Effect of Maillard-induced glycosylation on the nutritional quality, solubility, thermal stability and molecular configuration of whey proteinv

International Dairy Journal

Volumn 25, Issue 2, 2012, Pages 112-122

  Wang, Qian ^a   Ismail, Baraem ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLATED; HEATING TEMPERATURES; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; INTERMOLECULAR INTERACTIONS; ISOELECTRIC POINT (PI); MAILLARD REACTION; MOLECULAR CONFIGURATIONS; NUTRITIONAL QUALITIES; PHYSICO-CHEMICALS; PROTEIN CONCENTRATIONS; SULFHYDRYL GROUPS; SURFACE HYDROPHOBICITY; WHEY PROTEIN ISOLATE; WHEY PROTEINS;

DEXTRAN; ESTERIFICATION; GLYCOSYLATION; LIQUID CHROMATOGRAPHY; SOLUBILITY; THERMODYNAMIC STABILITY;

PROTEINS;

EID: 84861330638     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2012.02.009     Document Type: Article

References (38)

1. Akhtar M., Dickinson E. Whey protein-maltodextrin conjugates as emulsifying agents: an alternative to gum Arabic. Food Hydrocolloids 2007, 21:607-616.
2. Ames J.M. The Maillard reaction 1992, 99-153. Royal Society of Chemistry, London, UK. B.J.F. Hudson (Ed.).
3. Armstrong H.J., Hill S.E., Schrooyen P., Mitchell J.R. A comparison of the viscoelastic properties of conventional and Maillard protein gels. Journal of Texture Studies 1994, 25:285-298.
4. Brands C.M.J., Alink G.M., Boekel M.A., Jongen W.M.F. Mutagenicity of heated sugar-casein systems: effect of the Maillard reaction. Journal of Agricultural and Food Chemistry 2000, 48:2271-2275.
5. Canales B.K., Higgins L., Markowski T., Anderson L., Li Q.A., Monga M. Presence of five conditioning film proteins are highly associated with early stent encrustation. Journal of Endourology 2009, 23:1437-1442.
6. Chevalier F., Chobert J.M., Popineau Y., Nicolas M.G., Haertle T. Improvement of functional properties of beta-lactoglobulin glycated through the Maillard reaction is related to the nature of the sugar. International Dairy Journal 2001, 11:145-152.
7. Erbersdobler H.F., Brandt A., Scharrer E., Wangenheim B. Transport and metabolism studies with fructose amino acids. Progress in Food and Nutrition Science 1981, 5:257-263.
8. Gan C.Y., Phuah L.H., Chin E.T., AlKarkhi P.N., Abbas F.M., Easa A.M. Combined cross-linking treatments of bovine serum albumin gel beadlets for controlled-delivery of caffeine. Food Hydrocolloids 2009, 23:1398-1405.
9. Guerra-Hernandez E., Gomez C.L., Garcia-Villanova B., Sanchez N.C., Gomez J.M.R. Effect of storage on non-enzymatic browning of liquid infant milk formulae. Journal of the Science of Food and Agriculture 2002, 82:587-592.
10. Handa A., Kuroda N. Functional improvement in dried egg white through the Maillard reaction. Journal of Agricultural and Food Chemistry 1999, 47:1845-1850.
11. Haug I.J., Skar H.M., Vegarud G.E., Langsrud T., Draget K.I. Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry. Food Hydrocolloids 2009, 23:2287-2293.
12. Hiller B., Lorenzen P.C. Functional properties of milk proteins as affected by Maillard reaction induced oligomerisation. Food Research International 2010, 43:1155-1166.
13. Imetti S., Cairolo S., Gregori B.D., Bonomi F. Modifications of high-order structures upon heating of β-lactoglobulin: dependence on the protein concentration. Journal of Agricultural and Food Chemistry 1995, 43:53-58.
14. Jiménez-Castaño L., Villamiel M., López-Fandiño R. Glycosylation of individual whey proteins by Maillard reaction using dextran of different molecular mass. Food Hydrocolloids 2007, 21:433-443.
15. Jiménez-Castaño L., Villamiel M., Martin-Alvarez P.J., Olano A., López-Fandiño R. Effect of the dry-heating conditions on the glycosylation of β-lactoglobulin with dextran through the Maillard reaction. Food Hydrocolloids 2005, 19:831-837.
