bovine casein micelles. 2. Mineral solubilization and its relation to casein release. J. Dairy Res. 1989, 56:727-735.
12. Dupont D., Mandalari G., Molle D., Jardin J., Leonil J., Faulks R.M., Wickham M.S.J., Mills E.N.C., Mackie A.R. Comparative resistance of food proteins to adult and infant in vitro digestion models. Mol. Nutr. Food Res. 2010, 54:767-780.
13. Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 1967, 6:1948-1954.
14. FitzGerald R.J., Meisel H. Milk protein-derived peptide inhibitors of angiotensin-I-converting enzyme. Br. J. Nutr. 2000, 84(Suppl. 1):S33-37.
15. Gallinat J.L., Qanbari S., Drögemüller C., Pimentel E.C.G., Thaller G., Tetens J. DNA-based identification of novel bovine casein gene variants. J. Dairy Sci. 2013, 96:699-709.
16. Garnier J., Ribadeau-Dumas B., Mocquot G. A new method for the preparation of an immunologically homogeneous β-casein. J. Dairy Res. 1964, 31:131-136.
17. Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino-acid sequence data. Anal. Biochem. 1989, 182:319-326.
18. Gómez-Ruiz J.A., Lopez-Exposito I., Pihlanto A., Ramos M., Recio I. Antioxidant activity of ovine casein hydrolysates: Identification of active peptides by HPLC-MS/MS. Eur. Food Res. Technol. 2008, 227:1061-1067.
19. Halliwell B. Oxidative stress and cancer: Have we moved forward?. Biochem. J. 2007, 401:1-11.
20. Hipp N.J., Groves M.L., Custer J.H., McMeekin T.L. Separation of α-, β- and γ-casein. J. Dairy Sci. 1952, 35:272-281.
21. Hur S.J., Lim B.O., Decker E.A., McClements D.J. In vitro human digestion models for food applications. Food Chem. 2011, 125:1-12.
22. Imafidon G.I., Farkye N.Y., Spanier A.M. Isolation, purification, and alteration of some functional groups of major milk proteins: A review. Crit. Rev. Food Sci. Nutr. 1997, 37:663-689.
23. Jensen H.B., Holland J.W., Poulsen N.A., Larsen L.B. Milk protein genetic variants and isoforms identified in bovine milk representing extremes in coagulation properties. J. Dairy Sci. 2012, 95:2891-2903. a.
24. Jensen H.B., Poulsen N.A., Andersen K.K., Hammershoj M., Poulsen H.D., Larsen L.B. Distinct composition of bovine milk from Jersey and Holstein-Friesian cows with good, poor, or noncoagulation properties as reflected in protein genetic variants and isoforms. J. Dairy Sci. 2012, 95:6905-6917. b.
25. Jinsmaa Y., Yoshikawa M. Enzymatic release of neocasomorphin and beta-casomorphin from bovine beta-casein. Peptides 1999, 20:957-962.
26. Kalantzi L., Goumas K., Kalioras V., Abrahamsson B., Dressman J.B., Reppas C. Characterization of the human upper gastrointestinal contents under conditions simulating bioavailability/bioequivalence studies. Pharm. Res. 2006, 23:165-176.
27. Kamiński S., Cieslinska A., Kostyra E. Polymorphism of bovine beta-casein and its potential effect on human health. J. Appl. Genet. 2007, 48:189-198.
28. Kang D.H., Gho Y.S., Suh M.K., Kang C.H. Highly sensitive and fast protein detection with Coomassie brilliant blue in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Bull. Korean Chem. Soc. 2002, 23:1511-1512.
29. Korhonen H., Pihlanto A. Bioactive peptides: Production and functionality. Int. Dairy J. 2006, 16:945-960.
30. Kollipara L., Zahedi R.P. Protein carbamylation: In vivo modification or in vitro artefact?. Proteomics 2013, 13:941-944.
31. Kuipers B.J.H., Gruppen H. Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214nm to enable quantitative reverse phase high-performance liquid chromatography-mass spectrometry analysis. J. Agric. Food Chem. 2007, 55:5445-5451.
32. Kumar R., Singhal V., Sangwan R.B., Mann B. Comparative studies on antioxidant activity of buffalo and cow milk casein and their hydrolysates. Milchwissenschaft 2010, 65:287-290.
33. Larsen L.B., Rasmussen M.D., Bjerring M., Nielsen J.H. Proteases and protein degradation in milk from cows infected with Streptococcus uberis. Int. Dairy J. 2004, 14:899-907.
34. Lisson M., Erhardt G. Milk protein variants and human nutrition. Ernahrungs Umschau 2011, 58:602-607.
35. Lisson M., Lochnit G., Erhardt G. Genetic variants of bovine beta- and kappa-casein result in different immunoglobulin E-binding epitopes after in vitro gastrointestinal digestion. J. Dairy Sci. 2013, 96:5532-5543.
36. Martin P., Szymanowska M., Zwierzchowski L., Leroux C. The impact of genetic polymorphisms on the protein composition of ruminant milks. Reprod. Nutr. Dev. 2002, 42:433-459.
37. Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 1987, 262:10035-10038.
38. Meisel H. Overview on milk protein-derived peptides. Int. Dairy J. 1998, 8:363-373.
39. Moon J.K., Shibamoto T. Antioxidant assays for plant and food components. J. Agric. Food Chem. 2009, 57:1655-1666.
40. Mullally M.M., O'Callaghan D.M., FitzGerald R.J., Donnelly W.J., Dalton J.P. Proteolytic and peptidolytic activities in commercial pancreatic protease preparations and their relationship to some whey protein hydrolyzate characteristics. J. Agric. Food Chem. 1994, 42:2973-2981.
41. Mun K.C., Golper T.A. Impaired biological activity of erythropoietin by cyanate carbamylation. Blood Purif. 2000, 18:13-17.
42. Nagpal R., Behare P., Rana R., Kumar A., Kumar M., Arora S., Morotta F., Jain S., Yadav H. Bioactive peptides derived from milk proteins and their health beneficial potentials: An update. Food Funct. 2011, 2:18-27.
43. O'Connell J.E., Grinberg V.Y., de Kruif C.G. Association behavior of β-casein. J. Colloid Interface Sci. 2003, 258:33-39.
44. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption-coefficient of a protein. Protein Sci. 1995, 4:2411-2423.
45. Payens T.A., van Markwijk B. Some features of association of beta-casein. Biochim. Biophys. Acta 1963, 71:517-530.
46. Phelan M., Aherne A., FitzGerald R.J., O'Brien N.M. Casein-derived bioactive peptides: Biological effects, industrial uses, safety aspects and regulatory status. Int. Dairy J. 2009, 19:643-654.
47. Pihlanto A. Antioxidative peptides derived from milk proteins. Int. Dairy J. 2006, 16:1306-1314.
48. Piper D.W., Fenton B.H. pH stability and activity curves of pepsin with special reference to their clinical importance. Gut 1965, 6:506-508.
49. Poulsen N.A., Bertelsen H.P., Jensen H.B., Gustavsson F., Glantz M., Mansson H.L., Andren A., Paulsson M., Bendixen C., Buitenhuis A.J., Larsen L.B. The occurrence of noncoagulating milk and the association of bovine milk coagulation properties with genetic variants of the caseins in 3 Scandinavian dairy breeds. J. Dairy Sci. 2013, 96:4830-4842.
50. Re R., Pellegrini N., Proteggente A., Pannala A., Yang M., Rice-Evans C. Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic. Biol. Med. 1999, 26:1231-1237.
51. Sarmadi B.H., Ismail A. Antioxidative peptides from food proteins: A review. Peptides 2010, 31:1949-1956.
52. Sentandreu M.A., Toldra F. A rapid, simple and sensitive fluorescence method for the assay of angiotensin-I converting enzyme. Food Chem. 2006, 97:546-554.
53. Shah N.P. Effects of milk-derived bioactives: An overview. Br. J. Nutr. 2000, 84(Suppl. 1):S3-10.
54. Silva S.V., Malcata F.X. Caseins as source of bioactive peptides. Int. Dairy J. 2005, 15:1-15.
55. Stark G.R. Reactions of cyanate with functional groups of proteins. 3. Reactions with amino and carboxyl groups. Biochemistry 1965, 4:1030-1036.
56. Stark G.R., Stein W.H., Moore S. Reactions of cyanate present in aqueous urea with amino acids and proteins. J. Biol. Chem. 1960, 235:3177-3181.
57. Su R., Liang M., Qi W., Liu R., Yuan S., He Z. Pancreatic hydrolysis of bovine casein: Peptide release and time-dependent reaction behavior. Food Chem. 2012, 133:851-858.
58. Udenfriend S., Stein S., Bohlen P., Dairman W. Fluorescamine-Reagent for assay of amino acids, peptides, proteins, and primary amines in picomole range. Science 1972, 178:871-872.
59. Ulleberg E.K., Comi I., Holm H., Herud E.B., Jacobsen M., Vegarud G.E. Human gastrointestinal juices intended for use in in vitro digestion models. Food Dig. 2011, 2:52-61.
60. Valko M., Leibfritz D., Moncol J., Cronin M.T.D., Mazur M., Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int. J. Biochem. Cell Biol. 2007, 39:44-84.
61. Weimann C., Meisel H., Erhardt G. Short communication: Bovine kappa-casein variants result in different angiotensin I converting enzyme (ACE) inhibitory peptides. J. Dairy Sci. 2009, 92:1885-1888.
62. Wickham M., Faulks R., Mills C. In vitro digestion methods for assessing the effect of food structure on allergen breakdown. Mol. Nutr. Food Res. 2009, 53:952-958.
63. Wu J., Aluko R.E., Nakai S. Structural requirements of angiotensin I-converting enzyme inhibitory peptides: Quantitative structure-activity relationship study of di- and tripeptides. J. Agric. Food Chem. 2006, 54:732-738.