In vitro gastric digestion of heat-induced aggregates of β-lactoglobulin

Journal of Dairy Science

Volumn 96, Issue 1, 2013, Pages 63-74

  Peram, Malleswara R ^a   Loveday, Simon M ^a   Ye, Aiqian ^a   Singh, Harjinder ^a  

^a MASSEY UNIVERSITY   (New Zealand)

Author keywords

lactoglobulin; Heat induced aggregate; In vitro gastric digestibility; Pepsin

Indexed keywords

LACTOGLOBULIN;

ANIMAL; ARTICLE; CATTLE; DIGESTION; GEL CHROMATOGRAPHY; HEAT; IN VITRO STUDY; METABOLISM; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN DEGRADATION; STOMACH;

ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; DIGESTION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HOT TEMPERATURE; LACTOGLOBULINS; MOLECULAR WEIGHT; PROTEOLYSIS; STOMACH;

EID: 84871608855     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2012-5896     Document Type: Article

References (23)

1. Chobert J.M., Briand L., Grinberg V., Haertlé T. Impact of esterification on the folding and the susceptibility to peptic proteolysis of β-lactoglobulin. Biochim. Biophys. Acta 1995, 1248:170-176.
2. Creamer L.K., Bienvenue A., Nilsson H., Paulsson M., van Wanroij M., Lowe E.K., Anema S.G., Boland M.J., Jimenez-Flores R. Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine β-lactoglobulin. J. Agric. Food Chem. 2004, 52:7660-7668.
3. Dalgalarrondo M., Dufour E., Chobert J.M., Bertrand-Harb C., Haertlé T. Proteolysis of β-lactoglobulin and β-casein by pepsin in ethanolic media. Int. Dairy J. 1995, 5:1-14.
4. Damodaran S. Amino acids, peptides, and proteins. Fennema's Food Chemistry 2007, 217-329. CRC Press, Boca Raton, FL. 4th. S. Damodaran, K.L. Parkin, O.R. Fennema (Eds.).
5. Fox P.F., McSweeney P.L.H. Chapter 7 in Advanced Dairy Chemistry 2003, 1. Part A. Kluwer Academic/Plenum Publishers, New York, NY. 3rd.
6. Guo M.R., Fox P.F., Flynn A., Kindstedt P.S. Susceptibility of β-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. J. Dairy Sci. 1995, 78:2336-2344.
7. Harwalkar V.R. Measurement of thermal denaturation of β-lactoglobulin at pH 2.5. J. Dairy Sci. 1980, 63:1043-1051.
8. Havea P., Singh H., Creamer L.K., Campanella O.H. Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions. J. Dairy Res. 1998, 65:79-91.
9. Hoffmann M.A.M., Van Mil P.J.J.M. Heat-induced aggregation of β-lactoglobulin as a function of pH. J. Agric. Food Chem. 1999, 47:1898-1905.
10. Iametti S., Cairoli S., De Gregori B., Bonomi F. Modifications of high-order structures upon heating of β-lactoglobulin: Dependence on the protein concentration. J. Agric. Food Chem. 1995, 43:53-58.
11. Iametti S., De Gregori B., Vecchio G., Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem. 1996, 237:106-112.
12. Li-Chan E.C.Y. Properties of proteins in food systems: An introduction. Proteins in Food Processing 2004, 2-26. Woodhead Publishing, Cambridge, UK. 1st. R.Y. Yada (Ed.).
13. Manderson G.A., Hardman M.J., Creamer L.K. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. J. Agric. Food Chem. 1998, 46:5052-5061.
14. McKenzie H.A. β-Lactoglobulins. Milk Proteins 1971, 257-330. Academic Press, New York, NY. H.A. McKenzie (Ed.).
15. Mills E.N.C., Sancho A.I., Rigby N.M., Jenkins J.A., Mackie A.R. Impact of food processing on the structural and allergenic properties of food allergens. Mol. Nutr. Food Res. 2009, 53:963-969.
16. Miranda G., Pelissier J.P. Kinetic studies of in vivo digestion of bovine unheated skim-milk proteins in the rat stomach. J. Dairy Res. 1983, 50:27-36.
17. Papiz M.Z., Sawyer L., Eliopoulos E.E., North A.C.T., Findlay J.B.C., Sivaprasadarao R., Jones T.A., Newcomer M.E., Kraulis P.J. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986, 324:383-385.
18. Reddy I.M., Kella N.K.D., Kinsella J.E. Structural and conformational basis of the resistance of β-lactoglobulin to peptic and chymotryptic digestion. J. Agric. Food Chem. 1988, 36:737-741.
19. Schmidt D.G., Van Markwijk B.W. Enzymatic hydrolysis of whey proteins: Influence of heat treatment of α-lactalbumin and β-lactoglobulin on their proteolysis by pepsin and papain. Neth. Milk Dairy J. 1993, 47:15-22.
20. Schokker E.P., Singh H., Pinder D.N., Norris G.E., Creamer L.K. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. Int. Dairy J. 1999, 9:791-800.
21. Thomas K., Aalbers M., Bannon G.A., Bartels M., Dearman R.J., Esdaile D.J., Fu T.J., Glatt C.M., Hadfield N., Hatzos C., Hefle S.L., Heylings J.R., Goodman R.E., Henry B., Herouet C., Holsapple M., Ladics G.S., Landry T.D., MacIntosh S.C., Rice E.A., Privalle L.S., Steiner H.Y., Teshima R., van Ree R., Woolhiser M., Zawodny J. A multi-laboratory evaluation of a common in vitro pepsin digestion assay protocol used in assessing the safety of novel proteins. Regul. Toxicol. Pharmacol. 2004, 39:87-98.
22. Xiong Y.L., Dawson K.A., Wan L. Thermal aggregation of β-lactoglobulin: Effect of pH, ionic environment and thiol reagent. J. Dairy Sci. 1993, 76:70-77.
23. Zeece M., Huppertz T., Kelly A. Effect of high-pressure treatment on in vitro digestibility of β-lactoglobulin. Innov. Food Sci. Emerg. Technol. 2008, 9:62-69.