16. Kato Y., Nakamura K., Kitamura T., Moriyama H., Hasegawa M., Sasaki H. Separation of proteins by hydrophobic interaction chromatography at low salt concentration. Journal of Chromatography 2002, 20:143-149.
17. Krause R., Knoll K., Henle T. Studies on the formation of furosine and pyridosine during acid hydrolysis of different Amadori products of lysine. European Food Research and Technology 2003, 216:277-283.
18. Kontopidis G., Holt C., Sawyer L. β-Lactoglobulin: binding properties, structure, and function. Journal of Dairy Science 2004, 87:785-796.
19. LaClair C.E., Etzel M.R. Turbidity and protein aggregation in whey protein beverages. Journal of Food Science 2009, 74:C526-C535.
20. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
21. Leonil J., Molle D., Fauquant J., Maubois L., Pearce R.J., Bouhallab S. Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. Journal of Dairy Science 1997, 80:2270-2281.
22. Lillard J.S., Clare D.A., Daubert C.R. Glycosylation and expanded utility of a modified whey protein ingredient via carbohydrate conjugation at low pH. Journal of Dairy Science 2009, 92:135-148.
23. Losito I., Stringano E., Carulli S., Palmisano F. Correlation between lactosylation and denaturation of major whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry. Analytical and Bioanalytical Chemistry 2010, 396:2293-2306.
24. Moor C.V., Ha E.Y.W. Off-flavors of whey protein concentrates: a literature review. International Dairy Journal 1991, 1:1-11.
25. Nacka F., Chobert J.M. Induction of new physicochemical and functional properties by the glycosylation of whey proteins. Journal of Protein Chemistry 1998, 17:495-503.
26. Nicorescu I., Riaublanc A., Loisel C., Vial C., Djelveh G., Cuvelier G., et al. Impact of protein self-assemblages on foam properties. Food Research International 2009, 42:1434-1445.
27. Oliver C.M., Melton L.D., Stanley R.A. Creating proteins with novel functionality via the Maillard reaction: a review. Critical Reviews in Food Science and Nutrition 2006, 46:337-350.
28. Pelegrine D.H.G., Gasparetto C.A. Whey proteins solubility as function of temperature and pH. Food Science and Technology 2005, 38:77-80.
29. Rufian-Henares J.A., Guerra-Hernández E., García-Villanova B. Maillard reaction in enteral formula processing: furosine, loss of o-phthaldialdehyde reactivity, and fluorescence. Food Research International 2002, 35:527-533.
30. Rufian-Henares J.A., Guerra-Hernández E., García-Villanova B. Available lysine and fluorescence in heated milk proteins/dextrinomaltose or lactose solutions. Food Chemistry 2006, 98:685-692.
31. Sava N., Plancken V. The kinetics of heat-induced structural changes of β-lactoglobulin. Journal of Dairy Science 2005, 88:1646-1653.
32. Tang C.H., Li L., Yang X.Q. Influence of transglutaminase-induced cross-linking on in vitro digestibility of soy protein isolate. Journal of Food Biochemistry 2006, 30:718-731.
33. ® 2010, Microsoft, New York, NY, USA.
34. Xu D., Yuan F., Wang X., Li X., Hou Z., Gao Y.X. The effect of whey protein isolate-dextran conjugates on the freeze-thaw stability of oil-in-water emulsions. Journal of Dispersion Science and Technology 2011, 32:77-83.
35. Yang, V. C., & Langer, R. S. (1985). Rapid method for determination the isoelectric point for amphoteric molecules. United States Patent No. 4666855.
36. Ye A.T. Characterization of cold-set gels produced from heated emulsions stabilized by whey protein. International Dairy Journal 2009, 19:721-727.
37. Zhu D., Damodaran S., Lucey J. Formation of whey protein isolate (WPI)-dextran conjugates in aqueous solutions. Journal of Agricultural and Food Chemistry 2008, 56:7113-7118.
38. Zhu D., Damodaran S., Lucey J. Physicochemical and emulsifying properties of whey protein isolate (WPI)-dextran conjugates produced in aqueous solution. Journal of Agricultural and Food Chemistry 2010, 58:2988-2994.